|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-218 |
6.57e-108 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 309.28 E-value: 6.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRFKSVGFILQASNLIPFLTVQQQLELVDHLTGSKEK---AKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKerrERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-218 |
1.10e-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: 285.92 E-value: 1.10e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 FKSVGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKkerRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-218 |
2.65e-73 |
|
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: 221.92 E-value: 2.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRFKSVGFILQASNLIPFLT----VQQQLELVdhltGSKE-KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALY 156
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTalenVMLPLELA----GRRDaRARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 157 HDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-218 |
1.64e-69 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 212.99 E-value: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:COG3638 1 PMLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRfKSVGFILQASNLIPFLTVqqqLELVdhLTG----------------SKEKAKANQLFDDLGITGLKHQLPQELSGGE 145
Cdd:COG3638 78 LR-RRIGMIFQQFNLVPRLSV---LTNV--LAGrlgrtstwrsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 146 RQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQvDLARRYADRIIGLRDGRV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-218 |
7.72e-67 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 205.29 E-value: 7.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RFKsVGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRkeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDRMLKYCDK-VYRMQDGEL 218
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELL-EEINRRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-218 |
1.51e-65 |
|
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: 201.97 E-value: 1.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERsRL 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RFKSVGFILQ--ASNLIPFLTVQQQLE--LVDHLTGSKEKAKANQLFDDLGITGLK----HQLPQELSGGERQRAAIARA 154
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPeevlNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 155 LYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKY-CDKVYRMQDGEL 218
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-219 |
1.73e-64 |
|
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: 199.09 E-value: 1.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfKSVGFILQASNLIPFLT----VQQQLELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTarqnVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELC 219
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-218 |
7.56e-64 |
|
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: 197.57 E-value: 7.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RFKSVGFILQASNLIPFLTVqqqLELVDH--LTGSKEKAKANQL-FDDLGITGLKHQL---PQELSGGERQRAAIARALY 156
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTA---LENVAMplLIGKKSVKEAKERaYEMLEKVGLEHRInhrPSELSGGERQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 157 HDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-200 |
1.00e-60 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 190.69 E-value: 1.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKers 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfksVGFILQASNLIPFLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYH 157
Cdd:COG1116 82 ------RGVVFQEPALLPWLTVLDNVALgleLRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499604739 158 DPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-217 |
1.38e-60 |
|
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: 189.70 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLR 83
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNLIPFLTVqqqLELVdhLTGS----------------KEKAKANQLFDDLGITGLKHQLPQELSGGERQ 147
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSV---LENV--LSGRlgrrstwrslfglfpkEEKQRALAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 148 RAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQvDLAREYADRIVGLKDGR 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-218 |
3.02e-60 |
|
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: 196.66 E-value: 3.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTF-QDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:COG1123 260 LLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRfKSVGFILQ--ASNLIPFLTVQQQLE--LVDHLTGSKE--KAKANQLFDDLGI-TGLKHQLPQELSGGERQRAAIARA 154
Cdd:COG1123 340 LR-RRVQMVFQdpYSSLNPRMTVGDIIAepLRLHGLLSRAerRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 155 LYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRI 483
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-218 |
7.51e-59 |
|
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: 185.63 E-value: 7.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 16 GHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGgLQTPSSGQLIIDGTDYTHLSEKERSRLrfksVGFILQAS 94
Cdd:COG1120 12 GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLrALAG-LLKPSSGEVLLDGRDLASLSRRELARR----IAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 NLIPFLTVqqqLELV-----DHLT-----GSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILA 164
Cdd:COG1120 85 PAPFGLTV---RELValgryPHLGlfgrpSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 165 DEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDlNLAARYADRLVLLKDGRI 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-200 |
1.83e-57 |
|
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: 181.13 E-value: 1.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRlr 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP---VTGPGPDR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksvGFILQASNLIPFLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03293 76 ----GYVFQQDALLPWLTVLDNVALgleLQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-221 |
5.81e-57 |
|
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: 180.47 E-value: 5.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfKSVGFILQASNLIPFLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALpleIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEVVEE 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-218 |
