|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-210 |
1.52e-111 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 318.53 E-value: 1.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFK 80
Cdd:COG1136 17 GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLRRRHIGFVFQFFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:COG1136 97 LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISDS 210
Cdd:COG1136 177 SKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-206 |
2.46e-98 |
|
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: 284.77 E-value: 2.46e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFK 80
Cdd:cd03255 13 GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:cd03255 93 LLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:cd03255 173 SETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-212 |
1.26e-86 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 255.36 E-value: 1.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFKLLREST 86
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:COG2884 96 VYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 167 IMNLFKSLNQQeGTTIIMVTHDPHVAEQCE-RVIKIIDGRVISDSKE 212
Cdd:COG2884 176 IMELLEEINRR-GTTVLIATHDLELVDRMPkRVLELEDGRLVRDEAR 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-210 |
4.01e-78 |
|
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: 233.87 E-value: 4.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFK 80
Cdd:COG4181 21 GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARHVGFVFQSFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGksRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:COG4181 101 LLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISDS 210
Cdd:COG4181 179 AATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDT 228
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-201 |
1.00e-74 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 224.42 E-value: 1.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLRES 85
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 227351261 166 EIMNLFKSLNqQEGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:TIGR03608 172 EVLDLLLELN-DEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-207 |
1.32e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 223.42 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFK 80
Cdd:COG1135 14 KGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR-RKIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:COG1135 93 LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:COG1135 173 PETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-207 |
5.15e-70 |
|
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: 213.60 E-value: 5.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHpihDYTRKQFSSLRN--QNVGFVFQN 78
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGT---DLTLLSGKELRKarRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:cd03258 91 FNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 159 LDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:cd03258 171 LDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-219 |
9.99e-70 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 224.60 E-value: 9.99e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFK 80
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK10535 97 LLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 161 SETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQCERVIKIIDGRVISDSKEENQRAGN 219
Cdd:PRK10535 177 SHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVA 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-188 |
9.00e-68 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 208.79 E-value: 9.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDytrkqfsslRNQNVGFVFQNFK 80
Cdd:COG1116 20 GGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---------PGPDRGVVFQEPA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LL--ResTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:COG1116 91 LLpwL--TVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGA 168
|
170 180 190
....*....|....*....|....*....|
gi 227351261 159 LDSETSQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:COG1116 169 LDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-205 |
6.66e-67 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 204.79 E-value: 6.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFKLLRE 84
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:TIGR02673 94 RTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 227351261 165 QEIMNLFKSLNQQeGTTIIMVTHDPHVAEQC-ERVIKIIDGR 205
Cdd:TIGR02673 174 ERILDLLKRLNKR-GTTVIVATHDLSLVDRVaHRVIILDDGR 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-206 |
2.41e-66 |
|
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: 203.41 E-value: 2.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFKLLRESTV 87
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 88 ADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEI 167
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 168 MNLFKSLNQQeGTTIIMVTHDPH-VAEQCERVIKIIDGRV 206
Cdd:cd03292 176 MNLLKKINKA-GTTVVVATHAKElVDTTRHRVIALERGKL 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-209 |
3.32e-66 |
|
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: 203.72 E-value: 3.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhdyTRKQFSSLRnQNVGFVFQN-----Fk 80
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR-RKVGLVFQNpddqlF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 llrESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:COG1122 90 ---APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 161 SETSQEIMNLFKSLNqQEGTTIIMVTHDP-HVAEQCERVIKIIDGRVISD 209
Cdd:COG1122 167 PRGRRELLELLKRLN-KEGKTVIIVTHDLdLVAELADRVIVLDDGRIVAD 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-207 |
1.41e-63 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 205.52 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQN-- 78
Cdd:COG1123 274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELR-RRVQMVFQDpy 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 ---FKLLresTVADNVALPL-LYAGKSRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:COG1123 353 sslNPRM---TVGDIIAEPLrLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 154 EPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:COG1123 430 EPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-206 |
7.37e-63 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 194.88 E-value: 7.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFK 80
Cdd:TIGR02211 14 GKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQFHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:TIGR02211 94 LLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:TIGR02211 174 NNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-188 |
8.96e-63 |
|
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: 194.61 E-value: 8.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDytrkqfsslRNQNVGFVFQNFK 80
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------PGPDRGYVFQQDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:cd03293 84 LLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
170 180
....*....|....*....|....*...
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:cd03293 164 ALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-206 |
3.87e-62 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 193.46 E-value: 3.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFK 80
Cdd:PRK10584 19 GEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK10584 99 LIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-205 |
7.13e-62 |
|
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: 191.91 E-value: 7.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNFKL-LRES 85
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPDDqFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03225 92 TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 227351261 166 EIMNLFKSLNQQeGTTIIMVTHDPH-VAEQCERVIKIIDGR 205
Cdd:cd03225 172 ELLELLKKLKAE-GKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-213 |
2.33e-61 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 191.73 E-value: 2.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLI-NIIGFLDDDfEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFKLLRE 84
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLkLIIGLLRPD-SGEILVDGQDITGLSEKELYELR-RRIGMLFQGGALFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLL-YAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:COG1127 97 LTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPIT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 164 SQEIMNLFKSLNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVI-SDSKEE 213
Cdd:COG1127 177 SAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIaEGTPEE 228
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
1-206 |
3.43e-61 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 190.62 E-value: 3.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFK 80
Cdd:TIGR02982 14 GSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR-RRIGYIFQAHN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPL-LYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:TIGR02982 93 LLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 160 DSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:TIGR02982 173 DSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
7-205 |
7.58e-61 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 189.54 E-value: 7.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLREST 86
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:NF038007 100 IFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARA 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 227351261 167 IMNLFKSLNQQeGTTIIMVTHDPHVAEQCERVIKIIDGR 205
Cdd:NF038007 180 VLQQLKYINQK-GTTIIMVTHSDEASTYGNRIINMKDGK 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-207 |
1.85e-60 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 189.25 E-value: 1.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNqNVGFVFQNFKLLRES 85
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR-RMGMLFQSGALFDSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGK-SRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:cd03261 93 TVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 165 QEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:cd03261 173 GVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIV 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-207 |
3.62e-60 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 188.66 E-value: 3.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDyTRKQFSSLRnQNVGFVFQNFKLLRE 84
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLR-RKVGMVFQQFNLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYA-GKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:COG1126 92 LTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPEL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 164 SQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:COG1126 172 VGEVLDVMRDL-AKEGMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-209 |
6.78e-60 |
|
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: 188.09 E-value: 6.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFsslrNQNVGFVFQN-- 78
Cdd:COG1124 14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF----RRRVQMVFQDpy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 -----FKllresTVADNVALPLLYAGksRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:COG1124 90 aslhpRH-----TVDRILAEPLRIHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:COG1124 163 DEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEE 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-207 |
2.05e-59 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 190.01 E-value: 2.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFK 80
Cdd:PRK11153 14 GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-RQIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK11153 93 LLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:PRK11153 173 PATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-209 |
2.69e-59 |
|
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: 186.62 E-value: 2.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQnVGFVFQNFKLLRE 84
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ-IGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLL---------YAGKSRKEINgRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:cd03256 93 LSVLENVLSGRLgrrstwrslFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 156 TGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRVISD 209
Cdd:cd03256 172 VASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRIVFD 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-207 |
6.13e-59 |
|
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: 185.02 E-value: 6.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQnVGFVFQNfk 80
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKE-IQMVFQD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 lLRES-----TVADNVALPLLYAGKSRKE--INGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:cd03257 91 -PMSSlnprmTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:cd03257 170 DEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-209 |
1.37e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.88 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFKLLR 83
Cdd:COG3638 15 GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLR-RRIGMIFQQFNLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLL-YAGK--------SRKEINgRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:COG3638 94 RLSVLTNVLAGRLgRTSTwrsllglfPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 155 PTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:COG3638 173 PVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVVFD 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-206 |
1.64e-57 |
|
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: 180.80 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDyTRKQFSSLRnQNVGFVFQNFKLLRE 84
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR-QKVGMVFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYA-GKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:cd03262 91 LTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 164 SQEIMNLFKSLnQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRV 206
Cdd:cd03262 171 VGEVLDVMKDL-AEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-206 |
2.79e-57 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 181.17 E-value: 2.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLREST 86
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 167 IMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-189 |
3.95e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 184.53 E-value: 3.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHD---YTRkqfsslrnqNVGFVFQNFK 80
Cdd:COG3842 18 VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIaGFETPD-SGRILLDGRDVTGlppEKR---------NVGMVFQDYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:COG3842 88 LFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
170 180
....*....|....*....|....*....
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDP 189
Cdd:COG3842 168 AKLREEMREELRRLQRELGITFIYVTHDQ 196
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-209 |
1.69e-56 |
|
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: 180.34 E-value: 1.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQN-----F 79
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQFpehqlF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 kllrESTVADNVALPLLYAGKSRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:TIGR04521 97 ----EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 159 LDSETSQEIMNLFKSLNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISD 209
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLD 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-213 |
2.12e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 182.27 E-value: 2.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDD-----FEGTYFYQDHPIHDytrkqfsslRNqnVGFVFQ 77
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaGLETPDsgrivLNGRDLFTNLPPRE---------RR--VGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 78 NFKLLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 158 ALDSETSQEIM-NLFKSLNQQEGTTIImVTHDPHVA-EQCERVIKIIDGRVI-SDSKEE 213
Cdd:COG1118 163 ALDAKVRKELRrWLRRLHDELGGTTVF-VTHDQEEAlELADRVVVMNQGRIEqVGTPDE 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-199 |
2.36e-55 |
|
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: 178.71 E-value: 2.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDD--FEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQN--- 78
Cdd:COG0444 18 VKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKELRKIRGREIQMIFQDpmt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 -----FkllresTVADNVALPLLYAGK-SRKEINGRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIARAISTHPQF 149
Cdd:COG0444 98 slnpvM------TVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 150 LIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVI 199
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVA 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-207 |
2.59e-55 |
|
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: 175.40 E-value: 2.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQfsslrnQNVGFVFQNFKLLRE 84
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaGLERPD-SGEILIDGRDVTGVPPER------RNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 165 QEIMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRVI 207
Cdd:cd03259 167 EELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRIV 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-213 |
7.85e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 174.87 E-value: 7.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIhdytRKQFSSLRnQNVGFVFQNFKLL 82
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlGLLRPT-SGEVRVLGEDV----ARDPAEVR-RRIGYVPQEPALY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:COG1131 86 PDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 163 TSQEIMNLFKSLNqQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI-SDSKEE 213
Cdd:COG1131 166 ARRELWELLRELA-AEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVaDGTPDE 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-209 |
1.27e-53 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 179.33 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDD--DFEGTYFYQDHPIHDYTRKqfssLRNQNVGFVFQ 77
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHggRISGEVLLDGRDLLELSEA----LRGRRIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 78 NFKL-LRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:COG1123 91 DPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 157 GALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVISD 209
Cdd:COG1123 171 TALDVTTQAEILDLLRELQRERGTTVLLITHDLGvVAEIADRVVVMDDGRIVED 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-188 |
1.47e-52 |
|
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: 168.95 E-value: 1.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHD---YTRkqfsslrnqNVGFVFQNFKL 81
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKR---------PVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:cd03300 84 FPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180
....*....|....*....|....*..
gi 227351261 162 ETSQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:cd03300 164 KLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-207 |
7.38e-52 |
|
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: 166.97 E-value: 7.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDF-----EGTYFYQDHPIHDYtRKQFSSLRNQnVGFVFQNF 79
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDL-DVDVLELRRR-VGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLREStVADNVALPLLYAG-KSRKEINGRVSETLKQVGLAGYE--EQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:cd03260 91 NPFPGS-IYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 157 GALDSETSQEIMNLFKSLNQQegTTIIMVTHDPHVAEQC-ERVIKIIDGRVI 207
Cdd:cd03260 170 SALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLV 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-207 |
1.98e-51 |
|
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: 166.36 E-value: 1.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHpihDYTRKqfsSLRNQNVGFVFQNFKLLR 83
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATDV---PVQERNVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGKSRK----EINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:cd03296 88 HMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 227351261 160 DSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRVI 207
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIE 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-206 |
3.04e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.99 E-value: 3.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYT----RKQfsslrnqnVGFVFQNFKLL 82
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppewRRQ--------VAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 REsTVADNVALPLLYAGKSRKEinGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:COG4619 87 GG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 227351261 162 ETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRV 206
Cdd:COG4619 164 ENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-211 |
6.07e-51 |
|
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: 165.16 E-value: 6.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNFKLLRES 85
Cdd:TIGR02315 16 QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR-RRIGMIFQHYNLIERL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSE--------TLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:TIGR02315 95 TVLENVLHGRLGYKPTWRSLLGRFSEedkeralsALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 158 ALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRVISDSK 211
Cdd:TIGR02315 175 SLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEIVFDGA 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-207 |
2.99e-50 |
|
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: 164.35 E-value: 2.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLRESTV 87
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 88 ADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEI 167
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 227351261 168 MNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKII-DGRVI 207
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMkDGRLV 240
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-189 |
7.40e-50 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 165.63 E-value: 7.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfsslRNqnVGFVFQNFKLLRE 84
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----RN--IAMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD---- 160
Cdd:COG3839 90 MTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklr 169
|
170 180
....*....|....*....|....*....
gi 227351261 161 SETSQEIMNLFKSLnqqeGTTIIMVTHDP 189
Cdd:COG3839 170 VEMRAEIKRLHRRL----GTTTIYVTHDQ 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
7-213 |
1.02e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 162.18 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDytrkqfsslRNQNVGFVFQNFKLLRE- 84
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlGLLPPT-SGTVRLFGKPPRR---------ARRRIGYVPQRAEVDWDf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 -STVADNVALPLLYA----GKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:COG1121 91 pITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 160 DSETSQEIMNLFKSLNqQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVISDSKEE 213
Cdd:COG1121 171 DAATEEALYELLRELR-REGKTILVVTHDLGaVREYFDRVLLLNRGLVAHGPPEE 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-205 |
1.19e-49 |
|
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: 159.66 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRkqFSSLRNQNVGFVFQNFKLLRES 85
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED--ELPPLRRRIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLlyagksrkeingrvsetlkqvglagyeeqlpknmSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03229 92 TVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 227351261 166 EIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGR 205
Cdd:cd03229 138 EVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-209 |
3.04e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 160.64 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 2 SQRF---HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDyTRKQFSSLRnQNVGFVFQN 78
Cdd:PRK09493 8 SKHFgptQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIR-QEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLRESTVADNVAL-PLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:PRK09493 86 FYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 158 ALDSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQC-ERVIKIIDGRVISD 209
Cdd:PRK09493 166 ALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAED 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-188 |
8.12e-49 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 160.41 E-value: 8.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIH--DYTRkqfsslrnqnvGFVFQ 77
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIaGFLAPS-SGEITLDGVPVTgpGADR-----------GVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 78 NFKLLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190
....*....|....*....|....*....|.
gi 227351261 158 ALDSETSQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-209 |
1.51e-48 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 159.44 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNFKLLRES 85
Cdd:COG1120 16 VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLLKPS-SGEVLLDGRDLASLSRRELA----RRIAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVAL---PLL--YAGKSRKEINgRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:COG1120 91 TVRELVALgryPHLglFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDP-HVAEQCERVIKIIDGRVISD 209
Cdd:COG1120 170 LAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQ 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-207 |
3.92e-48 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 158.37 E-value: 3.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 3 QRFH---VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhDYTR---KQFSSLRN--QNVGF 74
Cdd:PRK11264 11 KKFHgqtVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI-DTARslsQQKGLIRQlrQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 75 VFQNFKLLRESTVADNVAL-PLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:PRK11264 90 VFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 154 EPTGALDSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRVI 207
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQL-AQEKRTMVIVTHEMSFArDVADRAIFMDQGRIV 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-213 |
6.38e-48 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 166.93 E-value: 6.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRkqfSSLRNQnVGFVFQNFKLLrES 85
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlGLYEPT-SGRILIDGIDLRQIDP---ASLRRQ-IGVVLQDVFLF-SG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALpllyagkSRKEIN-GRVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:COG2274 564 TIRENITL-------GDPDATdEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227351261 154 EPTGALDSETSQEIMNLFKSLNQqeGTTIIMVTHDPHVAEQCERVIKIIDGRVISD-SKEE 213
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDgTHEE 695
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-213 |
2.83e-47 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 155.73 E-value: 2.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHpihDYTRKqfsSLRNQNVGFVFQNFKLLR 83
Cdd:TIGR00968 12 SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ---DATRV---HARDRKIGFVFQHYALFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:TIGR00968 86 HLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 164 SQEIMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRVIS-DSKEE 213
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAmEVADRIVVMSNGKIEQiGSPDE 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-211 |
9.38e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 155.28 E-value: 9.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLI-NIIGFLDDDfEGTYFyqdhpIHDYTRKQFSSLRN--QNVGFVFQN----F 79
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAkLLNGLLLPT-SGKVT-----VDGLDTLDEENLWEirKKVGMVFQNpdnqF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KllrESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:TIGR04520 91 V---GATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSML 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 160 DSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISDSK 211
Cdd:TIGR04520 168 DPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-205 |
1.15e-46 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 151.77 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKqfsSLRnQNVGFVFQNFKLLrES 85
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLlRLYDPT-SGEILIDGVDLRDLDLE---SLR-KNIAYVPQDPFLF-SG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNValpllyagksrkeingrvsetlkqvglagyeeqlpknMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03228 91 TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 166 EIMNLFKSLnqQEGTTIIMVTHDPHVAEQCERVIKIIDGR 205
Cdd:cd03228 134 LILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-207 |
3.55e-46 |
|
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: 160.31 E-value: 3.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 3 QRFHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRkqfSSLRNQnVGFVFQNFKL 81
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlGFLPPY-SGSILINGVDLSDLDP---ASWRRQ-IAWVPQNPYL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LrESTVADNVALpllyaGK---SRKEINgrvsETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHP 147
Cdd:COG4988 423 F-AGTIRENLRL-----GRpdaSDEELE----AALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 148 QFLIADEPTGALDSETSQEIMNLFKSLNQqeGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIV 550
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-207 |
8.34e-46 |
|
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: 151.15 E-value: 8.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDfEGTYFYQDHPIHDyTRKQfsslrnqnVGFVFQNFKLLRE 84
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLKPT-SGSIRVFGKPLEK-ERKR--------IGYVPQRRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 S--TVADNVALPLL-------YAGKSRKEingRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:cd03235 83 FpiSVRDVVLMGLYghkglfrRLSKADKA---KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 156 TGALDSETSQEIMNLFKSLNqQEGTTIIMVTHDPH-VAEQCERVIkIIDGRVI 207
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGlVLEYFDRVL-LLNRTVV 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-207 |
1.33e-45 |
|
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: 158.78 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQfssLRnQNVGFVFQNFKLLReS 85
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLDPQ-SGSITLGGVDLRDLDEDD---LR-RRIAVVPQRPHLFD-T 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNvalpLLYAgksRKEIN-GRVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:COG4987 424 TLREN----LRLA---RPDATdEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 154 EPTGALDSETSQEIMNLFksLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:COG4987 497 EPTEGLDAATEQALLADL--LEALAGRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-206 |
1.45e-45 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 150.80 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQnVGFVFQNFKLLRESTV 87
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 88 ADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEI 167
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 168 MNLFKSLNQQeGTTIIMVTHDPH-VAEQCERVIKIIDGRV 206
Cdd:PRK10908 177 LRLFEEFNRV-GVTVLMATHDIGlISRRSYRMLTLSDGHL 215
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-188 |
1.83e-45 |
|
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: 154.42 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTyFYQDHpiHDYTRKQfSSLRNqnVGFVFQNFKLLR 83
Cdd:TIGR03265 16 AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGT-IYQGG--RDITRLP-PQKRD--YGIVFQSYALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:TIGR03265 90 NLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARV 169
|
170 180
....*....|....*....|....*
gi 227351261 164 SQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:TIGR03265 170 REHLRTEIRQLQRRLGVTTIMVTHD 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
8-156 |
2.34e-45 |
|
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: 147.79 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFsslrNQNVGFVFQNFKLLREST 86
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIaGLLSPT-EGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQL----PKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-209 |
2.92e-45 |
|
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: 150.96 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPI-----HDYTRKqfsslrnqnvGFV--F 76
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFYRPT-SGRILFDGRDItglppHRIARL----------GIArtF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 77 QNFKLLRESTVADNVALPLLY---------------AGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIAR 141
Cdd:COG0411 86 QNPRLFPELTVLENVLVAAHArlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 142 AISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVISD 209
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDlVMGLADRIVVLDFGRVIAE 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-207 |
2.22e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.71 E-value: 2.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKqfsSLRNQnVGFVFQNFKLLREs 85
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLlRFYDPT-SGRILIDGVDIRDLTLE---SLRRQ-IGVVPQDTFLFSG- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAgkSRKEINgrvsETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:COG1132 429 TIRENIRYGRPDA--TDEEVE----EAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 155 PTGALDSETSQEImnlFKSLNQ-QEGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:COG1132 503 ATSALDTETEALI---QEALERlMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-188 |
2.94e-44 |
|
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: 147.83 E-value: 2.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfssLRnQNVGFVFQNFKLLR 83
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR-RKIGYVIQQIGLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGKSRKEINGRVSETLKQVGL--AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:cd03295 89 HMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDP 168
|
170 180
....*....|....*....|....*..
gi 227351261 162 ETSQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:cd03295 169 ITRDQLQEEFKRLQQELGKTIVFVTHD 195
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-209 |
3.56e-44 |
|
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: 147.58 E-value: 3.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIhdyTRKQFSSLRNQNVGFVFQNFKLLR 83
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFLRPT-SGSVLFDGEDI---TGLPPHEIARLGIGRTFQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAG----------KSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:cd03219 89 ELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 154 EPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHDPH-VAEQCERVIKIIDGRVISD 209
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDvVMSLADRVTVLDQGRVIAE 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-206 |
5.81e-44 |
|
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: 146.25 E-value: 5.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfsslrnQNVGFVFQNFKLLRE 84
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD------RDIAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 227351261 165 QEIMNLFKSLNQQEGTTIIMVTHDphvaeQCE------RVIKIIDGRV 206
Cdd:cd03301 167 VQMRAELKRLQQRLGTTTIYVTHD-----QVEamtmadRIAVMNDGQI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-209 |
1.51e-43 |
|
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: 144.12 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNfkllres 85
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLaGLLKPS-SGEILLDGKDLASLSPKELA----RKIAYVPQA------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 tvadnvalpllyagksrkeingrvsetLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03214 82 ---------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 166 EIMNLFKSLNQQEGTTIIMVTHDP-HVAEQCERVIKIIDGRVISD 209
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQ 179
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-199 |
1.81e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 149.08 E-value: 1.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHpihDYTRkqfSSLRNQNVGFVFQNFKLLR 83
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSR---LHARDRKVGFVFQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGK----SRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:PRK10851 88 HMTVFDNIAFGLTVLPRrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 227351261 160 DSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVI 199
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAmEVADRVV 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-207 |
1.84e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 145.93 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhDYTR----KQFSSLRnQNVGFVFQNFK 80
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQkpseKAIRLLR-QKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADN-VALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:COG4161 93 LWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 227351261 160 DSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:COG4161 173 DPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-209 |
4.55e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 144.51 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHvlhdINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHD---YTRKqFSSLrnqnvgfvF 76
Cdd:COG3840 12 GDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIaGFLPPD-SGRILWNGQDLTAlppAERP-VSML--------F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 77 QNFKLLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 157 GALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAAD 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-207 |
7.21e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 144.39 E-value: 7.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhDYTR----KQFSSLRnQNVGFVFQNFKLL 82
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKtpsdKAIRELR-RNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADN-VALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:PRK11124 95 PHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 162 ETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:PRK11124 175 EITAQIVSIIREL-AETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-188 |
1.39e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 144.17 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIH------------DytRKQFSSLRnQNVG 73
Cdd:COG4598 22 EVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpaD--RRQLQRIR-TRLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 74 FVFQNFKLLRESTVADNVAL-PLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:COG4598 99 MVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLnQQEGTTIIMVTHD 188
Cdd:COG4598 179 DEPTSALDPELVGEVLKVMRDL-AEEGRTMLVVTHE 213
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-188 |
7.88e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 143.69 E-value: 7.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfssLRnQNVGFVFQNFKLLREST 86
Cdd:COG1125 17 AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LR-RRIGYVIQQIGLFPHMT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVAL-PLLyAGKSRKEINGRVSETLKQVGL--AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:COG1125 93 VAENIATvPRL-LGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPIT 171
|
170 180
....*....|....*....|....*
gi 227351261 164 SQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:COG1125 172 REQLQDELLRLQRELGKTIVFVTHD 196
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-206 |
1.64e-41 |
|
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: 138.68 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQfsslrNQNVGFVFQNFKLL 82
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlGLLKPD-SGEIKVLGKDIKKEPEEV-----KRRIGYLPEEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVALpllyagksrkeingrvsetlkqvglagyeeqlpknmSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:cd03230 86 ENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 163 TSQEIMNLFKSLNqQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRV 206
Cdd:cd03230 130 SRREFWELLRELK-KEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-187 |
2.65e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.94 E-value: 2.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTL---INIIGFLDDDF--EGTYFYQDHPIHDYTRKQfSSLRnQNVGFVFQN- 78
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLlrcLNRMNDLIPGArvEGEILLDGEDIYDPDVDV-VELR-RRVGMVFQKp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 --FKLlresTVADNVALPLLYAG-KSRKEINGRVSETLKQVGLagYEE---QLPKN---MSGGQQQRVSIARAISTHPQF 149
Cdd:COG1117 102 npFPK----SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAAL--WDEvkdRLKKSalgLSGGQQQRLCIARALAVEPEV 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 227351261 150 LIADEPTGALDSETSQEIMNLFKSLNQQegTTIIMVTH 187
Cdd:COG1117 176 LLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTH 211
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-214 |
3.88e-41 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 140.12 E-value: 3.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDD-----DFEGTYFYQDHPIHDYTRKQFSsLRnQNVGFVFQNF 79
Cdd:TIGR00972 14 KEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDKKIDVVE-LR-RRVGMVFQKP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLREStVADNVAL-PLLYAGKSRKEINGRVSETLKQVGLagYEE---QLPKN---MSGGQQQRVSIARAISTHPQFLIA 152
Cdd:TIGR00972 92 NPFPMS-IYDNIAYgPRLHGIKDKKELDEIVEESLKKAAL--WDEvkdRLHDSalgLSGGQQQRLCIARALAVEPEVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQegTTIIMVTHDPHVAEQC-ERVIKIIDGRVISDSKEEN 214
Cdd:TIGR00972 169 DEPTSALDPIATGKIEELIQELKKK--YTIVIVTHNMQQAARIsDRTAFFYDGELVEYGPTEQ 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-211 |
2.49e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 139.84 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGT--YFYQDHPIHDYTR-------------------KQ 63
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTieWIFKDEKNKKKTKekekvleklviqktrfkkiKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 64 FSSLRNQnVGFVFQ--NFKLLrESTVADNVALPLLYAGKSRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIA 140
Cdd:PRK13651 100 IKEIRRR-VGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351261 141 RAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSK 211
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-205 |
3.27e-40 |
|
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: 135.06 E-value: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfssLRNQnVGFVFQnfkllres 85
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRR-IGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 tvadnvalpllyagksrkeingrvsetlkqvglagyeeqlpknMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd00267 81 -------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 227351261 166 EIMNLFKSLNQQeGTTIIMVTHDPHVAEQ-CERVIKIIDGR 205
Cdd:cd00267 118 RLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-198 |
4.96e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.07 E-value: 4.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDytrkQFSSLRnQNVGFVFQNFKLLREST 86
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD----AREDYR-RRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEIngRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:COG4133 92 VRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180 190
....*....|....*....|....*....|..
gi 227351261 167 IMNLFKSLNQQeGTTIIMVTHDPHVAEQCERV 198
Cdd:COG4133 170 LAELIAAHLAR-GGAVLLTTHQPLELAAARVL 200
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-208 |
5.44e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 137.90 E-value: 5.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTL-INIIGFLDDDfEGTYFYQDHPIhDYTRKQFSSLRnQNVGFVFQNF-KLLRE 84
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILKPT-SGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNPdDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:PRK13639 94 PTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 165 QEIMNLFKSLNqQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVIS 208
Cdd:PRK13639 174 SQIMKLLYDLN-KEGITIIISTHDVDlVPVYADKVYVMSDGKIIK 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-206 |
9.68e-40 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 136.73 E-value: 9.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 2 SQRFH---VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIH---DYTRkqfsslrnqnvgFV 75
Cdd:PRK11247 19 SKRYGertVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAearEDTR------------LM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 76 FQNFKLLRESTVADNVALPLlyAGKSRKeingRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL--KGQWRD----AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 156 TGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDphVAEQ---CERVIKIIDGRV 206
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHD--VSEAvamADRVLLIEEGKI 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-207 |
1.11e-39 |
|
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: 142.52 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTL----INIIgflddDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQN- 78
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLR-RRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLreS---TVADNVALPL--LYAGKSRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:COG4172 372 FGSL--SprmTVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVV 505
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-208 |
1.44e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 137.07 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLI-NIIGFLDDDfEGTYFYQDHPIHDYT----RKQfsslrnqnVGFVFQN---- 78
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLLLPE-AGTITVGGMVLSEETvwdvRRQ--------VGMVFQNpdnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKllrESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:PRK13635 94 FV---GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 159 LDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVIS 208
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-207 |
2.08e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 136.72 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDyTRKQFSSLRNQnVGFVFQ--NFKLLrES 85
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKK-VGLVFQypEYQLF-EE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLA--GYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 164 SQEIMNLFKSLNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-188 |
2.11e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 135.98 E-value: 2.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLdddfegtyFYQDHPIHdytrkqfssLRNQNV-------GFVFQN 78
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIaGFV--------PYQHGSIT---------LDGKPVegpgaerGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|
gi 227351261 159 LDSETSQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-207 |
3.29e-39 |
|
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: 140.98 E-value: 3.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKS-TLINIIGFLDDDF---EGTYFYQDHPIHDYTRKQFSSLRNQNVGFVF 76
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSERELRRIRGNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 77 QnfkllrES--------TVADNVALPL-LYAGKSRKEINGRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIARAIS 144
Cdd:COG4172 99 Q------EPmtslnplhTIGKQIAEVLrLHRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRVMIAMALA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227351261 145 THPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVI 207
Cdd:COG4172 173 NEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGvVRRFADRVAVMRQGEIV 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-209 |
7.86e-39 |
|
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: 133.00 E-value: 7.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDFEGTYfyqdhpIH--DYTrkqFSSLRNQNVGFVFQNFKLLREST 86
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIaGFETPQSGRVL------INgvDVT---AAPPADRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:cd03298 87 VEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 167 IMNLFKSLNQQEGTTIIMVTHDPHVAEQC-ERVIKIIDGRVISD 209
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQ 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-210 |
1.95e-38 |
|
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: 132.03 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 9 HDINIEID-QGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLRESTV 87
Cdd:cd03297 13 FTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 88 ADNVALPLlyAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEI 167
Cdd:cd03297 93 RENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 168 MNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISDS 210
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
10-199 |
1.33e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.93 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQN-FKLL--REsT 86
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQDpYASLnpRM-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAG-KSRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD-SET 163
Cdd:COG4608 114 VGDIIAEPLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvSIQ 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 164 SQeIMNLFKSLNQQEGTTIIMVTHD----PHVaeqCERVI 199
Cdd:COG4608 194 AQ-VLNLLEDLQDELGLTYLFISHDlsvvRHI---SDRVA 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-206 |
3.80e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.15 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfsslrnQNVGFVFQNFKLLREST 86
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN------RHVNTVFQSYALFPHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:PRK09452 103 VFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 227351261 167 IMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRV 206
Cdd:PRK09452 183 MQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
8-188 |
6.47e-37 |
|
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: 128.74 E-value: 6.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFsslrnqnvgFVFQNFKLLRESTV 87
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 88 ADNVALPL--LYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 227351261 166 EIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHD 174
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-214 |
9.99e-37 |
|
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: 128.61 E-value: 9.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYtrkqfsSLRNQNVGFVFQNFKLLRES 85
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIaGFIKPD-SGKILLNGKDITNL------PPEKRDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 166 EIMNLFKSLNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEEN 214
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-209 |
1.21e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 129.04 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQNF- 79
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR-RDIQMVFQDSi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 -KLLRESTVADNVALPLLY-AGKSRKEINGRVSETLKQVGLA-GYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:PRK10419 100 sAVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 157 GALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVET 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-187 |
1.44e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 129.37 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTR-KQFSSLRnQNVGFVFQnF--KLLRE 84
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnKKLKPLR-KKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAgyEEQL---PKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP--EELLarsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180
....*....|....*....|....*.
gi 227351261 162 ETSQEIMNLFKSLNQQEGTTIIMVTH 187
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
5-212 |
2.05e-36 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 130.58 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHvLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQfsslrnQNVGFVFQNFKLLR 83
Cdd:NF040840 14 FK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIaGIWPPD-SGKIYLDGKDITNLPPEK------RGIAYVYQNYMLFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:NF040840 86 HKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 164 SQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRV--ISDSKE 212
Cdd:NF040840 166 RDELIREMKRWHREFGFTAIHVTHNFEEALSlADRVGIMLNGRLsqVGDVRE 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-201 |
3.18e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 126.44 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDF--EGTYFYQDHPIHDYTRKQfsslrnQNVGFVFQNFKLLRE 84
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAFsaSGEVLLNGRRLTALPAEQ------RRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNV--ALPLLYAGKSRKEingRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:COG4136 91 LSVGENLafALPPTIGRAQRRA---RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 227351261 163 TSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:COG4136 168 LRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-209 |
8.31e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.29 E-value: 8.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHdytrkqFSSLR---NQNVGFVFQNFKL 81
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILsGVYQPD-SGEILLDGEPVR------FRSPRdaqAAGIAIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LRESTVADNVALPLLYAGK---SRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:COG1129 91 VPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 159 LdseTSQEIMNLFKSLNQ--QEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISD 209
Cdd:COG1129 171 L---TEREVERLFRIIRRlkAQGVAIIYISHRlDEVFEIADRVTVLRDGRLVGT 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-209 |
1.12e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 127.13 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDytRKQFSSLRNqNVGFVFQN-FKLLRES 85
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD--EENLWDIRN-KAGMVFQNpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:PRK13633 102 IVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 166 EIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISD 209
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-207 |
1.80e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 126.50 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhDYTRKQFSSLRnQNVGFVFQN-FKLLRE 84
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR-ESVGMVFQDpDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 165 QEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVI 207
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDiVPLYCDNVFVMKEGRVI 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-199 |
6.70e-35 |
|
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: 129.33 E-value: 6.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKqfsSLRNQnVGFVFQNFKLLrES 85
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLlGFVDPT-EGSIAVNGVPLADADAD---SWRDQ-IAWVPQHPFLF-AG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAgkSRKEIngrvSETLKQVGLAGYEEQLPKN-----------MSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:TIGR02857 411 TIAENIRLARPDA--SDAEI----REALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 155 PTGALDSETSQEIMNLFKSLNQqeGTTIIMVTHDPHVAEQCERVI 199
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIV 527
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-208 |
6.74e-35 |
|
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: 123.49 E-value: 6.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKqfsSLRNQnVGFVFQNFKLLRe 84
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLmRFYDPQ-KGQILIDGIDIRDISRK---SLRSM-IGVVLQDTFLFS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAgkSRKEINgrvsETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:cd03254 91 GTIMENIRLGRPNA--TDEEVI----EAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 154 EPTGALDSETSQEIMNLFKSLnqQEGTTIIMVTHDPHVAEQCERVIKIIDGRVIS 208
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
9-207 |
7.04e-35 |
|
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: 123.63 E-value: 7.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 9 HDINIEIDQGELVAIIGESGSGKS-TLINIIGFLDDDF---EGTYFYQDHPIHDytrkqfSSLRNQNVGFVFQN----FK 80
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPGLtqtSGEILLDGRPLLP------LSIRGRHIATIMQNprtaFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLResTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:TIGR02770 77 PLF--TMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 158 ALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHV-AEQCERVIKIIDGRVI 207
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVvARIADEVAVMDDGRIV 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-188 |
7.61e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 124.31 E-value: 7.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIH----------DYTRKQFSSLRNQnVGFVF 76
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTR-LTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 77 QNFKLLRESTVADNV-ALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQ-LPKNMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190
....*....|....*....|....*....|....
gi 227351261 155 PTGALDSETSQEIMNLFKSLnQQEGTTIIMVTHD 188
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHE 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-207 |
3.40e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 3.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHdytrkqfSSLRNQNVGFVFQN--FKLLRE 84
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQDvdYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 StvadnVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:cd03226 88 S-----VREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 165 QEIMNLFKSLnQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVI 207
Cdd:cd03226 163 ERVGELIREL-AAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-205 |
3.68e-34 |
|
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: 121.39 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINII--GFLDDDFEGTYFYQDHPIhDYTR---KQFSSLRNQNVGFV 75
Cdd:COG4778 20 GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLPDSGSILVRHDGGWV-DLAQaspREILALRRRTIGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 76 FQNFKLL-RESTVaDNVALPLLYAGKSRKEINGRVSETLKQVGLagyEEQL----PKNMSGGQQQRVSIARAISTHPQFL 150
Cdd:COG4778 99 SQFLRVIpRVSAL-DVVAEPLLERGVDREEARARARELLARLNL---PERLwdlpPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 151 IADEPTGALDSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGR 205
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-207 |
4.45e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 126.68 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHdytrkqFSSLR---NQNVGFVFQNFK 80
Cdd:COG3845 18 VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILyGLYQPD-SGEILIDGKPVR------IRSPRdaiALGIGMVHQHFM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVAL---PLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:COG3845 91 LVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 158 ALdseTSQEIMNLFKSLNQ--QEGTTIIMVTHDPH-VAEQCERVIKIIDGRVI 207
Cdd:COG3845 171 VL---TPQEADELFEILRRlaAEGKSIIFITHKLReVMAIADRVTVLRRGKVV 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-188 |
5.21e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.06 E-value: 5.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHpihDYTRkqfSSLRNQNVGFVFQNFKLLREST 86
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTH---RSIQQRDICMVFQSYALFPHMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:PRK11432 95 LGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180
....*....|....*....|..