1.46e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 182.58 E-value: 1.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGgLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrCINL-LERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfKSVGFILQASNLIPFLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALpleIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDdrM---LKYCDKVYRMQDGEL 218
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE--MdvvRRICDRVAVLENGRI 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-218 |
7.99e-56 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 178.07 E-value: 7.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHlsekERSRLR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR----RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 FKSVGFILQ--ASNLIPFLTVQQQLELVDHLTGSKE-KAKANQLFDDLGIT-GLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:COG1124 78 RRRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDrEERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKY-CDKVYRMQDGEL 218
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-217 |
8.77e-56 |
|
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: 176.50 E-value: 8.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTktFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfk 85
Cdd:cd03225 2 LKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 sVGFILQASNL-IPFLTVQQQLELV---DHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPAL 161
Cdd:cd03225 77 -VGLVFQNPDDqFFGPTVEEEVAFGlenLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 162 ILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-218 |
3.78e-55 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 175.60 E-value: 3.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLR 83
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQ-ASNLIPFLTVQQ-------QLELvdhltgSKE--KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIAR 153
Cdd:COG1122 75 -RKVGLVFQnPDDQLFAPTVEEdvafgpeNLGL------PREeiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-218 |
4.44e-54 |
|
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: 173.24 E-value: 4.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:COG1127 5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfKSVGFILQASNLIPFLTVQQ--QLELVDHLTGSKE--KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:COG1127 81 R-RRIGMLFQGGALFDSLTVFEnvAFPLREHTDLSEAeiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
1.80e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.40 E-value: 1.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlr 83
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksVGFILQASNLIPFLTVQQQLELVDHLTG---SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:COG1131 75 ---IGYVPQEPALYPDLTVRENLRFFARLYGlprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELL-RELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-218 |
4.51e-53 |
|
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: 168.77 E-value: 4.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfksVGFILQAsnlipfltv 102
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK----IAYVPQA--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 qqqLELVdhltgskekakanqlfddlGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKL 182
Cdd:cd03214 82 ---LELL-------------------GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLEL 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 499604739 183 LAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03214 140 LRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRI 176
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-200 |
6.53e-52 |
|
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: 170.23 E-value: 6.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTF-LTIAGGLQTP--SSGQLIIDGTDYTHLSEKER 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 SRLRFKSVGFILQ--ASNLIPFLTVQQQLE--LVDHLTGSKE--KAKANQLFDDLGITGLKHQL---PQELSGGERQRAA 150
Cdd:COG0444 81 RKIRGREIQMIFQdpMTSLNPVMTVGDQIAepLRIHGGLSKAeaRERAIELLERVGLPDPERRLdryPHELSGGMRQRVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499604739 151 IARALYHDPALILADEPTASLD-TEKAyEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDvTIQA-QILNLLKDLQRELGLAILFITHD 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-217 |
9.66e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 167.09 E-value: 9.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHlSEKERSRL 82
Cdd:COG1126 1 MIEIENLHKSF--GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfKSVGFILQASNLIPFLTVQQQLEL--VDHLTGSKEKA--KANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLapIKVKKMSKAEAeeRAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 159 PALILADEPTASLDTEKAYEV---VKLLAKEskekNKAIIMVTHDdrM---LKYCDKVYRMQDGE 217
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVldvMRDLAKE----GMTMVVVTHE--MgfaREVADRVVFMDGGR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
1.36e-51 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 173.94 E-value: 1.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MS-VLTFKQVTKTFQDGhhEINALKATDFSIEAGEFVAIIGPSGSGKSTF-LTIAGGLQTPS--SGQLIIDGTDYTHLSE 76
Cdd:COG1123 1 MTpLLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGGriSGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 77 KERSRlrfkSVGFILQ--ASNLIPfLTVQQQLELV---DHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAI 151
Cdd:COG1123 79 ALRGR----RIGMVFQdpMTQLNP-VTVGDQIAEAlenLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 152 ARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRI 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-218 |
1.57e-51 |
|
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: 166.04 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTKTFQdghHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRfK 85
Cdd:cd03292 3 FINVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 SVGFILQASNLIPFLTVQQQLELVDHLTGSKEKAKANQLFDDLGITGLKHQ---LPQELSGGERQRAAIARALYHDPALI 162
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKhraLPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 163 LADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDRML-KYCDKVYRMQDGEL 218
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-217 |
1.72e-51 |
|
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: 164.67 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFqdghHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLsEKERSRLR 83
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNLIPFLTVQQQLELVdhltgskekakanqlfddlgitglkhqlpqeLSGGERQRAAIARALYHDPALIL 163
Cdd:cd03229 76 -RRIGMVFQDFALFPHLTVLENIALG-------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 164 ADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