gi 227351261 167 IMNLFKSLNQQEGTTIIMVTHD 188
Cdd:PRK11432 175 MREKIRELQQQFNITSLYVTHD 196
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
23-213 |
1.19e-33 |
|
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: 122.60 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 23 IIGESGSGKSTLINII-GFLDDDFEGTYFYQDHPIHdytrkqfSSLRNQNVGFVFQNFKLLRESTVADNVALPLLYAGKS 101
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLaGFEQPDSGSIMLDGEDVTN-------VPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 102 RKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTT 181
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180 190
....*....|....*....|....*....|...
gi 227351261 182 IIMVTHDPHVA-EQCERVIKIIDGRVISDSKEE 213
Cdd:TIGR01187 154 FVFVTHDQEEAmTMSDRIAIMRKGKIAQIGTPE 186
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-209 |
1.77e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.61 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFSSLR---NQN--VGFVFqnfk 80
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGELTPS-SGEVRLNGRPLAAWSPWELARRRavlPQHssLAFPF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 llresTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAI-------STHPQFLIAD 153
Cdd:COG4559 91 -----TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 154 EPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:COG4559 166 EPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQyADRILLLHQGRLVAQ 221
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-207 |
1.83e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 120.71 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfsslRNQNVGFVFQ--N 78
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY----RCKHIRMIFQdpN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLRESTVADNVALPLLYAGK-SRKEINGRVSETLKQVGLagYEEQL---PKNMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:COG4167 98 TSLNPRLNIGQILEEPLRLNTDlTAEEREERIFATLRLVGL--LPEHAnfyPHMLSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 155 PTGALD-SETSQeIMNLFKSLNQQEGTTIIMVTHDP----HVAEQcerVIKIIDGRVI 207
Cdd:COG4167 176 ALAALDmSVRSQ-IINLMLELQEKLGISYIYVSQHLgivkHISDK---VLVMHQGEVV 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-207 |
2.13e-33 |
|
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: 119.15 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHdYTRKQfsslRNQNVGFVFQNF 79
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtGELRPT-SGTAYINGYSIR-TDRKA----ARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLRESTVADNValpLLYA---GKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:cd03263 85 ALFDELTVREHL---RFYArlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 157 GALDSETSQEIMNLFKSLnqQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:cd03263 162 SGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-210 |
2.20e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.99 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 3 QRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhdyTRKQFSSLRNQnVGFVFQN-FKL 81
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDIRHK-IGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:PRK13650 94 FVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 227351261 162 ETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISDS 210
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTS 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-207 |
4.01e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.10 E-value: 4.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHpihDYTRKQFSSLRNqNVGFVFQN----FKll 82
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKEIRK-KIGIIFQNpdnqFI-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 rESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:PRK13632 98 -GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 163 TSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
10-207 |
5.60e-33 |
|
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: 121.75 E-value: 5.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLRESTVAD 89
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 90 NvalpLLYAGKSRKEINGRVS--ETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEI 167
Cdd:COG4148 97 N----LLYGRKRAPRAERRISfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 227351261 168 MNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVI 207
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRVV 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-209 |
7.87e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.72 E-value: 7.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFSSLR-----NQNVGFVFqnf 79
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPD-SGEVRLNGRPLADWSPAELARRRavlpqHSSLSFPF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 kllresTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAI------STHPQFLIAD 153
Cdd:PRK13548 92 ------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 154 EPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVAD 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-206 |
1.25e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhdyTRKQFSSLRnQNVGFVFQNFK-LLREST 86
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLR-KHIGIVFQNPDnQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:PRK13648 101 VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 167 IMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-207 |
1.92e-32 |
|
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: 117.33 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIG-FLDDDfEGTYFYQDHPIHDYTrkqFSSLRNQnVGFVFQNFKLLREs 85
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrFYDVD-SGRILIDGHDVRDYT---LASLRRQ-IGLVSQDVFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVAlpllYA--GKSRKEingrVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:cd03251 91 TVAENIA----YGrpGATREE----VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 153 DEPTGALDSETSQEIMnlfKSLNQ-QEGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:cd03251 163 DEATSALDTESERLVQ---AALERlMKNRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-188 |
3.07e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 119.75 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfsslrnQNVGFVFQNFKLLRES 85
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE------RGVGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS---- 161
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrv 170
|
170 180
....*....|....*....|....*..
gi 227351261 162 ETSQEIMNLFKSLnqqeGTTIIMVTHD 188
Cdd:PRK11000 171 QMRIEISRLHKRL----GRTMIYVTHD 193
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-213 |
3.81e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.98 E-value: 3.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKST---LINIIgFLDDDFEGTYFYQDHPihDYTRKQFSSLRNQnVGFVFQN-FKLL 82
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGL-LLPDDNPNSKITVDGI--TLTAKTVWDIREK-VGIVFQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 163 TSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVI-SDSKEE 213
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLaQGSPVE 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-207 |
4.04e-32 |
|
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: 122.13 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIG-FLDDDfEGTYFYQDHPIHDYTrkqFSSLRNQnVGFVFQNFKLLrES 85
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPrFYEPD-SGQILLDGHDLADYT---LASLRRQ-VALVSQDVVLF-ND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALpllyaGKSRKEINGRVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:TIGR02203 421 TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 155 PTGALDSETSQEIMNLFKSLnqQEGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:TIGR02203 496 ATSALDNESERLVQAALERL--MQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-206 |
5.61e-32 |
|
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: 114.24 E-value: 5.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFsslrNQNVGFVFQNFKLLrEST 86
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL----GDHVGYLPQDDELF-SGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNValpllyagksrkeingrvsetlkqvglagyeeqlpknMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:cd03246 92 IAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 167 IMNLFKSLNQQeGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:cd03246 135 LNQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-208 |
1.50e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 116.65 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRK--QFSSLRNQnVGFVFQ--NFK 80
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRKE-IGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLREsTVADNVALPLLYAGKSRKEINGRVSETLKQVGLA-GYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 160 DSETSQEIMNLFKSLNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVIS 208
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVIS 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-209 |
1.59e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 115.88 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 2 SQRFH---VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFL---DDDFEGTYFYQDHPIHDYTR--KQFSSLRNQNvG 73
Cdd:PRK09984 11 AKTFNqhqALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaRDIRKSRANT-G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 74 FVFQNFKLLRESTVADNVALPLL-----------YAGKSRKEingRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARA 142
Cdd:PRK09984 90 YIFQQFNLVNRLSVLENVLIGALgstpfwrtcfsWFTREQKQ---RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 143 ISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRVISD 209
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHVFYD 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
12-209 |
1.60e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 114.68 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 12 NIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFY--QDHPIHDYTRKQFSSLrnqnvgfvFQNFKLLRESTVA 88
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIaGFLTPA-SGSLTLngQDHTTTPPSRRPVSML--------FQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 89 DNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIM 168
Cdd:PRK10771 90 QNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 227351261 169 NLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWD 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-213 |
1.96e-31 |
|
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: 114.39 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhdytRKQFSSLRnQNVGFVFQNFKLLRE 84
Cdd:cd03265 13 FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV----VREPREVR-RRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 165 QEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVIS-DSKEE 213
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAeGTPEE 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
6-206 |
2.00e-31 |
|
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: 114.19 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHpihDYTRkqfSSLRNQNVGFVFQNFKLLRES 85
Cdd:TIGR01277 12 HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ---SHTG---LAPYQRPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:TIGR01277 86 TVRQNIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 227351261 166 EIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRV 206
Cdd:TIGR01277 166 EMLALVKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-213 |
2.28e-31 |
|
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: 114.80 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIG------------FLDDDFEGTyfyqdhPIHDytrkqfssLRnQNVG 73
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlpptygndvrLFGERRGGE------DVWE--------LR-KRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 74 FV---FQNFklLRESTVADNVALPLLYA--GKSRK---EINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAIST 145
Cdd:COG1119 82 LVspaLQLR--FPRDETVLDVVLSGFFDsiGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351261 146 HPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHdpHVAE--QC-ERVIKIIDGRVISD-SKEE 213
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH--HVEEipPGiTHVLLLKDGRVVAAgPKEE 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-210 |
4.26e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.26 E-value: 4.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQnfklLRE 84
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STV-ADNVALPLLYAGKSRK----EINGRVSETLKQVGLA-GYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:PRK13646 96 SQLfEDTVEREIIFGPKNFKmnldEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 159 LDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVISDS 210
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-207 |
7.99e-31 |
|
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: 112.53 E-value: 7.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLdDDFEGTYFYQDHPIhdyTRKQfSSLRNQN-VGFVFQNFKL 81
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLL-PPRSGSIRFDGRDI---TGLP-PHERARAgIGYVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LRESTVADNvalpLLYAGKSRKEinGRVSETLKQVglagYE---------EQLPKNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:cd03224 87 FPELTVEEN----LLLGAYARRR--AKRKARLERV----YElfprlkerrKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNqQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEiADRAYVLERGRVV 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-207 |
1.69e-30 |
|
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: 110.21 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHdytrkqFSSLR---NQNVGFVFQnfk 80
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLYKPD-SGEILVDGKEVS------FASPRdarRAGIAMVYQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 llrestvadnvalpllyagksrkeingrvsetlkqvglagyeeqlpknMSGGQQQRVSIARAISTHPQFLIADEPTGALd 160
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL- 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 161 seTSQEIMNLFKSLNQ--QEGTTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:cd03216 114 --TPAEVERLFKVIRRlrAQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-219 |
2.08e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 114.82 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLRESTVAD 89
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 90 NvalpLLYA-----GKSRKEINGRVSETLkqvGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:TIGR02142 95 N----LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 165 QEIMNLFKSLNQQEGTTIIMVTHDP-HVAEQCERVIKIIDGRVISDSK-EENQRAGN 219
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHSLqEVLRLADRVVVLEDGRVAAAGPiAEVWASPD 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-207 |
2.24e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.11 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKST----LINIIGFldddfEGTYFYQDHPIHDYTRKQFSSLRNQnVGFVFQ---- 77
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpns 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 78 --NFKLLRESTVADnvALPLLYAGKSRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:PRK15134 374 slNPRLNVLQIIEE--GLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 155 PTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVV 505
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-213 |
3.18e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 117.27 E-value: 3.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRkqfSSLRnQNVGFVFQNFKLLrES 85
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDP---ADLR-RNIGYVPQDPRLF-YG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRkeingrVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:TIGR03375 554 TLRDNIALGAPYADDEE------ILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDE 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 155 PTGALDSETSQEIMNLFKSLnqQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISD-SKEE 213
Cdd:TIGR03375 628 PTSAMDNRSEERFKDRLKRW--LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADgPKDQ 685
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-208 |
4.05e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 4.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINiigflddDFEGTYFYQDHPIH----DYTRKQFSSLRNQnVGFVFQN-FK 80
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLL-------HLNGIYLPQRGRVKvmgrEVNAENEKWVRSK-VGLVFQDpDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK13647 91 QVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 227351261 161 SETSQEIMNLFKSLNQQeGTTIIMVTHDPH-VAEQCERVIKIIDGRVIS 208
Cdd:PRK13647 171 PRGQETLMEILDRLHNQ-GKTVIVATHDVDlAAEWADQVIVLKEGRVLA 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-207 |
5.99e-30 |
|
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: 109.56 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDD-DFEGTYFYQDHPIHDytrkqfSSLRNQnVGFVFQNFKLLRE 84
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGlGVSGEVLINGRPLDK------RSFRKI-IGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNvalpLLYAGKSRkeingrvsetlkqvGLagyeeqlpknmSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:cd03213 97 LTVRET----LMFAAKLR--------------GL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 165 QEIMNLFKSLNQQeGTTIIMVTHDP--HVAEQCERVIKIIDGRVI 207
Cdd:cd03213 148 LQVMSLLRRLADT-GRTIICSIHQPssEIFELFDKLLLLSQGRVI 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-209 |
6.63e-30 |
|
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: 110.37 E-value: 6.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRkqfSSLRnQNVGFVFQNFKLLReS 85
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP---ADLR-RNIGYVPQDVTLFY-G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRkeingrVSETLKQVGL--------AGYEEQLPK---NMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:cd03245 93 TLRDNITLGAPLADDER------ILRAAELAGVtdfvnkhpNGLDLQIGErgrGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 155 PTGALDSETSQEIMNLFKSLnqQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISD 209
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-207 |
1.27e-29 |
|
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: 110.01 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTrkqFSSLRnQNVGFVFQNFKLLREsT 86
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLR-RAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVAlpllYagksrkeinGRVSETLKQVGLA---------------GYEEQLPKN---MSGGQQQRVSIARAISTHPQ 148
Cdd:cd03253 91 IGYNIR----Y---------GRPDATDEEVIEAakaaqihdkimrfpdGYDTIVGERglkLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 149 FLIADEPTGALDSETSQEIMNLFKSLNQqeGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-213 |
1.72e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 111.76 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKS-TLINIIGFLDddFEGTYF-----YQDHPIHDYTRKQFSSLRNQNVGFVFQN 78
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLID--YPGRVMaekleFNGQDLQRISEKERRNLVGAEVAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 --FKLLRESTVADNVALPL-LYAGKSRKEINGRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:PRK11022 98 pmTSLNPCYTVGFQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEE 213
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQVVETGKAH 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-194 |
1.75e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.59 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQN-- 78
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKIQIVFQNpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLRESTVADNVALPLLYAGK-SRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:PRK11308 103 GSLNPRKKVGQILEEPLLINTSlSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 227351261 157 GALDSETSQEIMNLFKSLNQQEGTTIIMVTHD----PHVAEQ 194
Cdd:PRK11308 183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDlsvvEHIADE 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-213 |
2.76e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.79 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIhdyTR-KQFSslRNQNVGFVFQNFKL-- 81
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIaGSLPPD-SGSILIDGKDV---TKlPEYK--RAKYIGRVFQDPMMgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 ---LresTVADNVALPL-------LYAGKSRKEINgRVSETLKQVGLaGYEEQLPKNM---SGGQQQRVSIARAISTHPQ 148
Cdd:COG1101 94 apsM---TIEENLALAYrrgkrrgLRRGLTKKRRE-LFRELLATLGL-GLENRLDTKVgllSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 149 FLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQC-ERVIKIIDGRVISDSKEE 213
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRIILDVSGE 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-207 |
9.64e-29 |
|
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: 106.98 E-value: 9.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFsslrnqnvGFVFQNFKLLRES 85
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlGIILPD-SGEVLFDGKPLDIAARNRI--------GYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNvalpLLY----AGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:cd03269 86 KVIDQ----LVYlaqlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 162 ETSQEIMNLFKSLnQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:cd03269 162 VNVELLKDVIREL-ARAGKTVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-207 |
1.38e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 111.82 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDD--DFEGTYFY------------------------------Q 52
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYhvalcekcgyverpskvgepcpvcggtlepE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 53 DHPIHDYTRKQFSSLRNQNVGFVFQNFKLLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGG 132
Cdd:TIGR03269 93 EVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 133 QQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAIWLENGEIK 248
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-213 |
1.56e-28 |
|
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: 107.19 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIgfldddfEGTYFYQDHPI----HDYTRKQFSSLRNQnVGFVFQNFKLL 82
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI-------QRFYVPENGRVlvdgHDLALADPAWLRRQ-VGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 REStVADNVALPllYAGKSRKeingRVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLI 151
Cdd:cd03252 89 NRS-IRDNIALA--DPGMSME----RVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351261 152 ADEPTGALDSETSQEIMNLFKSLNqqEGTTIIMVTHDPHVAEQCERVIKIIDGRVISDSKEE 213
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHD 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-208 |
1.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 108.28 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQ-NFKLLREST 86
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAG-YEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 166 EIMNLFKSLNQQeGTTIIMVTH-DPHVAEQCERVIKIIDGRVIS 208
Cdd:PRK13643 182 EMMQLFESIHQS-GQTVVLVTHlMDDVADYADYVYLLEKGHIIS 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
8-187 |
1.94e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.91 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPI-HDYTRKQFSSLRNQnVGFVFQnF--KLLRE 84
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKK-VGLVFQ-FpeSQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAgyEEQLPKN---MSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIS--ESLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180
....*....|....*....|....*.
gi 227351261 162 ETSQEIMNLFKSLNqQEGTTIIMVTH 187
Cdd:PRK13649 179 KGRKELMTLFKKLH-QSGMTIVLVTH 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-207 |
2.19e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.46 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 3 QRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRkqfSSLRnQNVGFVFQNFKLL 82
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALR-QAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 rESTVADNValpLLYAGKSRKEingRVSETLKQVGLAGYEEQLP----------KNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:PRK11160 427 -SATLRDNL---LLAAPNASDE---ALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQqeGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQII 552
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-188 |
2.58e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.54 E-value: 2.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHD---YTRKqfsslrnqnVGFVFQNFKLL 82
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppYQRP---------INMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180
....*....|....*....|....*.
gi 227351261 163 TSQEIMNLFKSLNQQEGTTIIMVTHD 188
Cdd:PRK11607 184 LRDRMQLEVVDILERVGVTCVMVTHD 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-209 |
4.10e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 105.69 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYfyqdhpihdYTRKQFSSLRNQNVGFvfqnfk 80
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV---------TVRGRVSSLLGLGGGF------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 lLRESTVADNVALPLLYAGKSRKEINGRVSETlkqVGLAGYEE--QLP-KNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:cd03220 96 -NPELTGRENIYLNGRLLGLSRKEIDEKIDEI---IEFSELGDfiDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 158 ALDSETSQEIMNLFKSLNQQeGTTIIMVTHDPH-VAEQCERVIKIIDGRVISD 209
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSsIKRLCDRALVLEKGKIRFD 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-188 |
8.07e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 108.01 E-value: 8.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYtrkqfsSLRNQNVGFVFQNFKLLRE 84
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------EPADRDIAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS--- 161
Cdd:PRK11650 91 MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklr 170
|
170 180
....*....|....*....|....*...
gi 227351261 162 -ETSQEIMNLFKSLnqqeGTTIIMVTHD 188
Cdd:PRK11650 171 vQMRLEIQRLHRRL----KTTSLYVTHD 194
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-210 |
8.07e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 106.33 E-value: 8.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhdyTRKQFSSLRNQnVGFVFQN-FKLLREST 86
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL---TAENVWNLRRK-IGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 167 IMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISDS 210
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-207 |
8.70e-28 |
|
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: 104.61 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDhpihDYTRKQFSSLRNqnVGFVFQNFKLLRES 85
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG----KSYQKNIEALRR--IGALIEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINgrvsETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03268 88 TARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 227351261 166 EIMNLFKSLNQQeGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:cd03268 164 ELRELILSLRDQ-GITVLISSHLLSEIQKvADRIGIINKGKLI 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-205 |
9.68e-28 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 107.12 E-value: 9.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKS-TLINIIGFLDDD--FEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQN--FKLLRE 84
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRAEQISMIFQDpmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPL-LYAGKSRKEINGRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK09473 114 MRVGEQLMEVLmLHKGMSKAEAFEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGR 205
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
8-214 |
1.33e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYT-RKQFSSLRNQnVGFVFQnF--KLLRE 84
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgNKNLKKLRKK-VSLVFQ-FpeAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAgyeEQL----PKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK13641 101 NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLS---EDLisksPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 161 SETSQEIMNLFKSLnQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEEN 214
Cdd:PRK13641 178 PEGRKEMMQLFKDY-QKAGHTVILVTHNmDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-207 |
1.43e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 109.34 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTrkqFSSLRNQnVGFVFQNFKLLREsTV 87
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLRNQ-VALVSQNVHLFND-TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 88 ADNVAlpllYAGK---SRKEIngrvsETLKQVGLA-GYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:PRK11176 434 ANNIA----YARTeqySREQI-----EEAARMAYAmDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILIL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 153 DEPTGALDSETSQEIMnlfKSLNQ-QEGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:PRK11176 505 DEATSALDTESERAIQ---AALDElQKNRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-207 |
1.77e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.96 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFSSL---RnqnvGfvfqnfk 80
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIlGILAPD-SGEVLWDGEPLDPEDRRRIGYLpeeR----G------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNvalpLLY----AGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:COG4152 82 LYPKMKVGEQ----LVYlarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 157 GALDSETSQEIMNLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAK-GTTVIFSSHQmELVEELCDRIVIINKGRKV 208
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1-206 |
2.10e-27 |
|
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: 108.68 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRfHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDdFEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNF 79
Cdd:COG4618 342 GSKR-PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVWPP-TAGSVRLDGADLSQWDREELG----RHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLrESTVADNVAlpllyagksR-KEING-RVSETLKQVGL--------AGYEEQL---PKNMSGGQQQRVSIARAISTH 146
Cdd:COG4618 416 ELF-DGTIAENIA---------RfGDADPeKVVAAAKLAGVhemilrlpDGYDTRIgegGARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 147 PQFLIADEPTGALDSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-207 |
3.05e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.04 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLRESTVAD 89
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 90 NVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMN 169
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190
....*....|....*....|....*....|....*....
gi 227351261 170 LFKSLNQQEGTTIIMVTHDPHVAEQC-ERVIKIIDGRVI 207
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVV 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-199 |
4.72e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFsslrNQNVGFVFQNFKLLREsT 86
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEinGRVSETLKQVGLAgyEEQLPKN---MSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDP--AIFLDDLERFALP--DTILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 227351261 164 SQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVI 199
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
7-199 |
5.48e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.93 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYfyqdhpihdyTRKqfsslRNQNVGFVFQNFKLLRE- 84
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLaGVLRPT-SGTV----------RRA-----GGARVAYVPQRSEVPDSl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 -STVADNVAL----PLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:NF040873 71 pLTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 160 DSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQCERVI 199
Cdd:NF040873 151 DAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCV 189
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-207 |
5.72e-27 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 103.37 E-value: 5.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINIIG--FLDDDFEGTYFYQDHPIHDYTRKQFSSLR---NQNVGFVFQNFK--LL 82
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAgrLAPDHGTATYIMRSGAELELYQLSEAERRrlmRTEWGFVHQNPRdgLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVALPLLYAGKSRKeinGRVSET----LKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:TIGR02323 101 MRVSAGANIGERLMAIGARHY---GNIRATaqdwLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 158 ALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAE-QCERVIKIIDGRVI 207
Cdd:TIGR02323 178 GLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVV 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-207 |
1.02e-26 |
|
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: 101.89 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGeLVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhdytRKQFSSLRnQNVGFVFQNFKLLRES 85
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLR-RRIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03264 88 TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 227351261 166 EIMNLFKSLNqqEGTTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:cd03264 168 RFRNLLSELG--EDRIVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
6-207 |
2.13e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 106.28 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDD---DFEGTYFYQDHPIhdyTRKQFSslrnQNVGFVFQNFKLL 82
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI---DAKEMR----AISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADN------VALPLLYAGKSRKEingRVSETLKQVGLA-------GYEEQLpKNMSGGQQQRVSIARAISTHPQF 149
Cdd:TIGR00955 112 PTLTVREHlmfqahLRMPRRVTKKEKRE---RVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 150 LIADEPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHDP--HVAEQCERVIKIIDGRVI 207
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPssELFELFDKIILMAEGRVA 246
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-207 |
2.46e-26 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 101.46 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYtrkQFSSLRNQnVGFVFQNfKLLREST 86
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRSQ-IGLVSQE-PVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALpllyagksrkeinGRVSETLKQVGLA---------------GYEEQLPKN---MSGGQQQRVSIARAISTHPQ 148
Cdd:cd03249 93 IAENIRY-------------GKPDATDEEVEEAakkanihdfimslpdGYDTLVGERgsqLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 149 FLIADEPTGALDSETSQEIMnlfKSLNQ-QEGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQ---EALDRaMKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-189 |
3.42e-26 |
|
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: 105.14 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRfhVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFSSLrnqnVGFVFQNF 79
Cdd:TIGR02868 346 GAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLaGLLDPL-QGEVTLDGVPVSSLDQDEVRRR----VSVCAQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLrESTVADNVALpllyagkSRKEINGR-VSETLKQVGLAGYEEQLPKNM-----------SGGQQQRVSIARAISTHP 147
Cdd:TIGR02868 419 HLF-DTTVRENLRL-------ARPDATDEeLWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 227351261 148 QFLIADEPTGALDSETSQEIM-NLFKSLnqqEGTTIIMVTHDP 189
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLeDLLAAL---SGRTVVLITHHL 530
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-207 |
5.87e-26 |
|
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: 100.31 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFSSLrnqNVGFVFQNFKLLRE 84
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIvGLVKPD-SGKILLDGQDITKLPMHKRARL---GIGYLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:cd03218 90 LTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 165 QEIMNLFKSLNQQE-GttiIMVThDPHVAEQ---CERVIKIIDGRVI 207
Cdd:cd03218 170 QDIQKIIKILKDRGiG---VLIT-DHNVRETlsiTDRAYIIYEGKVL 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-205 |
6.29e-26 |
|
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: 99.47 E-value: 6.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGfldddfegtyfyqdhpihDYTRKQFSSLRNQNVGFVFQNfKLLRES 85
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLG------------------ELEKLSGSVSVPGSIAYVSQE-PWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNValplLYAGKSRKEingRVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:cd03250 81 TIRENI----LFGKPFDEE---RYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 155 PTGALDSETSQEIMN--LFKSLnqQEGTTIIMVTHDPHVAEQCERVIKIIDGR 205
Cdd:cd03250 154 PLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-214 |
7.53e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.22 E-value: 7.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTL-INIIGFLDDDfEGTYFYQDHPIHDYTRKQfsSLRnQNVGFVFQNFKL----- 81
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLLRPQ-KGKVLVSGIDTGDFSKLQ--GIR-KLVGIVFQNPETqfvgr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LRESTVA---DNVALPLLyagksrkEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:PRK13644 94 TVEEDLAfgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 159 LDSETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQCERVIKIIDGRVISDSKEEN 214
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPEN 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-207 |
7.63e-26 |
|
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: 100.06 E-value: 7.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDdFEGTYFYQDHPI-----HDYTRKqfsslrnqNVGFVFQ 77
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLLPP-RSGSIRFDGEDItglppHRIARL--------GIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 78 N---FKLLresTVADNVALPLlYAGKSRKEINGRVS----------ETLKQvgLAGyeeqlpkNMSGGQQQRVSIARAIS 144
Cdd:COG0410 86 GrriFPSL---TVEENLLLGA-YARRDRAEVRADLErvyelfprlkERRRQ--RAG-------TLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 145 THPQFLIADEPTGALdsetS----QEIMNLFKSLNqQEGTTIIMVTHDPHVAEQ-CERVIkIID-GRVI 207
Cdd:COG0410 153 SRPKLLLLDEPSLGL----AplivEEIFEIIRRLN-REGVTILLVEQNARFALEiADRAY-VLErGRIV 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-209 |
1.58e-25 |
|
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: 98.98 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 2 SQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDD-----FEGTyfyqdhpihDYTRKQFSSLRnqNVGFV 75
Cdd:cd03266 15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLaGLLEPDagfatVDGF---------DVVKEPAEARR--RLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 76 FQNFKLLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 156 TGALDSETSQEIMNLFKSLnQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVISD 209
Cdd:cd03266 164 TTGLDVMATRALREFIRQL-RALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYE 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-207 |
1.60e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.74 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIH---DYTRKQFSSLRNQnVGFVFQNFKLLR 83
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkDIFQIDAIKLRKE-VGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAG-KSRKEINGRVSETLKQVGLagYEEQLPK------NMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 157 GALDSETSQEIMNLFKSLNQQegTTIIMVTHDP-HVAEQCERVIKIIDGRVI 207
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPqQVARVADYVAFLYNGELV 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-207 |
1.64e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.62 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFY-----QDHPIHDYTRKQFSSLRNQNVGFVFQN-FK 80
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPD-AGEVHYrmrdgQLRDLYALSEAERRRLLRTEWGFVHQHpRD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVAD-NVALPLLYAG-KSRKEINGRVSETLKQVGLAGYE-EQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:PRK11701 101 GLRMQVSAGgNIGERLMAVGaRHYGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 158 ALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:PRK11701 181 GLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVV 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-198 |
1.90e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.60 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDF-----EGTYFYQDHpihDYTRKQFSSLRnQNVGFVFQNFKL 81
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQ---DIFKMDVIELR-RRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LRESTVADNVAL--PLLYAGKSRKEINGRVSETLKQVGLagYEEQLPK------NMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:PRK14247 94 IPNLSIFENVALglKLNRLVKSKKELQERVRWALEKAQL--WDEVKDRldapagKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 154 EPTGALDSETSQEIMNLFKSLNQQegTTIIMVTHDPhvaEQCERV 198
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD--MTIVLVTHFP---QQAARI 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-198 |
2.05e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.53 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFL-----DDDFEG--------TYFYQDHPIHdyTRKQfsslrnqnV 72
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGevrlfgrnIYSPDVDPIE--VRRE--------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 73 GFVFQNFKLLRESTVADNVALPLLYAG--KSRKEINGRVSETLKQVGLagYEE------QLPKNMSGGQQQRVSIARAIS 144
Cdd:PRK14267 88 GMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAAL--WDEvkdrlnDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 145 THPQFLIADEPTGALDSETSQEIMNLFKSLnqQEGTTIIMVTHDPhvaEQCERV 198
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSP---AQAARV 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-209 |
3.32e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGfldddfeGTYfyqdHP----IHdyTRKQFSSLRNQNVGFVf 76
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA-------GIL----EPtsgrVE--VNGRVSALLELGAGFH- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 77 qnfkllRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQlP-KNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:COG1134 101 ------PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 156 TGALDSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:COG1134 174 LAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMD 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-207 |
3.90e-25 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 96.61 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 3 QRFHVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYT---RKQFSSLrNQNVgFVFqn 78
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLKPQ-QGEITLDGVPVSDLEkalSSLISVL-NQRP-YLF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 fkllrESTVADNVALPLlyagksrkeingrvsetlkqvglagyeeqlpknmSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:cd03247 88 -----DTTLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 227351261 159 LDSETSQEIMNLFksLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:cd03247 129 LDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
7-208 |
4.19e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 98.71 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNFKLLREST 86
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVAL---PLLYA-GKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:PRK10575 102 VRELVAIgryPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 163 TSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVIS 208
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIA 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
10-207 |
5.25e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.78 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLIN-IIGfLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQN--FKLLREST 86
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPL--LYAGKSRKEINGRVSETLKQVGLAgyeEQL----PKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK15079 117 IGEIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLL---PNLinryPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 161 SETSQEIMNLFKSLNQQEGTTIIMVTHDphvaeqcERVIKIIDGRVI 207
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHD-------LAVVKHISDRVL 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
7-189 |
5.63e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 97.73 E-value: 5.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDD---FEGTYFYQDHPIHdytRKQFSslrnQNVGFVFQNFKLLR 83
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK---PDQFQ----KCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVAD------NVALPLLYAGKSRKEINgrVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:cd03234 95 GLTVREtltytaILRLPRKSSDAIRKKRV--EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190
....*....|....*....|....*....|..
gi 227351261 158 ALDSETSQEIMNLFKSLnQQEGTTIIMVTHDP 189
Cdd:cd03234 173 GLDSFTALNLVSTLSQL-ARRNRIVILTIHQP 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-207 |
1.41e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 98.38 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 2 SQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTY----FYQDHPIHDYTR---------KQFSSLR 68
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELitnpyskkiKNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 69 nQNVGFVFQ--NFKLLREsTVADNVALPLLYAGKSRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAIST 145
Cdd:PRK13631 116 -RRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351261 146 HPQFLIADEPTGALDSETSQEIMNLFKSlNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTmEHVLEVADEVIVMDKGKIL 255
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-208 |
3.18e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.80 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIhdyTRKQFSSLRnQNVGFVFQNFK-LLRE 84
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVR-KFVGLVFQNPDdQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:PRK13652 94 PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 165 QEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVIS 208
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGRIVA 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-198 |
3.23e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 97.67 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKStLI--NIIGFLDDDFEGT---YFYQDHPIHDYTRKQFSSLRNQNVGFVFQN 78
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKS-LIakAICGITKDNWHVTadrFRWNGIDLLKLSPRERRKIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 -----------FKLLRESTVADNVALPLLYAGKSRKEingRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIARAIS 144
Cdd:COG4170 98 psscldpsakiGDQLIEAIPSWTFKGKWWQRFKWRKK---RAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 145 THPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERV 198
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLEsISQWADTI 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-217 |
5.07e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.99 E-value: 5.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQnVGFVFQNFKLLREST 86
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEI-NGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:PRK11831 101 VFDNVAYPLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 166 EIMNLFKSLNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEENQRA 217
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-201 |
6.65e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.73 E-value: 6.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYfyqDHPihdytrkqfsslRNQNVGFVFQNFKL----L 82
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI---ARP------------AGARVLFLPQRPYLplgtL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 REStvadnvalpLLYAGKSRKEINGRVSETLKQVGLAGYEEQL------PKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:COG4178 443 REA---------LLYPATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 157 GALDSETSQEIMNLFKSlnQQEGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:COG4178 514 SALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-207 |
7.19e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 11 INIEIDQGELVAIIGESGSGKSTLIN-IIGFLDddFEGTYFYQDHPIHDYTRKQFsslrNQNVGFVFQNFKLLrESTVAD 89
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNaLLGFLP--YQGSLKINGIELRELDPESW----RKHLSWVGQNPQLP-HGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 90 NVALpllyagkSRKEIN-GRVSETLKQVGLAGYEEQLPKNM-----------SGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:PRK11174 442 NVLL-------GNPDASdEQLQQALENAWVSEFLPLLPQGLdtpigdqaaglSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 158 ALDSETSQEIMNlfkSLNQQ-EGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:PRK11174 515 SLDAHSEQLVMQ---ALNAAsRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-206 |
7.71e-24 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 98.57 E-value: 7.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNFKLLrEST 86
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELF-PGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVAlpllyagksRKEINGRVSETLKQVGLAGYEE---QLPK-----------NMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:TIGR01842 408 VAENIA---------RFGENADPEKIIEAAKLAGVHElilRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQEGTTIImVTHDPHVAEQCERVIKIIDGRV 206
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGCVDKILVLQDGRI 531
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-209 |
9.31e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNFKLLREST 86
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVAL---PLL-YAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:PRK11231 93 VRELVAYgrsPWLsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 227351261 163 TSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:PRK11231 173 HQVELMRLMRELNTQ-GKTVVTVLHDLNQASRyCDHLVVLANGHVMAQ 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-206 |
1.15e-23 |
|
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: 92.88 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHdytRKQFSSLRNQNVGFVFQNFK---LLR 83
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT---RRSPRDAIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLyagksrkeingrvsetlkqvglagyeeqlpknMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:cd03215 92 DLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 164 SQEIMNLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKIIDGRV 206
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-207 |
1.30e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.00 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRnQNVGFVFQN--FKLLR 83
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGKSR-KEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 162 ETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIV 543
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-190 |
1.74e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.72 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDD-----DFEGTYFYQDHPIHDyTRKQFSSLRNQnVGFVFQNFKL 81
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYE-RRVNLNRLRRQ-VSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LREStVADNVALPLLYAG-KSRKEINGRVSETLKQVGLagYEEQLPK------NMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:PRK14258 100 FPMS-VYDNVAYGVKIVGwRPKLEIDDIVESALKDADL--WDEIKHKihksalDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 227351261 155 PTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH 190
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLH 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
8-212 |
5.97e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDD-----DFEGTYFYQDHPIHDyTRKQFSSLRNQnVGFVFQN---F 79
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYS-PRTDTVDLRKE-IGMVFQQpnpF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLlresTVADNVALPLLYAG-KSRKEINGRVSETLKQVGLagYEE---QLPKN---MSGGQQQRVSIARAISTHPQFLIA 152
Cdd:PRK14239 99 PM----SIYENVVYGLRLKGiKDKQVLDEAVEKSLKGASI--WDEvkdRLHDSalgLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQegTTIIMVTHDPHVAEQ-CERVIKIIDGRVI--SDSKE 212
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRiSDRTGFFLDGDLIeyNDTKQ 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-206 |
6.51e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 96.33 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKqfsSLRNQnVGFVFQNFKLLRESt 86
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH---YLHRQ-VALVGQEPVLFSGS- 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRkeingrVSETLKQVGLAGYEEQLPKN-----------MSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:TIGR00958 571 VRENIAYGLTDTPDEE------IMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 156 TGALDSETSQeimnLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:TIGR00958 645 TSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-207 |
6.98e-23 |
|
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: 91.79 E-value: 6.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfssLRnQNVGFVFQNfKLLREST 86
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD---LR-SRISIIPQD-PVLFSGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVAlPLLYAgkSRKEINgrvsETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:cd03244 94 IRSNLD-PFGEY--SDEELW----QALERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 156 TGALDSETSQEIMNL----FKslnqqeGTTIIMVTHDPHVAEQCERVIKIIDGRVI 207
Cdd:cd03244 167 TASVDPETDALIQKTireaFK------DCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-193 |
9.43e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 91.56 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 3 QRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIgfldddFEGTYFYQDHPIHDYTRKQFSslrnqnvgfvfqnfkll 82
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL------AGALKGTPVAGCVDVPDNQFG----------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVAlpllyagkSRKEINGRVsETLKQVGLAgyEEQL----PKNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:COG2401 98 REASLIDAIG--------RKGDFKDAV-ELLNAVGLS--DAVLwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|....*
gi 227351261 159 LDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAE 193
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHHYDVID 201
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-216 |
1.18e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.98 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 11 INIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSslrNQNVGFVFQNFKLLRESTVADN 90
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 91 --VALPL-----LYAG--------KSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:PRK11300 101 llVAQHQqlktgLFSGllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351261 156 TGALDSETSQEIMNLFKSLNQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEENQR 216
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDmKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-209 |
2.52e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.59 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNFK 80
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVA------LPLLyaGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:PRK10253 92 TPGDITVQELVArgryphQPLF--TRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 155 PTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVA-EQCERVIKIIDGRVISD 209
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQ 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
10-214 |
2.85e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 92.63 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLRESTVAD 89
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 90 NvalpLLYaGKSRKeingRVSETLKQVGLAGYE---EQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:PRK11144 96 N----LRY-GMAKS----MVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 167 IMNLFKSLNQQEGTTIIMVTHD----PHVAeqcERVIKIIDGRVISDSKEEN 214
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSldeiLRLA---DRVVVLEQGKVKAFGPLEE 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-217 |
7.16e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 7.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRfHVLHDINIEIDQGELVAIIGESGSGKS-TLINIIGFLDDD----FEGTYFYQDHPIHDYTRKQFSSLRNQNVGFV 75
Cdd:PRK15134 19 QTVR-TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 76 FQnfkllrESTVADNvalPL------------LYAGKSRKEINGRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIA 140
Cdd:PRK15134 98 FQ------EPMVSLN---PLhtlekqlyevlsLHRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 141 RAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVIsdskEENQRA 217
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCV----EQNRAA 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-194 |
9.97e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.85 E-value: 9.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 3 QRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIH--DYtrkqfsSLRNQNVGFVFQN-- 78
Cdd:PRK15112 24 QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDY------SYRSQRIRMIFQDps 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLRESTVADNVALPL-LYAGKSRKEINGRVSETLKQVGL----AGYeeqLPKNMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:PRK15112 98 TSLNPRQRISQILDFPLrLNTDLEPEQREKQIIETLRQVGLlpdhASY---YPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 154 EPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHD----PHVAEQ 194
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGISYIYVTQHlgmmKHISDQ 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-214 |
1.23e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.23 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 2 SQRFHVLHDINIEIDQGELVAIIGESGSGKS----TLINIIGFLDDDFEGTYFY------QDHPIHDYTRKQFSSLRNQN 71
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLlrrrsrQVIELSEQSAAQMRHVRGAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 72 VGFVFQN--FKLLRESTVADNVALPL-LYAGKSRKEINGRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIARAIST 145
Cdd:PRK10261 106 MAMIFQEpmTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAQTILsryPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 146 HPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVISDSKEEN 214
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGSVEQ 255
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
9-207 |
1.58e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.99 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 9 HDINIEIDQGELVAIIGESGSGKS-TLINIIGFLDDDFE---GTYFYQDHPIHDytrkqfSSLRNQNVGFVFQN----FK 80
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGVRqtaGRVLLDGKPVAP------CALRGRKIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLResTVADNVALPLLYAGKSRKeiNGRVSETLKQVGLAGYEEQL---PKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:PRK10418 94 PLH--TMHTHARETCLALGKPAD--DATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 158 ALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQC-ERVIKIIDGRVI 207
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIV 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-198 |
2.66e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.69 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDD-----DFEGTYFYQDHPIHDyTRKQFSSLRNQnVGFVFQNF 79
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLREStVADNVAlpllYAGKsrkeING--------------------RVSETLKQVGLAgyeeqlpknMSGGQQQRVSI 139
Cdd:PRK14243 101 NPFPKS-IYDNIA----YGAR----INGykgdmdelverslrqaalwdEVKDKLKQSGLS---------LSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 140 ARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQegTTIIMVTHDphvAEQCERV 198
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHN---MQQAARV 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-188 |
2.77e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 3 QRFHVLHDINIEIDQGELVAIIGESGSGKSTL-INIIGFLDDDfEGTYFYQDHPIhDYTRKQFSSLRNQnVGFVFQN-FK 80
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQ-KGAVLWQGKPL-DYSKRGLLALRQQ-VATVFQDpEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180
....*....|....*....|....*...