8-221 |
2.76e-51 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 165.76 E-value: 2.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 8 QVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRFKSV 87
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 88 GFILQASNLIPFLTVQQQLELvDHLTGSKEKAKANQ-LFDDLGITGLKHQL---PQELSGGERQRAAIARALYHDPALIL 163
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSrALEMLAAVGLEHRAnhrPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 164 ADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-222 |
1.10e-50 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 164.18 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRFKSVGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSrqsRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQER 222
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEEA 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
2.74e-50 |
|
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: 162.69 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlr 83
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksVGFILQASNLIPFLTVQQ--QLELVDHLTGSKE-KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03259 74 ---IGMVFQDYALFPHLTVAEniAFGLKLRGVPKAEiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGRIVQ 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
3.14e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 162.29 E-value: 3.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTktFQDGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLS-EKERSRl 82
Cdd:COG4619 1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfksVGFILQASNLIPfLTVQQQLELVDHLTGSK-EKAKANQLFDDLGIT-GLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:COG4619 76 ----VAYVPQEPALWG-GTVRDNLPFPFQLRERKfDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLK-YCDKVYRMQDGEL 218
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-219 |
3.90e-50 |
|
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: 163.06 E-value: 3.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRfK 85
Cdd:cd03261 3 LRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 SVGFILQASNLIPFLTVQQ--QLELVDHLTGSKE--KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPAL 161
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFEnvAFPLREHTRLSEEeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 162 ILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELC 219
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-218 |
2.86e-49 |
|
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: 160.00 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHlSEKERSRLR 83
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNLIPFLTVQQQLEL----VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLapikVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDdrM---LKYCDKVYRMQDGEL 218
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVM-KDLAEEGMTMVVVTHE--MgfaREVADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
1.09e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 162.57 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERs 80
Cdd:COG3842 3 MPALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfkSVGFILQASNLIPFLTVQQQ----LElVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALY 156
Cdd:COG3842 78 -----NVGMVFQDYALFPHLTVAENvafgLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 157 HDPALILADEPTASLDT----EKAYEVVKLLakesKEKNKAIIMVTHD--------DRMLkycdkVyrMQDGELCQ 220
Cdd:COG3842 152 PEPRVLLLDEPLSALDAklreEMREELRRLQ----RELGITFIYVTHDqeealalaDRIA-----V--MNDGRIEQ 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-220 |
2.27e-47 |
|
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: 156.31 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEINALkatDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEkerSRLR 83
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNL---NLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP---VELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFD--DLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:cd03295 75 -RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKekiRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQ 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
3.83e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.63 E-value: 3.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGgLQTPSSGQLIIDGTDYthlsEKER 79
Cdd:COG1121 4 MPAIELENLTVSY--GGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLkAILG-LLPPTSGTVRLFGKPP----RRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 SRlrfksVGFILQASNL---IPfLTVqqqLELVdhLTG------------SKEKAKANQLFDDLGITGLKHQLPQELSGG 144
Cdd:COG1121 75 RR-----IGYVPQRAEVdwdFP-ITV---RDVV--LMGrygrrglfrrpsRADREAVDEALERVGLEDLADRPIGELSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 145 ERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELC 219
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDlGAVREYFDRVLLLNRGLVA 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-210 |
5.01e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 154.91 E-value: 5.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFqdGHHEINAlkatDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlr 83
Cdd:COG3840 2 LRLDDLTYRY--GDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksVGFILQASNLIPFLTVQQQLELVDH----LTgSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:COG3840 73 ---VSMLFQENNLFPHLTVAQNIGLGLRpglkLT-AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKV 210
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDpEDAARIADRV 200
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
6.95e-47 |
|
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: 152.54 E-value: 6.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKErsrLR 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQasnlIPFLtvqqqlelvdhLTGSkekakanqLFDDLgitglkhqlpqeLSGGERQRAAIARALYHDPALIL 163
Cdd:cd03228 76 -KNIAYVPQ----DPFL-----------FSGT--------IRENI------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499604739 164 ADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGE 217
Cdd:cd03228 120 LDEATSALDPETEALILEALRALA--KGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-218 |
5.39e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 155.34 E-value: 5.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 5 TFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRf 84
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 85 KSVGFILQASNLIPFLTVQQQLELVDHLTG-SKE--KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPAL 161
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVALPLELAGtPKAeiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 162 ILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLK-YCDKVYRMQDGEL 218
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKrICDRVAVIDAGRL 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
1.41e-45 |
|
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: 158.77 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHheiNALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:COG4988 335 PSIELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LrfksVGFILQASNLIPfLTVQqqlelvDHLTGSKEKAKANQLFDDLGITGLKH---QLPQ-------E----LSGGERQ 147
Cdd:COG4988 412 Q----IAWVPQNPYLFA-GTIR------ENLRLGRPDASDEELEAALEAAGLDEfvaALPDgldtplgEggrgLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 148 RAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-218 |
3.84e-45 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 147.93 E-value: 3.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlr 83
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksVGFILQASNLIPFLTVQQQLelvdhltgskekakanqlfddlgitglkhqlpqELSGGERQRAAIARALYHDPALIL 163
Cdd:cd03230 75 ---IGYLPEEPSLYENLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 164 ADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03230 119 LDEPTSGLDPESRREFWELL-RELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-218 |
6.06e-45 |
|
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: 156.77 E-value: 6.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKS-TFLTIAGGLQTPS---SGQLIIDGTDYTHLSE 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 77 KERSRLRFKSVGFILQ--ASNLIPFLTVQQQ----LELVDHLTGSKEKAKANQLFDDLGITGLKHQL---PQELSGGERQ 147
Cdd:COG4172 84 RELRRIRGNRIAMIFQepMTSLNPLHTIGKQiaevLRLHRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 148 RAAIARALYHDPALILADEPTASLD-TEKAyEVVKLLAKESKEKNKAIIMVTHDdrmL----KYCDKVYRMQDGEL 218
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDvTVQA-QILDLLKDLQRELGMALLLITHD---LgvvrRFADRVAVMRQGEI 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
23-220 |
9.08e-45 |
|
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: 149.41 E-value: 9.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlrfksVGFILQASNLIPFLTV 102
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD------ISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQLEL-VDHLTGSKE--KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEV 179
Cdd:cd03299 89 YKNIAYgLKKRKVDKKeiERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499604739 180 VKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQ 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-218 |
1.35e-44 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 157.19 E-value: 1.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRFKSVGFILQASNLIPFLTVQQQLELVDHLTGS---KEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLerkQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
1.85e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 151.76 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAgGLQTPSSGQLIIDGTDYTHLSEKER 79
Cdd:COG3839 1 MASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLrMIA-GLEDPTSGEILIGGRDVTDLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 srlrfkSVGFILQ--AsnLIPFLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARA 154
Cdd:COG3839 76 ------NIAMVFQsyA--LYPHMTVYENIAFplkLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 155 LYHDPALILADEPTASLDtekayevVKL-------LAKESKEKNKAIIMVTHD--------DRMLkycdkVyrMQDGELC 219
Cdd:COG3839 148 LVREPKVFLLDEPLSNLD-------AKLrvemraeIKRLHRRLGTTTIYVTHDqveamtlaDRIA-----V--MNDGRIQ 213
|
.
gi 499604739 220 Q 220
Cdd:COG3839 214 Q 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-217 |
4.02e-44 |
|
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: 145.08 E-value: 4.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 5 TFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrf 84
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 85 ksVGFILQasnlipfltvqqqlelvdhltgskekakanqlfddlgitglkhqlpqeLSGGERQRAAIARALYHDPALILA 164
Cdd:cd00267 75 --IGYVPQ------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499604739 165 DEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDRML-KYCDKVYRMQDGE 217
Cdd:cd00267 105 DEPTSGLDPASRERLLELL-RELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-218 |
4.38e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 148.75 E-value: 4.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGH-HEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RFKsVGFILQASnlipfltvQQQL--ELVDH----------LTGSKEKAKANQLFDDLGIT-GLKHQLPQELSGGERQRA 149
Cdd:TIGR04521 81 RKK-VGLVFQFP--------EHQLfeETVYKdiafgpknlgLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 150 AIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKI 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-210 |
1.01e-43 |
|
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: 145.75 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 16 GHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYthlsEKERSRlrfksVGFILQASN 95
Cdd:cd03235 10 GGHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKR-----IGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 96 L---IPfLTVqqqLELVdhLTG------------SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03235 79 IdrdFP-ISV---RDVV--LMGlyghkglfrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKV 210
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDlGLVLEYFDRV 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-200 |
1.13e-43 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 146.78 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrLRfK 85
Cdd:PRK09493 4 FKNVSKHF--GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-IR-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 SVGFILQASNLIPFLTVqqqLELVD----HLTG-SKEKAK--ANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTA---LENVMfgplRVRGaSKEEAEkqARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD 200
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVM-QDLAEEGMTMVIVTHE 195
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-199 |
2.57e-43 |
|
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: 144.94 E-value: 2.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlrfksVGFILQASNLIPFLTVQQQL 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ELVD----HLTGSKEKAKANQLfDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKL 182
Cdd:cd03298 92 GLGLspglKLTAEDRQAIEVAL-ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170
....*....|....*..