gi 227351261 161 SETSQEIMNLFKSLNQQeGTTIIMVTHD 188
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQ-GNHVIISSHD 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-201 |
3.85e-21 |
|
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: 86.05 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYfyqdhpihdytrkqfSSLRNQNVGFVFQnfkllrest 86
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------GMPEGEDLLFLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 vadnvaLPLLYAGksrkeingrvseTLKqvglagyeEQL--P--KNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:cd03223 72 ------RPYLPLG------------TLR--------EQLiyPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 227351261 163 TSQEIMNLFKslnqQEGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:cd03223 126 SEDRLYQLLK----ELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-206 |
7.44e-21 |
|
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: 86.76 E-value: 7.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSlrnqNVGFVFQNFKLLRESt 86
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS----KVSLVGQEPVLFARS- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLlyAGKSrkeiNGRVSETLKQVGLAGYEEQLPKN-----------MSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:cd03248 104 LQDNIAYGL--QSCS----FECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 156 TGALDSETSQEIMNLFKSLNQQegTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-208 |
9.69e-21 |
|
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: 86.42 E-value: 9.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDfEGTYFYQDHPIhdyTRKQFSSLRNQNVGFVFQN---FKL 81
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLLPVK-SGSIRLDGEDI---TKLPPHERARAGIAYVPQGreiFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LresTVADNVALPLLYAGKSRKEINGRVSE---TLKQV--GLAGyeeqlpkNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:TIGR03410 90 L---TVEENLLTGLAALPRRSRKIPDEIYElfpVLKEMlgRRGG-------DLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 227351261 157 GALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIID-GRVIS 208
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMErGRVVA 212
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-187 |
1.06e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.49 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRkqfSSLRNQnVGFVFQNFKLLREs 85
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYDVT-SGRILIDGQDIRDVTQ---ASLRAA-IGIVPQDTVLFND- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVAlpllYA--GKSRKEINgrvsETLKQVGLAGYEEQLPKNM-----------SGGQQQRVSIARAISTHPQFLIA 152
Cdd:COG5265 447 TIAYNIA----YGrpDASEEEVE----AAARAAQIHDFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|....*.
gi 227351261 153 DEPTGALDSETSQEIMnlfKSLNQ-QEGTTIIMVTH 187
Cdd:COG5265 519 DEATSALDSRTERAIQ---AALREvARGRTTLVIAH 551
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-208 |
1.14e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQdhpihdytrkqfsslRNQNVGFVFQNFKLLREST 86
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNV--ALPLLYAGKSRKE-------------------------ING-----RVSETLKQVGLAGYEEQLP-KNMSGGQ 133
Cdd:COG0488 78 VLDTVldGDAELRALEAELEeleaklaepdedlerlaelqeefeaLGGweaeaRAEEILSGLGFPEEDLDRPvSELSGGW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 134 QQRVSIARAISTHPQFLIADEPTGALDSETsqeIMNLFKSLNQQEGtTIIMVTHDPH-VAEQCERVIKIIDGRVIS 208
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPG-TVLVVSHDRYfLDRVATRILELDRGKLTL 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-208 |
1.65e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.08 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINII------GflddDFEGTYFYQDHPIhdytrkQFSSLRN-QNVGFVF--QN 78
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphG----SYEGEILFDGEVC------RFKDIRDsEALGIVIihQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLRESTVADNVAL---PLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:NF040905 87 LALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 156 TGALDSETSQEIMNLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKIIDGRVIS 208
Cdd:NF040905 167 TAALNEEDSAALLDLLLELKAQ-GITSIIISHKlNEIRRVADSITVLRDGRTIE 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
8-208 |
1.76e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.83 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINII------GflddDFEGTYFYQDHPIhdytrkQFSSLRN-QNVGFV--FQN 78
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphG----TYEGEIIFEGEEL------QASNIRDtERAGIAiiHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 79 FKLLRESTVADNVAL--PLLYAGK-SRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:PRK13549 91 LALVKELSVLENIFLgnEITPGGImDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 156 TGAL-DSETSQeIMNLFKSLnQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVIS 208
Cdd:PRK13549 171 TASLtESETAV-LLDIIRDL-KAHGIACIYISHKlNEVKAISDTICVIRDGRHIG 223
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-194 |
2.75e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 87.17 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 11 INIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDFEGT---YFYQDHPIHDYTRKQFSSLRNQNVGFVFQNfkllREST 86
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKaICGVTKDNWRVTadrMRFDDIDLLRLSPRERRKLVGHNVSMIFQE----PQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 V--ADNVALPLL-------YAGKSRKEIN---GRVSETLKQVGLAGYEE---QLPKNMSGGQQQRVSIARAISTHPQFLI 151
Cdd:PRK15093 102 LdpSERVGRQLMqnipgwtYKGRWWQRFGwrkRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 227351261 152 ADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ 194
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQ 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-213 |
3.32e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.08 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHD---YTRKQFSslrnqnVGFVFQNFKLL 82
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIvGLVKPD-SGRIFLDGEDITHlpmHKRARLG------IGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:COG1137 91 RKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 163 TSQEIMNLFKSLnQQEGttI-IMVThDPHVAEQ---CERVIKIIDGRVI-SDSKEE 213
Cdd:COG1137 171 AVADIQKIIRHL-KERG--IgVLIT-DHNVRETlgiCDRAYIISEGKVLaEGTPEE 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-187 |
8.17e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.08 E-value: 8.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRkqfSSLRnQNVGFVFQNFKLLRES 85
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLmGYYPLT-EGEIRLDGRPLSSLSH---SVLR-QGVAMVQQDPVVLADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVAdNVALpllyaGKSRKEinGRVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:PRK10790 431 FLA-NVTL-----GRDISE--EQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190
....*....|....*....|....*....|...
gi 227351261 155 PTGALDSETSQEIMNLFKSLNQQegTTIIMVTH 187
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREH--TTLVVIAH 533
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-211 |
9.77e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.52 E-value: 9.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLdddfegtyfyqdHP------IHDYT----RKQFSslrnQNVGF 74
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL------------VPtsgevrVLGYVpfkrRKEFA----RRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 75 VF-------------QNFKLLREstvadnvalplLYaGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIAR 141
Cdd:COG4586 100 VFgqrsqlwwdlpaiDSFRLLKA-----------IY-RIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351261 142 AISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIkIID-GRVISDSK 211
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdIEALCDRVI-VIDhGRIIYDGS 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-214 |
1.48e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.39 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 11 INIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQ--DHPIhDYTRKQFSsLR---NQNVGFVFQNFKLLRES 85
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgDEWV-DMTKPGPD-GRgraKRYIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADN----VALPLLYAGKSRKEINgrvseTLKQVGLAGYE-----EQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:TIGR03269 381 TVLDNlteaIGLELPDELARMKAVI-----TLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351261 157 GALDSET----SQEIMNLFKSLNQqegtTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEEN 214
Cdd:TIGR03269 456 GTMDPITkvdvTHSILKAREEMEQ----TFIIVSHDmDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-211 |
2.13e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRkqfssLRNQNVGFVFQNFKLLREST 86
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-----LARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 227351261 167 IMNLFKSLNQQeGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISDSK 211
Cdd:PRK13536 211 IWERLRSLLAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGR 255
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-189 |
2.76e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.23 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDytrkqfSSLRNQNVGFVFQNFkLLREST 86
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD------PDVAEACHYLGHRNA-MKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSrkeiNGRVSETLKQVGLAGYEEqLP-KNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:PRK13539 90 VAENLEFWAAFLGGE----ELDIAAALEAVGLAPLAH-LPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|....*
gi 227351261 166 EIMNLFKS-LNQqeGTTIIMVTHDP 189
Cdd:PRK13539 165 LFAELIRAhLAQ--GGIVIAATHIP 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-213 |
3.38e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQD-----HPIHDYtrKQFSSLRNQnVGFVFQNFKL 81
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvllggRSIFNY--RDVLEFRRR-VGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 LREStVADNVaLPLLYAGK--SRKEINGRVSETLKQVGL-AGYEEQL---PKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:PRK14271 113 FPMS-IMDNV-LAGVRAHKlvPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 156 TGALDSETSQEIMNLFKSLNQQegTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEE 213
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADR--LTVIIVTHNlAQAARISDRAALFFDGRLVEEGPTE 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-207 |
4.62e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGfldddfeGTYFYQDHPIH-DYTRKQFSSLR---NQNVGFVFQNFKLLR 83
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILS-------GNYQPDAGSILiDGQEMRFASTTaalAAGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNV---ALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALd 160
Cdd:PRK11288 93 EMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 161 seTSQEIMNLFKSLNQ--QEGTTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:PRK11288 172 --SAREIEQLFRVIRElrAEGRVILYVSHRmEEIFALCDAITVFKDGRYV 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-214 |
4.63e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.88 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIG--FLDDDFEGTYFYQDHPIhdytrkQFSSLRN---QNVGFVFQNFKLL 82
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGSPL------KASNIRDterAGIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVAL--PLLYAGK--SRKEINGRVSETLKQVGLAGYEEQLP-KNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:TIGR02633 91 PELSVAENIFLgnEITLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 158 ALDSETSQEIMNLFKSLnQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEEN 214
Cdd:TIGR02633 171 SLTEKETEILLDIIRDL-KAHGVACVYISHKlNEVKAVCDTICVIRDGQHVATKDMST 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-192 |
5.30e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.23 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYtrkQFSSLRNQNVGFVFQNFKLLR 83
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGKSR-KEINGRVSETLKQvgLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:PRK11614 94 RMTVEENLAMGGFFAERDQfQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190
....*....|....*....|....*....|
gi 227351261 163 TSQEIMNLFKSLnQQEGTTIIMVTHDPHVA 192
Cdd:PRK11614 172 IIQQIFDTIEQL-REQGMTIFLVEQNANQA 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-207 |
5.90e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.63 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKqfsSLRnQNVGFVFQNFKLLREStV 87
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA---SLR-RNIAVVFQDAGLFNRS-I 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 88 ADNVALpllyagksrkeinGRVSETLKQVGLA---------------GYEEQLP---KNMSGGQQQRVSIARAISTHPQF 149
Cdd:PRK13657 426 EDNIRV-------------GRPDATDEEMRAAaeraqahdfierkpdGYDTVVGergRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 150 LIADEPTGALDSETSQEIMNLFKSLNQQEGTTIImvTHDPHVAEQCERVIKIIDGRVI 207
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMKGRTTFII--AHRLSTVRNADRILVFDNGRVV 548
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-210 |
6.62e-19 |
|
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: 81.61 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDH-PIHDytRKQFSSlrnqNVGFVF-QNFKLLR 83
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILsGLLQPT-SGEVRVAGLvPWKR--RKKFLR----RIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVAL-------PLLYAGKSRKEIngrvSETLKqvgLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:cd03267 109 DLPVIDSFYLlaaiydlPPARFKKRLDEL----SELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 157 GALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPH-VAEQCERVIKIIDGRVISDS 210
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
7-187 |
7.33e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.38 E-value: 7.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYtrkQFSSLRNQnVGFVFQNfKLLREST 86
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-LAVVSQT-PFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSET------LKQvglaGYEEQLPKN---MSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVARLASVhddilrLPQ----GYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190
....*....|....*....|....*....|.
gi 227351261 158 ALDSETSQEIMnlfKSLNQ-QEGTTIIMVTH 187
Cdd:PRK10789 481 AVDGRTEHQIL---HNLRQwGEGRTVIISAH 508
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-209 |
1.75e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLrnqNVGFVFQNFKLLRES 85
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNvalplLYAGK------------SRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIAD 153
Cdd:PRK09700 96 TVLEN-----LYIGRhltkkvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227351261 154 EPTGALdseTSQEIMNLFKSLNQ--QEGTTIIMVTHD-PHVAEQCERVIKIIDG-----RVISD 209
Cdd:PRK09700 171 EPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKlAEIRRICDRYTVMKDGssvcsGMVSD 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-207 |
2.04e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDhpihdytrkqfsslrNQNVGFVFQNFKLLRES 85
Cdd:COG0488 330 LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGELEPD-SGTVKLGE---------------TVKIGYFDQHQEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 -TVADNVALplLYAGKSRKEINGRvsetLKQVGLAGYEEQLP-KNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:COG0488 394 kTVLDELRD--GAPGGTEQEVRGY----LGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 164 SQEIMNLfksLNQQEGtTIIMVTHDPHVAEQ-CERVIKIIDGRVI 207
Cdd:COG0488 468 LEALEEA---LDDFPG-TVLLVSHDRYFLDRvATRILEFEDGGVR 508
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
11-208 |
3.26e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 11 INIEIDQGELVAIIGESGSGKSTLINII-GFLDddFEGTYFYQDHPIHDYTRKQFSSLR-----NQNVGFVFQNFKLLRE 84
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMaGLLP--GQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFAMPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 StvadnvalplLYAGKSRKEINGRVSETLKQVGLagyEEQLPKNM---SGGQQQRVSIARA-------ISTHPQFLIADE 154
Cdd:COG4138 93 H----------QPAGASSEAVEQLLAQLAEALGL---EDKLSRPLtqlSGGEWQRVRLAAVllqvwptINPEGQLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 155 PTGALDseTSQEIM--NLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKIIDGRVIS 208
Cdd:COG4138 160 PMNSLD--VAQQAAldRLLRELCQQ-GITVVMSSHDlNHTLRHADRVWLLKQGKLVA 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-211 |
5.82e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.85 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIG--FLDDDFEGTYFYQDHPIHDYTRKQfsslrnqnVGFVFQNFKLLRE 84
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgrIQGNNFTGTILANNRKPTKQILKR--------TGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADN-VALPLLYAGKS-RKEINGRVSET-LKQVGLAGYEEQLPKN-----MSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:PLN03211 155 LTVRETlVFCSLLRLPKSlTKQEKILVAESvISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 157 GALDSETSQEIMNLFKSLnQQEGTTIIMVTHDP--HVAEQCERVIKIIDGRVISDSK 211
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPssRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-205 |
5.96e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 77.10 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIgfldddfegtyfyqdhpihdytrkqfsslrnqnvgfvfqnfkllrest 86
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------------------------ 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 vadnvalpllyAGKSrKEINGRVseTLKQVGLAGYEEQLpknmSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:cd03221 47 -----------AGEL-EPDEGIV--TWGSTVKIGYFEQL----SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 167 IMNLFKSLNQqegtTIIMVTHDPHVAEQ-CERVIKIIDGR 205
Cdd:cd03221 109 LEEALKEYPG----TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-201 |
6.14e-18 |
|
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: 78.30 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHdytrKQFSSLRnQNVGFVFQNFKLLREST 86
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD----FQRDSIA-RGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNvaLPLLYAGKSRKEIngrvSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:cd03231 90 VLEN--LRFWHADHSDEQV----EEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 227351261 167 IMNLFKSLNQQeGTTIIMVTHDP-HVAEQCERVIKI 201
Cdd:cd03231 164 FAEAMAGHCAR-GGMVVLTTHQDlGLSEAGARELDL 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-207 |
1.37e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.45 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGfLDDDFEGTYFYQDHPIHdytrkqFSSLR---NQNVGFVFQNFK- 80
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARaLFG-ADPADSGEIRLDGKPVR------IRSPRdaiRAGIAYVPEDRKg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 --LLRESTVADNVALPLL--YAGK---SRKEINGRVSETLKQVGL-AGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:COG1129 339 egLVLDLSIRENITLASLdrLSRGgllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSElPELLGLSDRILVMREGRIV 473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-213 |
3.82e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.63 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDD------DFEGTYFYQdhPIHDYTrkqFSSLRNQNVGFvFQNFK 80
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHaetssvVIRGSVAYV--PQVSWI---FNATVRENILF-GSDFE 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPL---LYAGKSRKEINGRvsetlkqvGLagyeeqlpkNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:PLN03232 707 SERYWRAIDVTALQHdldLLPGRDLTEIGER--------GV---------NISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 158 ALDSETSQEImnlFKSLNQQE--GTTIIMVTHDPHVAEQCERVIKIIDGRVisdsKEE 213
Cdd:PLN03232 770 ALDAHVAHQV---FDSCMKDElkGKTRVLVTNQLHFLPLMDRIILVSEGMI----KEE 820
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-211 |
4.98e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.92 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQfsslrNQNVGFVFQNFKLLREST 86
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-----RQRVGVVPQFDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:PRK13537 97 VRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 227351261 167 IMNLFKSLnQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISDSK 211
Cdd:PRK13537 177 MWERLRSL-LARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGA 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-191 |
6.62e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYfyqdhpihdytrKQFSSLRnqnVGFVFQNFKLlrest 86
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR---IGYVPQKLYL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 vadNVALPL-------LYAGKSRKEIngrvSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:PRK09544 79 ---DTTLPLtvnrflrLRPGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190
....*....|....*....|....*....|..