gi 499604739 183 LAKESKEKNKAIIMVTH 199
Cdd:cd03298 171 VLDLHAETKMTVLMVTH 187
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-218 |
7.66e-43 |
|
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: 153.07 E-value: 7.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTktFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSekeRSRLR 83
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQAsnliPFL---TVQqqlelvDHLTGSKEKA---KANQLFDDLGITGLKHQLPQ-----------ELSGGER 146
Cdd:COG2274 549 -RQIGVVLQD----VFLfsgTIR------ENITLGDPDAtdeEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 147 QRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-218 |
8.01e-43 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 144.62 E-value: 8.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:COG4555 1 MIEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfksvGFILQASNLIPFLTVQQQLELV---DHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:COG4555 77 -----GVLPDERGLYDRLTVRENIRYFaelYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREIL-RALKKEGKTVLFSSHImQEVEALCDRVVILHKGKV 210
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
8-220 |
1.46e-42 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 143.79 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 8 QVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlrfksV 87
Cdd:TIGR00968 5 NISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRK------I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 88 GFILQASNLIPFLTVQQQ----LELVDHlTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALIL 163
Cdd:TIGR00968 75 GFVFQHYALFKHLTVRDNiafgLEIRKH-PKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 164 ADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:TIGR00968 154 LDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDqEEAMEVADRIVVMSNGKIEQ 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-218 |
1.87e-42 |
|
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: 150.69 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHeiNALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLr 83
Cdd:COG4987 334 LELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksVGFILQASNLipFL-TVQQQLELVdhltgsKEKAKANQLFDDLGITGLKH---QLPQ-----------ELSGGERQR 148
Cdd:COG4987 411 ---IAVVPQRPHL--FDtTLRENLRLA------RPDATDEELWAALERVGLGDwlaALPDgldtwlgeggrRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 149 AAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-220 |
1.97e-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: 145.23 E-value: 1.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 5 TFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLRf 84
Cdd:COG1125 3 EFENVTKRYPDGTV---AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGED---IRDLDPVELR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 85 KSVGFILQASNLIPFLTVQQQLELVDHLTG-SKEKAK--ANQLFDDLGI--TGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:COG1125 76 RRIGYVIQQIGLFPHMTVAENIATVPRLLGwDKERIRarVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 160 ALILADEPTASLD--T-EKAYEVVKLLAKESKeknKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:COG1125 156 PILLMDEPFGALDpiTrEQLQDELLRLQRELG---KTIVFVTHDiDEALKLGDRIAVMREGRIVQ 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-218 |
1.96e-41 |
|
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: 140.65 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 9 VTKTFqDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRfksVG 88
Cdd:cd03219 6 LTKRF-GGLV---ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG---IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 89 FILQASNLIPFLTVQQQLELVDHLTGS-------------KEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARAL 155
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARTGsglllararreerEARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 156 YHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELI-RELRERGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-220 |
3.98e-41 |
|
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: 140.86 E-value: 3.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRFKSVGFILQASNLIPFLT 101
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYE 178
Cdd:cd03294 119 VLENVAFgleVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499604739 179 VVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQ 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-220 |
5.59e-41 |
|
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: 138.93 E-value: 5.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlr 83
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksVGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03301 74 ---IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKdeiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-218 |
7.26e-41 |
|
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: 138.88 E-value: 7.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDghHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLsekERSRLR 83