gi 227351261 160 DSETSQEIMNLFKSLNQQEGTTIIMVTHDPHV 191
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-206 |
1.17e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRfhVLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYTRKQFSslrnQNVGFVFQNF 79
Cdd:PRK09536 14 GDTT--VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAInGTLTPT-AGTVLVAGDDVEALSARAAS----RRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLRESTVADNVAL---PLLYAGKSRKEINGR-VSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:PRK09536 87 SLSFEFDVRQVVEMgrtPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 156 TGALDSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRV 206
Cdd:PRK09536 167 TASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARyCDELVLLADGRV 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-208 |
1.21e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.70 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKST-LINIIGFLDDDfEGTYFYQDH-----PIHDYTRKqfsslrnqNVGFVFQNFK 80
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGIVPRD-AGNIIIDDEdisllPLHARARR--------GIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNV-ALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:PRK10895 89 IFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 227351261 160 DSETSQEIMNLFKSLnQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVIS 208
Cdd:PRK10895 169 DPISVIDIKRIIEHL-RDSGLGVLITDHNvRETLAVCERAYIVSQGHLIA 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-189 |
4.32e-16 |
|
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: 73.55 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHdytrkQFSSLRNQNVGFVFQNFKLLREST 86
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALpllYAGKSRKEINGrVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQE 166
Cdd:TIGR01189 90 ALENLHF---WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|...
gi 227351261 167 IMNLFKSlNQQEGTTIIMVTHDP 189
Cdd:TIGR01189 166 LAGLLRA-HLARGGIVLLTTHQD 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
7-206 |
7.25e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLIniiGFLDDDFEGT-----------YFYQDHPIHDYTrkqfssLRNqNVGFv 75
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLL---QSLLSQFEISegrvwaersiaYVPQQAWIMNAT------VRG-NILF- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 76 fqnFKLLRESTVADNValpllyagksrkeingRVSE---TLKQVGlAGYEEQLPK---NMSGGQQQRVSIARAISTHPQF 149
Cdd:PTZ00243 744 ---FDEEDAARLADAV----------------RVSQleaDLAQLG-GGLETEIGEkgvNLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 150 LIADEPTGALDSETSQEIM-NLFksLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:PTZ00243 804 YLLDDPLSALDAHVGERVVeECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
8-204 |
1.64e-15 |
|
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: 72.36 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKST-LINIIGFLdDDFEGTYFYQDHPIHDYTRKQFSSLRNQNVGFVFQNFKLLrEST 86
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSlLLAILGEM-QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSeTLKQVGLAGYEEQLP-----KNMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACS-LQPDIDLLPFGDQTEigergINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 162 ETSQEIMN--LFKSLnQQEGTTIIMVTHDPHVAEQCERVIKIIDG 204
Cdd:cd03290 174 HLSDHLMQegILKFL-QDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-206 |
2.31e-15 |
|
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: 74.28 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 11 INIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHdytrKQFSSLRnQNVGFVFQNFKLLRESTVADN 90
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE----TNLDAVR-QSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 91 ValpLLYA---GKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEI 167
Cdd:TIGR01257 1024 I---LFYAqlkGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 227351261 168 MNLFksLNQQEGTTIIMVTHdpHVAEQ---CERVIKIIDGRV 206
Cdd:TIGR01257 1101 WDLL--LKYRSGRTIIMSTH--HMDEAdllGDRIAIISQGRL 1138
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-209 |
2.31e-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: 74.09 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDFEGTYFYQDHPIHdyTRKQFSSLRnQNVGFVFQNFK---LLRES 85
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD--IRNPAQAIR-AGIAMVPEDRKrhgIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLL--YAGKSR----KEInGRVSETLKQVGLAGYEEQLP-KNMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:TIGR02633 355 GVGKNITLSVLksFCFKMRidaaAEL-QIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 159 LDSETSQEIMNLFKSLnQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISD 209
Cdd:TIGR02633 434 VDVGAKYEIYKLINQL-AQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-187 |
4.48e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVL-HDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDyTRKQFsslrNQNvgfvfqnfkLL-- 82
Cdd:PRK13538 14 RILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEY----HQD---------LLyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 -------RESTVADNVALPLLYAGKSRKEingRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:PRK13538 80 ghqpgikTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|..
gi 227351261 156 TGALDSETSQEIMNLFkSLNQQEGTTIIMVTH 187
Cdd:PRK13538 157 FTAIDKQGVARLEALL-AQHAEQGGMVILTTH 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-217 |
7.48e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 7.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPI--HDY-TRKQfsslrnqnVGFVFQNFKLLRES 85
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLPAS-EGEAWLFGQPVdaGDIaTRRR--------VGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNValpLLYA---GKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSE 162
Cdd:NF033858 355 TVRQNL---ELHArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 163 TSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV-ISDSKEENQRA 217
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVlASDTPAALVAA 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-213 |
7.58e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.85 E-value: 7.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDddfegtyfyqdhpihdyTRKQFSSLRNQNVGFVFQnFKLLRE 84
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELP-----------------PRSDASVVIRGTVAYVPQ-VSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLY-AGKSRKEIngRVSE-----------TLKQVGLAGYeeqlpkNMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:PLN03130 693 ATVRDNILFGSPFdPERYERAI--DVTAlqhdldllpggDLTEIGERGV------NISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351261 153 DEPTGALDSETSQEIMNlfKSLNQQ-EGTTIIMVTHDPHVAEQCERVIKIIDGRVisdsKEE 213
Cdd:PLN03130 765 DDPLSALDAHVGRQVFD--KCIKDElRGKTRVLVTNQLHFLSQVDRIILVHEGMI----KEE 820
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
8-213 |
7.80e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDfEGTYFYQDHPIHdytrkqfSSLRNQNVGFVFQN------FK 80
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKaLMGFVRLA-SGKISILGQPTR-------QALQKNLVAYVPQSeevdwsFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PRK15056 95 VLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 227351261 161 SETSQEIMNLFKSLnQQEGTTIIMVTHD-PHVAEQCERVIkIIDGRVISDSKEE 213
Cdd:PRK15056 175 VKTEARIISLLREL-RDEGKTMLVSTHNlGSVTEFCDYTV-MVKGTVLASGPTE 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-187 |
9.85e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 9.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDFEGTYFYQDHPIHDYTRKQ-FSSLRNQNVGFVFQN-FKLLR 83
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmRFYDLKNDHHIVFKNEHTNDMTNEQdYQGDEEQNVGMKNVNeFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVAL--------------------------------PLLYAGKSRKEIN-GRVSETLKQVGLAG-------YEE 123
Cdd:PTZ00265 1263 EGGSGEDSTVfknsgkilldgvdicdynlkdlrnlfsivsqePMLFNMSIYENIKfGKEDATREDVKRACkfaaideFIE 1342
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 124 QLP-----------KNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTH 187
Cdd:PTZ00265 1343 SLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1-217 |
1.16e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.93 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVlHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYT----RKQFSSlrnqnvgfVF 76
Cdd:PRK10522 333 QDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQpedyRKLFSA--------VF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 77 QNFKLLR-----ESTVADNVA----LPLLYAGKSRKEINGRVSETlkqvglagyeeqlpkNMSGGQQQRVSIARAISTHP 147
Cdd:PRK10522 404 TDFHLFDqllgpEGKPANPALvekwLERLKMAHKLELEDGRISNL---------------KLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 148 QFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISDSKEENQRA 217
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAA 538
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-208 |
1.85e-14 |
|
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: 69.36 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTyfyqdhpIH----DYTRKQFSSLRNQnVGFVFQNFKLL 82
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGK-------IEidgiDISTIPLEDLRSS-LTIIPQDPTLF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 rESTVADNVALpllYAGKSRKEING--RVSETlkqvGLagyeeqlpkNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:cd03369 95 -SGTIRSNLDP---FDEYSDEEIYGalRVSEG----GL---------NLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 227351261 161 SETSQEIMNLFKSLNQqeGTTIIMVTHDPHVAEQCERVIKIIDGRVIS 208
Cdd:cd03369 158 YATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-211 |
1.93e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 18 GELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHdytrkqFSSLRN---QNVGFVFQNFKLLRESTVADNVAL 93
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLtGIYTRD-AGSILYLGKEVT------FNGPKSsqeAGIGIIHQELNLIPQLTIAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 94 PLLYAGK----SRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL-DSETSQeim 168
Cdd:PRK10762 103 GREFVNRfgriDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETES--- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 227351261 169 nLFKSLN--QQEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSK 211
Cdd:PRK10762 180 -LFRVIRelKSQGRGIVYISHRlKEIFEICDDVTVFRDGQFIAERE 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-187 |
2.44e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFH--------VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQD-HPIHDYTRKQFSSlrnqNVGF 74
Cdd:PTZ00265 389 RFHydtrkdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRS----KIGV 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 75 VFQNfKLLRESTVADNVALPLL-------------------YAGKS----------------------------RKEIN- 106
Cdd:PTZ00265 465 VSQD-PLLFSNSIKNNIKYSLYslkdlealsnyynedgndsQENKNkrnscrakcagdlndmsnttdsneliemRKNYQt 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 107 ---GRVSETLKQVGLAGYEEQLP-----------KNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFK 172
Cdd:PTZ00265 544 ikdSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
|
250
....*....|....*
gi 227351261 173 SLNQQEGTTIIMVTH 187
Cdd:PTZ00265 624 NLKGNENRITIIIAH 638
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
14-214 |
6.69e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 14 EIDQGELVAIIGESGSGKSTLIN-IIGFLddDFEGTYFYQDHPIHDYTRKQFSSLR-----NQNVGF---VFQNFKLlre 84
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLArMAGLL--PGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFampVFQYLTL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 stvadnvalpLLYAGKSRKEINGRVSETLKQVGLagyEEQLPKN---MSGGQQQRVSIA-------RAISTHPQFLIADE 154
Cdd:PRK03695 93 ----------HQPDKTRTEAVASALNEVAEALGL---DDKLGRSvnqLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351261 155 PTGALDseTSQEIMnLFKSLNQ--QEGTTIIMVTHD-PHVAEQCERVIKIIDGRVISDSKEEN 214
Cdd:PRK03695 160 PMNSLD--VAQQAA-LDRLLSElcQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-206 |
7.36e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.97 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDhpihdytrkqfsslrnqNVGFVFQNfKLLRESTV 87
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------------SVAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 88 ADNVALpllyaGKSRKEinGRVSETLKQVGLAGYEEQLPK-----------NMSGGQQQRVSIARAISTHPQFLIADEPT 156
Cdd:TIGR00957 716 RENILF-----GKALNE--KYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 157 GALDSETSQEIM-NLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:TIGR00957 789 SAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-189 |
9.66e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.88 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDD--FEGTYFYQDHPIHDYTRKQfsslrnqnVGFVFQNFKLLRES 85
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQRS--------TGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADnvalPLLYAGKSRkeingrvsetlkqvGLagyeeqlpknmSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03232 95 TVRE----ALRFSALLR--------------GL-----------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180
....*....|....*....|....
gi 227351261 166 EIMNLFKSLnQQEGTTIIMVTHDP 189
Cdd:cd03232 146 NIVRFLKKL-ADSGQAILCTIHQP 168
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-207 |
2.57e-13 |
|
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: 66.01 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GfldddfegtyfyqdHPIHDYTRkqfsslrnqnvGFVFQNFKLLRES 85
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImG--------------HPKYEVTE-----------GEILFKGEDITDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEING-RVSETLKQVGlagyeeqlpKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:cd03217 70 PPEERARLGIFLAFQYPPEIPGvKNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 165 QEIMNLFKSLNqQEGTTIIMVTHDPHVAEQCE--RVIKIIDGRVI 207
Cdd:cd03217 141 RLVAEVINKLR-EEGKSVLIITHYQRLLDYIKpdRVHVLYDGRIV 184
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
123-206 |
4.00e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.34 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 123 EQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEI---MNLFKslnqQEGTTIIMVTHD-PHVAEQCERV 198
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIyqlINQFK----AEGLSIILVSSEmPEVLGMSDRI 465
|
....*...
gi 227351261 199 IKIIDGRV 206
Cdd:PRK10762 466 LVMHEGRI 473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-160 |
5.05e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.97 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFsslRNQNVGFV---FQNFKLLR 83
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER---RRLGVAYIpedRLGRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNVALPLLYAGK-------SRKEINGRVSETLKQ--VGLAGyEEQLPKNMSGGQQQRVSIARAISTHPQFLIADE 154
Cdd:COG3845 350 DMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEfdVRTPG-PDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
....*.
gi 227351261 155 PTGALD 160
Cdd:COG3845 429 PTRGLD 434
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-188 |
5.06e-13 |
|
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: 67.27 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDhpihdytrkqfsslrNQNVGFVFQNFKLLRES 85
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP---------------GIKVGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVAL---PLLYAGKSRKEIN-----------------GRVSETLKQVGLAGYEEQL---------P------KNMS 130
Cdd:TIGR03719 84 TVRENVEEgvaEIKDALDRFNEISakyaepdadfdklaaeqAELQEIIDAADAWDLDSQLeiamdalrcPpwdadvTKLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 131 GGQQQRVSIARAISTHPQFLIADEPTGALDSETsqeIMNLFKSLNQQEGtTIIMVTHD 188
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPG-TVVAVTHD 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-212 |
7.38e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.47 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GfldddfegtyfyqdHPihDYTRKQFS-SLRNQNV------------ 72
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmG--------------HP--KYEVTSGSiLLDGEDIlelspderarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 73 -GFVFQ---------NFKLLResTVADNVALPLLYAGKSRKEINgrvsETLKQVGLAgyEEQLPKNM----SGGQQQRVS 138
Cdd:COG0396 79 iFLAFQypveipgvsVSNFLR--TALNARRGEELSAREFLKLLK----EKMKELGLD--EDFLDRYVnegfSGGEKKRNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 139 IARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLnQQEGTTIIMVTH--------DPHvaeqceRVIKIIDGRVI-SD 209
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHyqrildyiKPD------FVHVLVDGRIVkSG 223
|
...
gi 227351261 210 SKE 212
Cdd:COG0396 224 GKE 226
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
6-201 |
8.87e-13 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 63.88 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGF-----LDDDFEGTYFYQDHPIHDytrkQFSSLRNQNVGFvfqnfk 80
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYasgkaRLISFLPKFSRNKLIFID----QLQFLIDVGLGY------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 llrestvadnvaLPLlyagksrkeinGRVSETLkqvglagyeeqlpknmSGGQQQRVSIARAI--STHPQFLIADEPTGA 158
Cdd:cd03238 79 ------------LTL-----------GQKLSTL----------------SGGELQRVKLASELfsEPPGTLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 227351261 159 LDSETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDF 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
7-209 |
3.17e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLIniiGFLDDDF-----------EGTYFYQDHPIHDYTRKQFSSLR-----NQ 70
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLL---KALAGDLtgggaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 71 NVGFVFQnfkllrestvADNVALPLLY-----AGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAIS- 144
Cdd:PRK13547 93 QPAFAFS----------AREIVLLGRYpharrAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAq 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227351261 145 --------THPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQ-CERVIKIIDGRVISD 209
Cdd:PRK13547 163 lwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAH 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-209 |
4.16e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDFEGTYFYQDHPIHdyTRKQFSSLRNqNVGFVFQNFK---LL 82
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVK--IRNPQQAIAQ-GIAMVPEDRKrdgIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 RESTVADNVALPLL--YAGKSR----KEInGRVSETLKQVGLAGYEEQLP-KNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:PRK13549 354 PVMGVGKNITLAALdrFTGGSRiddaAEL-KTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 156 TGALDSETSQEIMNLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKIIDGRVISD 209
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSElPEVLGLSDRVLVMHEGKLKGD 486
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-207 |
4.43e-12 |
|
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: 62.67 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDF---EGTYFYQDHPIHDYTRKQFSSLrnqnvgfVFQ 77
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI-------IYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 78 NfkllrestvADNVALPLLyagksrkeingRVSETLKQVGLAGYEEQLpKNMSGGQQQRVSIARAISTHPQFLIADEPTG 157
Cdd:cd03233 89 S---------EEDVHFPTL-----------TVRETLDFALRCKGNEFV-RGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 158 ALDSETSQEIMNLFKSLNQQEGTTIIMVTHDP--HVAEQCERVIKIIDGRVI 207
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGRQI 199
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
101-211 |
7.20e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.60 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 101 SRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLnQQEGT 180
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGA 195
|
90 100 110
....*....|....*....|....*....|..
gi 227351261 181 TIIMVTHDPHVAEQCERVIKIID-GRVISDSK 211
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDrGRVIADGK 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-206 |
2.00e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.38 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFSSLrnqNVGFVFQNFKLLREST 86
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPLLFPNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKeingRVSETLKQVGLagyeeQLPKNMSGG-----QQQRVSIARAISTHPQFLIADEPTGALds 161
Cdd:PRK15439 103 VKENILFGLPKRQASMQ----KMKQLLAALGC-----QLDLDSSAGslevaDRQIVEILRGLMRDSRILILDEPTASL-- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 227351261 162 eTSQEIMNLFKSLN--QQEGTTIIMVTHD-PHVAEQCERVIKIIDGRV 206
Cdd:PRK15439 172 -TPAETERLFSRIRelLAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-206 |
3.45e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHdyTRKQFSSLRN---------QNVGFvFQNFK 80
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKgmayitesrRDNGF-FPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LLRESTVADNV-------ALPLL-------YAGKSRKEINGRVSETlkqvglagyeEQLPKNMSGGQQQRVSIARAISTH 146
Cdd:PRK09700 358 IAQNMAISRSLkdggykgAMGLFhevdeqrTAENQRELLALKCHSV----------NQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227351261 147 PQFLIADEPTGALDSETSQEIMNLFKSLnQQEGTTIIMVTHD-PHVAEQCERVIKIIDGRV 206
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-217 |
5.03e-11 |
|
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: 61.35 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 1 GSQRFHVlHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTYFYQDHPIHDYT----RKQFSSlrnqnvgfV 75
Cdd:COG4615 342 GDEGFTL-GPIDLTIRRGELVFIVGGNGSGKSTLAKLLtGLYRPE-SGEILLDGQPVTADNreayRQLFSA--------V 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 76 FQNF----KLL-RESTVADNVALPLLyagkSRKEI-------NGRVSETlkqvglagyeeqlpkNMSGGQQQRVSIARAI 143
Cdd:COG4615 412 FSDFhlfdRLLgLDGEADPARARELL----ERLELdhkvsveDGRFSTT---------------DLSQGQRKRLALLVAL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 144 STHPQFLIADEptGALDsetsQ----------EIMNLFKslnqQEGTTIIMVTHDPHVAEQCERVIKIIDGRVISDSKEE 213
Cdd:COG4615 473 LEDRPILVFDE--WAAD----QdpefrrvfytELLPELK----ARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPA 542
|
....
gi 227351261 214 NQRA 217
Cdd:COG4615 543 ALAA 546
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
4-201 |
5.79e-11 |
|
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: 59.96 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLIniigfLDDDF-EGTYFYQDhPIHDYTRKQFSSLRNQNVGF-------- 74
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSLA-----FDTIYaEGQRRYVE-SLSAYARQFLGQMDKPDVDSieglspai 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 75 -VFQNF--KLLReSTVAD----NVALPLLYAgksRKEINGRVsETLKQVGLaGY--EEQLPKNMSGGQQQRVSIARAIST 145
Cdd:cd03270 81 aIDQKTtsRNPR-STVGTvteiYDYLRLLFA---RVGIRERL-GFLVDVGL-GYltLSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 146 HPQFL--IADEPTGALDSETSQEIMNLFKSLnQQEGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:cd03270 155 GLTGVlyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-208 |
8.09e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDfEGTYFYQDHPIHDYTRKQfsSLRNqNVGFVFQNFKLLREST 86
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKcLFGIYQKD-SGSILFQGKEIDFKSSKE--ALEN-GISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVAL---PLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALdseT 163
Cdd:PRK10982 90 VMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---T 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 227351261 164 SQEIMNLFKSLNQ--QEGTTIIMVTHD-PHVAEQCERVIKIIDGRVIS 208
Cdd:PRK10982 167 EKEVNHLFTIIRKlkERGCGIVYISHKmEEIFQLCDEITILRDGQWIA 214
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
4-199 |
9.60e-11 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 59.55 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGF--------------LDDDFEGTYFYQDHPIH------------ 57
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYpalarrlhlkkeqpGNHDRIEGLEHIDKVIVidqspigrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 58 ---DYTrKQFSSLRNqnvgfVF----QNFKLLREStvadnvaLPLLYAGKSRKEI-----------------NGRVSETL 113
Cdd:cd03271 87 npaTYT-GVFDEIRE-----LFcevcKGKRYNRET-------LEVRYKGKSIADVldmtveealeffenipkIARKLQTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 114 KQVGLaGYEE--QLPKNMSGGQQQRVSIARAIS---THPQFLIADEPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHD 188
Cdd:cd03271 154 CDVGL-GYIKlgQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDK-GNTVVVIEHN 231
|
250
....*....|.
gi 227351261 189 PHVAEQCERVI 199
Cdd:cd03271 232 LDVIKCADWII 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
122-206 |
9.69e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 122 EEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQ-CERVIK 200
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQmADRVLV 475
|
....*.
gi 227351261 201 IIDGRV 206
Cdd:PRK15439 476 MHQGEI 481
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-206 |
1.03e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 5 FHVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYfyqdhpihdytrkqfssLRNQNVGFVFQNFKLLRE 84
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------------DRNGEVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETS 164
Cdd:PRK13546 100 LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 227351261 165 QEIMNLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKIIDGRV 206
Cdd:PRK13546 180 QKCLDKIYEFKEQ-NKTIFFVSHNlGQVRQFCTKIAWIEGGKL 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-206 |
1.76e-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: 59.96 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTrkqFSSLRNQnVGFVFQNfkllrest 86
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFK-ITIIPQD-------- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 vadnvalPLLYAGKSRKEIN--GRVSE-----TLKQVGLAGYEEQLP-----------KNMSGGQQQRVSIARAISTHPQ 148
Cdd:TIGR00957 1369 -------PVLFSGSLRMNLDpfSQYSDeevwwALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 149 FLIADEPTGALDSETSQEIMNLFKSlnQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-216 |
1.82e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 15 IDQGELVAIIGESGSGKSTLINIIG---FLDDdfeGTYFY-QDHPIhdyTRKQFSSLRNQNvGFVFqnfkllreSTVADN 90
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYeQDLIV---ARLQQDPPRNVE-GTVY--------DFVAEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 91 VA------------LPLLYAGKSRKEIN------------------GRVSETLKQVGLAGyeEQLPKNMSGGQQQRVSIA 140
Cdd:PRK11147 91 IEeqaeylkryhdiSHLVETDPSEKNLNelaklqeqldhhnlwqleNRINEVLAQLGLDP--DAALSSLSGGWLRKAALG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 141 RAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNqqegTTIIMVTHD-PHVAEQCERVIKIIDGRVIS---------DS 210
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ----GSIIFISHDrSFIRNMATRIVDLDRGKLVSypgnydqylLE 244
|
....*.
gi 227351261 211 KEENQR 216
Cdd:PRK11147 245 KEEALR 250
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-193 |
3.15e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDhpihdytrkqfsslrNQNVGFVFQNFKLLRES 85
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP---------------GIKVGYLPQEPQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNV--ALPLLYAGKSR-KEIN-----------------GRVSETLKQVGLAGYEEQL---------P------KNMS 130
Cdd:PRK11819 86 TVRENVeeGVAEVKAALDRfNEIYaayaepdadfdalaaeqGELQEIIDAADAWDLDSQLeiamdalrcPpwdakvTKLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 131 GGQQQRVSIARAISTHPQFLIADEPTGALDSETsqeIMNLFKSLNQQEGtTIIMVTHD----PHVAE 193
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG-TVVAVTHDryflDNVAG 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-204 |
4.04e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GfldddfegtyfyqDHP------IHDYTRKQFSSLR----NQNVGFV 75
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItG-------------DHPqgysndLTLFGRRRGSGETiwdiKKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 76 FQNFKL-LRESTVADNVALPL------LYAGKSRKEiNGRVSETLKQVGLAGYEEQLP-KNMSGGQQQRVSIARAISTHP 147
Cdd:PRK10938 342 SSSLHLdYRVSTSVRNVILSGffdsigIYQAVSDRQ-QKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHP 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 148 QFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQC--ERVIKIIDG 204
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPACitHRLEFVPDG 479
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-207 |
8.41e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDfEGT----------YFYQDHPiHDytrkqfsslrnqnvgfv 75
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELEPD-SGTvkwsenanigYYAQDHA-YD----------------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 76 FQNfkllrESTVADnvalpllYAGKSRKE---------INGRV----SETLKQVglagyeeqlpKNMSGGQQQRVSIARA 142
Cdd:PRK15064 395 FEN-----DLTLFD-------WMSQWRQEgddeqavrgTLGRLlfsqDDIKKSV----------KVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227351261 143 ISTHPQFLIADEPTGALDSEtSQEIMNLfkSLNQQEGtTIIMVTHD-PHVAEQCERVIKIIDGRVI 207
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDME-SIESLNM--ALEKYEG-TLIFVSHDrEFVSSLATRIIEITPDGVV 514
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-189 |
9.29e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 18 GELVAIIGESGSGKSTLINIigfLDDDFEGTYFYQDHPIHDYTRKQFSSLRnqNVGFVFQNFKLLRESTVADNV---ALP 94
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRPLDSSFQR--SIGYVQQQDLHLPTSTVRESLrfsAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 95 LLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGG----QQQRVSIARAISTHPQFLI-ADEPTGALDSETSQEIMN 169
Cdd:TIGR00956 864 RQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170 180
....*....|....*....|
gi 227351261 170 LFKSLnQQEGTTIIMVTHDP 189
Cdd:TIGR00956 944 LMRKL-ADHGQAILCTIHQP 962
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-167 |
2.30e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIgfldddfEGTYFYQDHPIHDYTRKQFSSlrnqnvgfvfqNFKLLREST 86
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI-------MGELEPSEGKIKHSGRISFSP-----------QTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAgksrkeiNGRVSETLKQVGLagyEEQLPK--------------NMSGGQQQRVSIARAISTHPQFLIA 152
Cdd:TIGR01271 503 IKDNIIFGLSYD-------EYRYTSVIKACQL---EEDIALfpekdktvlgeggiTLSGGQRARISLARAVYKDADLYLL 572
|
170
....*....|....*
gi 227351261 153 DEPTGALDSETSQEI 167
Cdd:TIGR01271 573 DSPFTHLDVVTEKEI 587
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
7-167 |
4.56e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.86 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLI-NIIGFLDDDfEGTyfyqdhpIHDYTRKQFSSlrnqnvgfvfqNFKLLRES 85
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELEPS-EGK-------IKHSGRISFSS-----------QFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEIngrVSETLKQVGLAGYEEQLPK-------NMSGGQQQRVSIARAISTHPQFLIADEPTGA 158
Cdd:cd03291 113 TIKENIIFGVSYDEYRYKSV---VKACQLEEDITKFPEKDNTvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
....*....
gi 227351261 159 LDSETSQEI 167
Cdd:cd03291 190 LDVFTEKEI 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-172 |
5.18e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 2 SQRFHVLHDINIEIDQGELVAIIGESGSGKSTLI-----NIIGFLDDDfEGTYFYQDHPIHDYtRKQFSSlrnqNVGFVF 76
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLktiasNTDGFHIGV-EGVITYDGITPEEI-KKHYRG----DVVYNA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 77 QNFKLLRESTVADNVALPLL-------YAGKSRKE-INGRVSETLKQVGLA-------GYEeqLPKNMSGGQQQRVSIAR 141
Cdd:TIGR00956 145 ETDVHFPHLTVGETLDFAARcktpqnrPDGVSREEyAKHIADVYMATYGLShtrntkvGND--FVRGVSGGERKRVSIAE 222
|
170 180 190
....*....|....*....|....*....|.
gi 227351261 142 AISTHPQFLIADEPTGALDSETSQEIMNLFK 172
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALK 253
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
6-206 |
1.02e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTyfyqdhpihdYTRKQFSSLRNQNVGFvfqNFKLlres 85
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT----------VDIKGSAALIAISSGL---NGQL---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 227351261 166 ---EIMNLFKslnqQEGTTIIMVTHD-PHVAEQCERVIKIIDGRV 206
Cdd:PRK13545 181 kclDKMNEFK----EQGKTIFFISHSlSQVKSFCTKALWLHYGQV 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-213 |
1.08e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDY----TRKQFSSLRNQNV---GFVFQNF 79
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFgltdLRRVLSIIPQSPVlfsGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLRESTVADnvalplLYAGKSRKEINGRVSETlkQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:PLN03232 1331 DPFSEHNDAD------LWEALERAHIKDVIDRN--PFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 160 DSETSQEIMNLFKSlnQQEGTTIIMVTHDPHVAEQCERVIKIIDGRVIS-DSKEE 213
Cdd:PLN03232 1403 DVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEyDSPQE 1455
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-188 |
1.17e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 18 GELVAIIGESGSGKSTLINII-GFLDDDFEGtyfYQDHPIHDYTRKQFSSLRNQNVgfvfqnFKLLRESTVADNVA---- 92
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILaGKLKPNLGK---FDDPPDWDEILDEFRGSELQNY------FTKLLEGDVKVIVKpqyv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 93 --LPLLYAGK-----SRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQ 165
Cdd:cd03236 97 dlIPKAVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|...
gi 227351261 166 EIMNLFKSLNqQEGTTIIMVTHD 188
Cdd:cd03236 177 NAARLIRELA-EDDNYVLVVEHD 198
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-162 |
1.21e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDYTRKQFsslrnqnVGFVFQNFKLLREST 86
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF-------MAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 87 VADNVALPLLYAGKSRKEINGrvsETLKQVGLAGYEEQLPKNMSGGQQQRVSIARA-ISTHPQFLIaDEPTGALDSE 162
Cdd:PRK13543 99 TLENLHFLCGLHGRRAKQMPG---SALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYANLDLE 171
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-187 |
1.24e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINII-GFLDDDF-EGTYFYQDHPIHDYTRKQFSSLRnqnvgfVFQNFKLLRE 84
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaGHPAYKIlEGDILFKGESILDLEPEERAHLG------IFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 85 STVADNVALpLLYAGKSRKEINGR-----------VSETLKQVGLAgyEEQLPKNM----SGGQQQRVSIARAISTHPQF 149
Cdd:CHL00131 96 IPGVSNADF-LRLAYNSKRKFQGLpeldplefleiINEKLKLVGMD--PSFLSRNVnegfSGGEKKRNEILQMALLDSEL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 227351261 150 LIADEPTGALDSETSQEIMNLFKSLNQQEgTTIIMVTH 187
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSE-NSIILITH 209
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-206 |
1.41e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.70 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINiiGFL-------DDDFEGTYfYQDHPIHDYtRKQFSSLrNQNVgFVFQnf 79
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLS--AFLrllntegDIQIDGVS-WNSVPLQKW-RKAFGVI-PQKV-FIFS-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 kllreSTVADNVAlPllYAGKSRKEInGRVSEtlkQVGLAGYEEQLPKNM-----------SGGQQQRVSIARAISTHPQ 148
Cdd:cd03289 91 -----GTFRKNLD-P--YGKWSDEEI-WKVAE---EVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 149 FLIADEPTGALDSETSQEIMnlfKSLNQQ-EGTTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIR---KTLKQAfADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-196 |
1.58e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.25 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 18 GELVAIIGESGSGKSTLINIigfLDDDFEGTYfyqdhpiHDYTRKQFSSLRN-----QNVGFVFQNFKLLRESTVADNVA 92
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKM---LTGDTTVTS-------GDATVAGKSILTNisdvhQNMGYCPQFDAIDDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 93 LPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFK 172
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180
....*....|....*....|....
gi 227351261 173 SLnQQEGTTIIMVTHDphvAEQCE 196
Cdd:TIGR01257 2115 SI-IREGRAVVLTSHS---MEECE 2134
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
6-201 |
2.52e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.68 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLIN------IIGFLDDDFEGTYFYQDHPIH---------------------- 57
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpaVEEFIEQGFCSNLSIQWGAISrlvhitrdlpgrsqrsipltyi 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 58 ---DYTRKQFSSL-RNQNVGFVFQNFKL------------LRESTVADN----------------VALPLLYAGKSRKEI 105
Cdd:PRK00635 689 kafDDLRELFAEQpRSKRLGLTKSHFSFntplgacaecqgLGSITTTDNrtsipcpsclgkrflpQVLEVRYKGKNIADI 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 106 NGRVS-----------------ETLKQVGLagyeEQLP-----KNMSGGQQQRVSIAR---AISTHPQFLIADEPTGALD 160
Cdd:PRK00635 769 LEMTAyeaekffldepsihekiHALCSLGL----DYLPlgrplSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLH 844
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 227351261 161 SETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:PRK00635 845 THDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-188 |
2.72e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 17 QGELVAIIGESGSGKSTLINII-GFLDDDFEGtyfYQDHPIHDYTRKQFSslrnqnvGFVFQN-FKLLRESTVadNVALP 94
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILsGELIPNLGD---YEEEPSWDEVLKRFR-------GTELQNyFKKLYNGEI--KVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 95 LLYAGKSRKEINGRVSETLKQVGLAGYEEQLPK-------------NMSGGQQQRVSIARAISTHPQFLIADEPTGALDS 161
Cdd:PRK13409 166 PQYVDLIPKVFKGKVRELLKKVDERGKLDEVVErlglenildrdisELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*..
gi 227351261 162 ETSQEIMNLFKSLnqQEGTTIIMVTHD 188
Cdd:PRK13409 246 RQRLNVARLIREL--AEGKYVLVVEHD 270
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
123-206 |
3.15e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 123 EQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHD-PHVAEQCERVIKI 201
Cdd:PRK11288 391 EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDlPEVLGVADRIVVM 469
|
....*
gi 227351261 202 IDGRV 206
Cdd:PRK11288 470 REGRI 474
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
17-207 |
3.21e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 17 QGELVAIIGESGSGKSTLINIIGFLdddfegtyfyqdhpihdytrkqfsslrnqnvgfvfqnfkllrestvadnvalpLL 96
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE-----------------------------------------------------LG 27
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 97 YAGKSRKEING-RVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIM-----NL 170
Cdd:smart00382 28 PPGGGVIYIDGeDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRL 107
|
170 180 190
....*....|....*....|....*....|....*..
gi 227351261 171 FKSLNQQEGTTIIMVTHDPHVAEqcERVIKIIDGRVI 207
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLG--PALLRRRFDRRI 142
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
7-206 |
3.60e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHPIHDY----TRKQFSSLRNQNVGFvfqnfkll 82
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYglreLRRQFSMIPQDPVLF-------- 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 83 rESTVADNVAlPLLYAgkSRKEingrVSETLKQVGL----AGYEEQLPK-------NMSGGQQQRVSIARA-ISTHPQFL 150
Cdd:PTZ00243 1397 -DGTVRQNVD-PFLEA--SSAE----VWAALELVGLrervASESEGIDSrvleggsNYSVGQRQLMCMARAlLKKGSGFI 1468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 151 IADEPTG----ALDSETSQEIMNLFKSLnqqegtTIIMVTHDPHVAEQCERVIKIIDGRV 206
Cdd:PTZ00243 1469 LMDEATAnidpALDRQIQATVMSAFSAY------TVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
4-199 |
6.98e-08 |
|
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: 52.32 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINII------GFLD---------DDFEGT-------YFYQDhPI----- 56
Cdd:TIGR00630 620 RENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTlypalaNRLNgaktvpgryTSIEGLehldkviHIDQS-PIgrtpr 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 57 ---------HDYTRKQFSSL-----RNQNVG-FVFqNFKLLR-ESTVADNV--------------------------ALP 94
Cdd:TIGR00630 699 snpatytgvFDEIRELFAETpeakvRGYTPGrFSF-NVKGGRcEACQGDGVikiemhflpdvyvpcevckgkrynreTLE 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 95 LLYAGKSRKEI-----------------NGRVSETLKQVGLaGYEE--QLPKNMSGGQQQRVSIARAIS---THPQFLIA 152
Cdd:TIGR00630 778 VKYKGKNIADVldmtveeayeffeavpsISRKLQTLCDVGL-GYIRlgQPATTLSGGEAQRIKLAKELSkrsTGRTLYIL 856
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 227351261 153 DEPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQCERVI 199
Cdd:TIGR00630 857 DEPTTGLHFDDIKKLLEVLQRLVDK-GNTVVVIEHNLDVIKTADYII 902
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
129-215 |
7.49e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 129 MSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDGRV-- 206
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVag 471
|
....*....