Cdd:cd03245 3 IEFRNVSFSYPN--QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL---DPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNLIpFLTVQQQLELVDHLTGSKEKAKANQLfddLGITGLKHQLP-----------QELSGGERQRAAIA 152
Cdd:cd03245 78 -RNIGYVPQDVTLF-YGTLRDNITLGAPLADDERILRAAEL---AGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 153 RALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEknKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-220 |
1.27e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 141.44 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSvLTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTD-YTHLSEKER 79
Cdd:COG1118 1 MS-IEVRNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 srlrfkSVGFILQASNLIPFLTVQQQLEL-VDHLTGSKE--KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALY 156
Cdd:COG1118 76 ------RVGFVFQHYALFPHMTVAENIAFgLRVRPPSKAeiRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 157 HDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqEEALELADRVVVMNQGRIEQ 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-218 |
3.57e-40 |
|
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: 136.66 E-value: 3.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEA-----GEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDY------THLSEKERSrlrfksVGFILQASN 95
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQRK------IGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 96 LIPFLTVQQQLELV-DHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTE 174
Cdd:cd03297 86 LFPHLNVRENLAFGlKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499604739 175 KAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRL 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-218 |
4.64e-40 |
|
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: 136.23 E-value: 4.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 15 DGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERsrlrFKSVGFILQAS 94
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKER----RKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 NLIPFL-TVQQQLELVDHLTgSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDT 173
Cdd:cd03226 81 DYQLFTdSVREELLLGLKEL-DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499604739 174 EKAYEVVKLLAKESKEKnKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03226 160 KNMERVGELIRELAAQG-KAVIVITHDyEFLAKVCDRVLLLANGAI 204
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
23-220 |
9.11e-40 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 139.44 E-value: 9.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlrfksVGFILQASNLIPFLTV 102
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------IAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQ----LELvdHLTGSKE-KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAY 177
Cdd:NF040840 90 FENiafgLKL--RKVPKEEiERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499604739 178 EVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:NF040840 168 ELIREMKRWHREFGFTAIHVTHNfEEALSLADRVGIMLNGRLSQ 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
1.32e-39 |
|
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: 135.83 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERsrlr 83
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fkSVGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03300 73 --PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKaeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKIQQ 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-215 |
1.93e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 134.53 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:COG4133 2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfksvGFILQASNLIPFLTVQQQLELVDHLTG-SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPAL 161
Cdd:COG4133 78 -----AYLGHADGLKPELTVRENLRFWAALYGlRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499604739 162 ILADEPTASLDTEKAYEVVKLLAKEsKEKNKAIIMVTHDDRMLKYCdKVYRMQD 215
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAA-RVLDLGD 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
2.57e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.53 E-value: 2.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSvLTFKQVTKTFqdGHHEinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDY---THLSEK 77
Cdd:COG4161 1 MS-IQLKNINCFY--GSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 78 ERSRLRfKSVGFILQASNLIPFLTVQQQL--ELVDHLTGSKEKA--KANQLFDDLGITGLKHQLPQELSGGERQRAAIAR 153
Cdd:COG4161 76 AIRLLR-QKVGMVFQQYNLWPHLTVMENLieAPCKVLGLSKEQAreKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSQTGITQVIVTHEvEFARKVASQVVYMEKG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-203 |
4.10e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 134.71 E-value: 4.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERsrlrfkSVGFILQASNLIPFLTVQQQL 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR------PVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ELVDH----LTGSkEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKL 182
Cdd:PRK10771 93 GLGLNpglkLNAA-QREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180
....*....|....*....|...