gi 227351261 207 ISDSKEENQ 215
Cdd:PRK10982 472 IVDTKTTTQ 480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-201 |
8.52e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLIN-IIGFLDDDFE----GTYFyqDHPIHDYTRKQFSSLrNQNVgFVFQnfkl 81
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSaLLRLLSTEGEiqidGVSW--NSVTLQTWRKAFGVI-PQKV-FIFS---- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 82 lreSTVADNVAlPllYAGKSRKEInGRVSEtlkQVGLAGYEEQLPKNM-----------SGGQQQRVSIARAISTHPQFL 150
Cdd:TIGR01271 1306 ---GTFRKNLD-P--YEQWSDEEI-WKVAE---EVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 151 IADEPTGALDSETSQEIMnlfKSLNQQ-EGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIR---KTLKQSfSNCTVILSEHRVEALLECQQFLVI 1424
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
13-202 |
1.21e-07 |
|
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: 50.30 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 13 IEIDQGeLVAIIGESGSGKSTLINII--GFLDDDFEGTYFYQDHPihDYTRKQFSSLRnqnVGFVFQN-----FKLLRES 85
Cdd:cd03240 18 IEFFSP-LTLIVGQNGAGKTTIIEALkyALTGELPPNSKGGAHDP--KLIREGEVRAQ---VKLAFENangkkYTITRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALplLYAGKSRKEIngrvsetlkqvglagyeEQLPKNMSGGQQQ------RVSIARAISTHPQFLIADEPTGAL 159
Cdd:cd03240 92 AILENVIF--CHQGESNWPL-----------------LDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 160 DSET-SQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKII 202
Cdd:cd03240 153 DEENiEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-188 |
1.40e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 17 QGELVAIIGESGSGKSTLINII--------GFLDDD---------FEGTyfyqdhPIHDYtrkqFSSLRNQNVgfvfqnf 79
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILsgelkpnlGDYDEEpswdevlkrFRGT------ELQDY----FKKLANGEI------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 kllrestvadNVALPLLYAGKSRKEINGRVSETLKQVG----LAGYEEQLP---------KNMSGGQQQRVSIARAISTH 146
Cdd:COG1245 161 ----------KVAHKPQYVDLIPKVFKGTVRELLEKVDergkLDELAEKLGlenildrdiSELSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 227351261 147 PQFLIADEPTGALDSETSQEIMNLFKSLnQQEGTTIIMVTHD 188
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHD 271
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
14-188 |
1.53e-07 |
|
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: 50.48 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 14 EIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGTyfyqdhpihdytrkqfSSLRNQNVGFVFQNFKLLRESTVADnva 92
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLaGVLKPD-EGD----------------IEIELDTVSYKPQYIKADYEGTVRD--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 93 lpLLYA-GKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSEtsQEIM--N 169
Cdd:cd03237 81 --LLSSiTKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE--QRLMasK 156
|
170
....*....|....*....
gi 227351261 170 LFKSLNQQEGTTIIMVTHD 188
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHD 175
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-213 |
3.92e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFyqdhpIHDYTRKQF--SSLRNqNVGFVFQ------- 77
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL-----IDGCDISKFglMDLRK-VLGIIPQapvlfsg 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 78 ----NFKLLRESTVADnvalplLYAGKSR---KEINGRVSETLK-QVGLAGyeeqlpKNMSGGQQQRVSIARAISTHPQF 149
Cdd:PLN03130 1328 tvrfNLDPFNEHNDAD------LWESLERahlKDVIRRNSLGLDaEVSEAG------ENFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227351261 150 LIADEPTGALDSET----SQEIMNLFKSlnqqegTTIIMVTHDPHVAEQCERVIKIIDGRVIS-DSKEE 213
Cdd:PLN03130 1396 LVLDEATAAVDVRTdaliQKTIREEFKS------CTMLIIAHRLNTIIDCDRILVLDAGRVVEfDTPEN 1458
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
7-205 |
9.52e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.59 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTyfyqdhpihdytrkqFSSLRNQNVGFVFQNFKLLReST 86
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR---------------LTKPAKGKLFYVPQRPYMTL-GT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 VADNVALPLLYAGKSRKEINGRVSET-LKQVGLagyEEQLPKNM------------SGGQQQRVSIARAISTHPQFLIAD 153
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKDLEQiLDNVQL---THILEREGgwsavqdwmdvlSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 227351261 154 EPTGALDSETSQEIMNLFKSLnqqeGTTIIMVTHDPHVAEQCERVIKiIDGR 205
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREF----GITLFSVSHRKSLWKYHEYLLY-MDGR 654
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
13-188 |
1.14e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 47.31 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 13 IEIDQGeLVAIIGESGSGKSTLINIIGF-LDDDFEGTYFYQDHPIHD------------YTRKQFSSLRNQNVgfvFQNF 79
Cdd:COG0419 19 IDFDDG-LNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVgseeasvelefeHGGKRYRIERRQGE---FAEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 80 KLLRESTVADNVA----LPLLYAGKSR-KEINGRVSETLKQVG-LAGYEEQL---------PKNMSGGQQQRVSIARAIS 144
Cdd:COG0419 95 LEAKPSERKEALKrllgLEIYEELKERlKELEEALESALEELAeLQKLKQEIlaqlsgldpIETLSGGERLRLALADLLS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 227351261 145 thpqfLIADepTGALDSETSQEIMNLFKSLNqqegttiiMVTHD 188
Cdd:COG0419 175 -----LILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
12-211 |
1.50e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 47.66 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 12 NIEIDQGELVAIIGESGSGKSTLINII-GFLDDDF-----EGTYFYQDHPihdYTRKQFSSLRNQNVGFV-----FQNFK 80
Cdd:COG4938 14 EAELELKPLTLLIGPNGSGKSTLIQALlLLLQSNFiylpaERSGPARLYP---SLVRELSDLGSRGEYTAdflaeLENLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 81 LL--RESTVADNVALPLLYAGKSRKEINGRVSETLKQVGLAGYEEQLP-KNMSGGQQQRVSI---ARAISTHPQFLIADE 154
Cdd:COG4938 91 ILddKSKELLEQVEEWLEKIFPGKVEVDASSDLVRLVFRPSGNGKRIPlSNVGSGVSELLPIllaLLSAAKPGSLLIIEE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 227351261 155 PTGALDSETSQEIMNLF-KSLNqqEGTTIIMVTHDPHVAEQCERVIKiiDGRVISDSK 211
Cdd:COG4938 171 PEAHLHPKAQSALAELLaELAN--SGVQVIIETHSDYILNGLRNLIK--EGKLLDPDD 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-214 |
1.62e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.60 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFYQDHpihDYTRKQFSSLRNQnVGFVFQNfkllrest 86
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI---DISKLPLHTLRSR-LSIILQD-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 87 vadnvalPLLYAGKSR-------KEINGRVSETLKQVGLAGYEEQLP-----------KNMSGGQQQRVSIARAISTHPQ 148
Cdd:cd03288 104 -------PILFSGSIRfnldpecKCTDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 149 FLIADEPTGALDSET----SQEIMNLFKSlnqqegTTIIMVTHDPHVAEQCERVIKIIDGRVISDSKEEN 214
Cdd:cd03288 177 ILIMDEATASIDMATenilQKVVMTAFAD------RTVVTIAHRVSTILDADLVLVLSRGILVECDTPEN 240
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
105-201 |
3.47e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 105 INGRVSeTLKQVGLaGY--EEQLPKNMSGGQQQRVSIARAISTHPQFL--IADEPTGALDSETSQEIMNLFKSLNQQeGT 180
Cdd:PRK00635 453 LKSRLS-ILIDLGL-PYltPERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GN 529
|
90 100
....*....|....*....|.
gi 227351261 181 TIIMVTHDPHVAEQCERVIKI 201
Cdd:PRK00635 530 TVLLVEHDEQMISLADRIIDI 550
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
4-191 |
3.62e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTLINIigfLDDDFEGTYFYQDHPIHDYTRKQFSSLRNQnvGFVFQNFKLLR 83
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISGFPKKQETFARIS--GYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 84 ESTVADNvalpLLYAGKSR--KEINGR-----VSETLKQVGLAGYEEQ---LP--KNMSGGQQQRVSIARAISTHPQFLI 151
Cdd:PLN03140 967 QVTVRES----LIYSAFLRlpKEVSKEekmmfVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 152 ADEPTGALDSETSQEIMNLFKSlNQQEGTTIIMVTHDPHV 191
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSI 1081
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
8-36 |
8.47e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.83 E-value: 8.47e-06
10 20
....*....|....*....|....*....
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLIN 36
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
10-206 |
1.81e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 10 DINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGTYFyqdhpihdytrkqfsslRNQNVGF-VFQNFKLlrestva 88
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------------RSAKVRMaVFSQHHV------- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 89 DNVAL---PLLYAGKSRKEI-NGRVSETLKQVGLAGYEEQLPK-NMSGGQQQRVSIARAISTHPQFLIADEPTGALDSET 163
Cdd:PLN03073 583 DGLDLssnPLLYMMRCFPGVpEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 227351261 164 SQEIMN---LFkslnqQEGttIIMVTHDPH-VAEQCERVIKIIDGRV 206
Cdd:PLN03073 663 VEALIQglvLF-----QGG--VLMVSHDEHlISGSVDELWVVSEGKV 702
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
6-36 |
2.73e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 2.73e-05
10 20 30
....*....|....*....|....*....|.
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLIN 36
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-210 |
3.18e-05 |
|
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: 44.00 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 14 EIDQGELVAIIGESGSGKSTLINII--------GFLDDDFEGTYFYQdHPIHDYtrkqfsslrnqnvgfvfqnfkllrES 85
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILagvlkpdeGEVDEDLKISYKPQ-YISPDY------------------------DG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNValpllyagksRKEINGRV------SETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGAL 159
Cdd:COG1245 417 TVEEFL----------RSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 227351261 160 DSETSQEIMNLFKSLNQQEGTTIIMVTHDphvaeqcervIKIIDgrVISDS 210
Cdd:COG1245 487 DVEQRLAVAKAIRRFAENRGKTAMVVDHD----------IYLID--YISDR 525
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
128-204 |
3.31e-05 |
|
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: 42.94 E-value: 3.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227351261 128 NMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQEGTTIIMVTHDPHVAEQCERVIKIIDG 204
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-210 |
4.23e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 14 EIDQGELVAIIGESGSGKSTLINII-GFLDDDfEGtyfyqdhpihdytrKQFSSLRnqnVGFVFQNFKLLRESTVADnva 92
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLaGVLKPD-EG--------------EVDPELK---ISYKPQYIKPDYDGTVED--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 93 lpLLYAGKSRKEINGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSEtsQEIM--NL 170
Cdd:PRK13409 420 --LLRSITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAvaKA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 227351261 171 FKSLNQQEGTTIIMVTHDphvaeqcervIKIIDgrVISDS 210
Cdd:PRK13409 496 IRRIAEEREATALVVDHD----------IYMID--YISDR 523
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
6-193 |
6.03e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLdddfEGTYFYQDHPIHDYTRKQFSSLrnQNVGFVFqnfkllres 85
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLA----LGGAQSATRRRSGVKAGCIVAA--VSAELIF--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 tvadnvalpllyagksrkeingrvseTLKQvglagyeeqlpknMSGGQQQRVSIARAISTHP----QFLIADEPTGALDS 161
Cdd:cd03227 74 --------------------------TRLQ-------------LSGGEKELSALALILALASlkprPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|..
gi 227351261 162 ETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAE 193
Cdd:cd03227 115 RDGQALAEAILEHLVK-GAQVIVITHLPELAE 145
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
102-213 |
1.48e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 102 RKEINGRVSETLKQVGlagyeeqlpkNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSLNQQeGTT 181
Cdd:NF040905 388 RKKMNIKTPSVFQKVG----------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKG 456
|
90 100 110
....*....|....*....|....*....|....
gi 227351261 182 IIMVTHD-PHVAEQCERVIKIIDGRVISD-SKEE 213
Cdd:NF040905 457 VIVISSElPELLGMCDRIYVMNEGRITGElPREE 490
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
8-216 |
2.12e-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: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGeLVAIIGESGSGKSTLINIIGFLDDDFEGTYFYqdhpIHDYTRKQFSSLRNQNVGFVFQNF--KLLREs 85
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFD----EEDFYLGDDPDLPEIEIELTFGSLlsRLLRL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 86 TVADNVALPLLYAGKSR--------KEINGRVSETLKQ------------------------VGLAGYEEQLPKNMSGGQ 133
Cdd:COG3593 88 LLKEEDKEELEEALEELneelkealKALNELLSEYLKElldgldlelelsldeledllkslsLRIEDGKELPLDRLGSGF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 134 QQRVSIA------RAISTHPQFLIA-DEPtgaldsETSQE---IMNLFKSLNQ--QEGTTIIMVTHDPHVAEQC--ERVI 199
Cdd:COG3593 168 QRLILLAllsalaELKRAPANPILLiEEP------EAHLHpqaQRRLLKLLKElsEKPNQVIITTHSPHLLSEVplENIR 241
|
250 260
....*....|....*....|....
gi 227351261 200 -------KIIDGRVISDSKEENQR 216
Cdd:COG3593 242 rlrrdsgGTTSTKLIDLDDEDLRK 265
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-185 |
2.18e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 8 LHDINIEIDQGELVAIIGESGSGKSTLINII--------GFLDDDFegtyfyqDHPihdyTRKQFSSLRnQNVGFVFQ-- 77
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALagelpllsGERQSQF-------SHI----TRLSFEQLQ-KLVSDEWQrn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 78 NFKLLreSTVADNValpllyaGKSRKEI-------NGRVSETLKQVGLAGYEEQLPKNMSGGQQQRVSIARAISTHPQFL 150
Cdd:PRK10938 87 NTDML--SPGEDDT-------GRTTAEIiqdevkdPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 227351261 151 IADEPTGALDSETSQEIMNLFKSLNQQeGTTIIMV 185
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
111-201 |
3.31e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 111 ETLKQVGLaGYeeqLP--KNMSG---GQQQRVSIARAI---STHPQFLIADEPTGALDSETSQEIMNLFKSLNQQeGTTI 182
Cdd:PRK00635 1681 QALIDNGL-GY---LPlgQNLSSlslSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSL-GHSV 1755
|
90
....*....|....*....
gi 227351261 183 IMVTHDPHVAEQCERVIKI 201
Cdd:PRK00635 1756 IYIDHDPALLKQADYLIEM 1774
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
4-34 |
4.27e-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: 40.77 E-value: 4.27e-04
10 20 30
....*....|....*....|....*....|.
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTL 34
Cdd:TIGR00630 8 REHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
6-35 |
5.11e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 5.11e-04
10 20 30
....*....|....*....|....*....|
gi 227351261 6 HVLHDINIEIDQGELVAIIGESGSGKSTLI 35
Cdd:pfam13555 10 GTFDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
4-34 |
7.14e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 7.14e-04
10 20 30
....*....|....*....|....*....|.
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTL 34
Cdd:COG0178 12 REHNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| p47_IIGP_like |
cd04104 |
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ... |
21-47 |
8.13e-04 |
|
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase family consists of several highly homologous proteins, including IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1. They are found in higher eukaryotes where they play a role in immune resistance against intracellular pathogens. p47 proteins exist at low resting levels in mouse cells, but are strongly induced by Type II interferon (IFN-gamma). ITGP is critical for resistance to Toxoplasma gondii infection and in involved in inhibition of Coxsackievirus-B3-induced apoptosis. TGTP was shown to limit vesicular stomatitis virus (VSV) infection of fibroblasts in vitro. IRG-47 is involved in resistance to T. gondii infection. LRG-47 has been implicated in resistance to T. gondii, Listeria monocytogenes, Leishmania, and mycobacterial infections. IIGP1 has been shown to localize to the ER and to the Golgi membranes in IFN-induced cells and inflamed tissues. In macrophages, IIGP1 interacts with hook3, a microtubule binding protein that participates in the organization of the cis-Golgi compartment.
Pssm-ID: 206690 Cd Length: 197 Bit Score: 38.85 E-value: 8.13e-04
10 20
....*....|....*....|....*..
gi 227351261 21 VAIIGESGSGKSTLINIIGFLDDDFEG 47
Cdd:cd04104 4 IAVTGESGAGKSSFINALRGIGHEEEG 30
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
62-201 |
1.59e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 62 KQFSSLRNQNVGFVFQNFKLLRESTVADNVALPLLyagksrKEINGRVSeTLKQVGLaGY--EEQLPKNMSGGQQQRVSI 139
Cdd:TIGR00630 428 KSIADVSELSIREAHEFFNQLTLTPEEKKIAEEVL------KEIRERLG-FLIDVGL-DYlsLSRAAGTLSGGEAQRIRL 499
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227351261 140 ARAISTHPQ--FLIADEPTGALDSETSQEIMNLFKSLNQQeGTTIIMVTHDPHVAEQCERVIKI 201
Cdd:TIGR00630 500 ATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDL-GNTLIVVEHDEDTIRAADYVIDI 562
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-41 |
1.62e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 1.62e-03
10 20 30
....*....|....*....|....*....|....*....
gi 227351261 3 QRFHVLHDINIEIdqGELVAIIGESGSGKSTLINIIGFL 41
Cdd:COG4637 8 KNFKSLRDLELPL--GPLTVLIGANGSGKSNLLDALRFL 44
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
4-34 |
2.40e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 2.40e-03
10 20 30
....*....|....*....|....*....|.
gi 227351261 4 RFHVLHDINIEIDQGELVAIIGESGSGKSTL 34
Cdd:PRK00349 12 REHNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
105-188 |
2.91e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.23 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 105 INGRVSETLKQVGLAGYEEQLP-KNMSGGQQQRVSIARAISTHPQFLIADEPTGALDSETsqeIMNLFKSLNQQEGtTII 183
Cdd:PRK10636 125 IRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQG-TLI 200
|
....*
gi 227351261 184 MVTHD 188
Cdd:PRK10636 201 LISHD 205
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
136-198 |
3.05e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.21 E-value: 3.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227351261 136 RVSIARAISTHPQFLIADEPTGALDSETSQEIMNLFKSL--NQQegttIIMVTHDPHVAEQCERV 198
Cdd:COG4717 572 RLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELakGRQ----VIYFTCHEELVELFQEE 632
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-160 |
3.17e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 3.17e-03
10 20 30
....*....|....*....|....*....|....
gi 227351261 127 KNMSGGQQQRVSIARAISTHPQFLIADEPTGALD 160
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-191 |
5.15e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 7 VLHDINIEIDQGELVAIIGESGSGKSTLINIIGFLDDDFEGT----------YFYQdhpihdytrKQFSSLRnqnvgfvf 76
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiglakgiklgYFAQ---------HQLEFLR-------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351261 77 qnfkllrestvADNVALPLLyAGKSRKEINGRVSETLKQVGLAGYE-EQLPKNMSGGQQQRVSIARAISTHPQFLIADEP 155
Cdd:PRK10636 390 -----------ADESPLQHL-ARLAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 227351261 156 TGALDSETSQEimnLFKSLNQQEGtTIIMVTHDPHV 191
Cdd:PRK10636 458 TNHLDLDMRQA---LTEALIDFEG-ALVVVSHDRHL 489
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
15-46 |
7.49e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 36.30 E-value: 7.49e-03
10 20 30
....*....|....*....|....*....|....
gi 227351261 15 IDQGE-LVAIIGESGSGKSTLIN-IIGFLDDDFE 46
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRrLLERLPDDVK 72
|
|
| |