gi 499604739 183 LAKESKEKNKAIIMVTH--DDRM 203
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHslEDAA 194
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-216 |
7.03e-39 |
|
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: 133.71 E-value: 7.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTF---QDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLQtPSSGQLIID----GTDYTHL 74
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLkCIYGNYL-PDSGSILVRhdggWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 75 SEKERSRLRFKSVGFILQasnlipFLTV---QQQLELVD----HLTGSKEKA--KANQLFDDLGItglkhqlPQEL---- 141
Cdd:COG4778 83 SPREILALRRRTIGYVSQ------FLRViprVSALDVVAepllERGVDREEAraRARELLARLNL-------PERLwdlp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 142 ----SGGERQRAAIARALYHDPALILADEPTASLDtEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLD-AANRAVVVELIEEAKARGTAIIGIFHDeEVREAVADRVVDVTPF 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-220 |
7.65e-39 |
|
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: 134.00 E-value: 7.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVlTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERS 80
Cdd:cd03296 1 MSI-EVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfksVGFILQASNLIPFLTVQQQ----LELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIAR 153
Cdd:cd03296 76 ------VGFVFQHYALFRHMTVFDNvafgLRVKPRSERPPEaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqEEALEVADRVVVMNKGRIEQ 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-200 |
1.57e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 133.83 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSeKERs 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-ADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfksvGFILQASNLIPFLTVQQQLELVDHLTG---SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYH 157
Cdd:COG4525 79 -------GVVFQKDALLPWLNVLDNVAFGLRLRGvpkAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499604739 158 DPALILADEPTASLDT---EKAYEvvkLLAKESKEKNKAIIMVTHD 200
Cdd:COG4525 152 DPRFLLMDEPFGALDAltrEQMQE---LLLDVWQRTGKGVFLITHS 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-169 |
6.19e-38 |
|
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: 128.92 E-value: 6.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLRfKSVGFILQASNLIPFLTV 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLR-KEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 103 QQQLELVDHLTG---SKEKAKANQLFDDLGITGLKHQL----PQELSGGERQRAAIARALYHDPALILADEPTA 169
Cdd:pfam00005 77 RENLRLGLLLKGlskREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-200 |
6.59e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 132.18 E-value: 6.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFqdghHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQL-----IIDGTdyTHLS 75
Cdd:PRK11264 1 MSAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 76 EKER--SRLRfKSVGFILQASNLIPFLTVQQQL----ELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRA 149
Cdd:PRK11264 75 QQKGliRQLR-QHVGFVFQNFNLFPHRTVLENIiegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499604739 150 AIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKnKAIIMVTHD 200
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHE 203
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
18-216 |
9.99e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 131.29 E-value: 9.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 18 HEINalkatdFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDY---THLSEKERSRLRfKSVGFILQAS 94
Cdd:PRK11124 19 FDIT------LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR-RNVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 NLIPFLTVQQQL-EL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:PRK11124 92 NLWPHLTVQQNLiEApcrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499604739 171 LDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:PRK11124 172 LDPEITAQIVSII-RELAETGITQVIVTHEvEVARKTASRVVYMENG 217
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
21-218 |
2.54e-37 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 130.09 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 21 NALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfkSVGFILQASNLIPFL 100
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL---GIGYLPQEASIFRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 TVQQQ----LELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKA 176
Cdd:TIGR04406 92 TVEENimavLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499604739 177 YEVVKLLaKESKEKNKAIIMVTHDDR-MLKYCDKVYRMQDGEL 218
Cdd:TIGR04406 172 GDIKKII-KHLKERGIGVLITDHNVReTLDICDRAYIISDGKV 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-218 |
4.34e-37 |
|
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: 129.22 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGL-----QTPSSGQLIIDGTDYTHLSEkE 78
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDV-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 79 RSRLRFKsVGFILQASNLIPfLTVQQQLELVDHLTGSKEKAKANQLFDD-LGITGLK-----HQLPQELSGGERQRAAIA 152
Cdd:cd03260 76 VLELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEaLRKAALWdevkdRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 153 RALYHDPALILADEPTASLD---TEKAYEVVKLLAKESkeknkAIIMVTHDDRMLKYC-DKVYRMQDGEL 218
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDpisTAKIEELIAELKKEY-----TIVIVTHNMQQAARVaDRTAFLLNGRL 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-199 |
4.50e-37 |
|
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: 128.83 E-value: 4.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlrfksVGFILQASNLIPFLTVQQQL 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ELVDH----LTgSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKL 182
Cdd:TIGR01277 92 GLGLHpglkLN-AEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170
....*....|....*..
gi 499604739 183 LAKESKEKNKAIIMVTH 199
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTH 187
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-221 |
6.89e-37 |
|
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: 129.86 E-value: 6.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTKTFQDGhhEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYthLSEKERSRLRfK 85
Cdd:TIGR04520 3 VENVSFSYPES--EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 SVGFILQ-ASNLIPFLTVQ---------QQLElvdhltgSKE-KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARA 154
Cdd:TIGR04520 78 KVGMVFQnPDNQFVGATVEddvafglenLGVP-------REEmRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 155 LYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKyCDKVYRMQDGELCQE 221
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDmEEAVL-ADRVIVMNKGKIVAE 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-218 |
7.29e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.38 E-value: 7.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFqDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:COG1129 4 LLEMRGISKSF-GGVK---ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfksVGFILQASNLIPFLTVQQQL----E-----LVDHltgSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIAR 153
Cdd:COG1129 80 G---IAIIHQELNLVPNLSVAENIflgrEprrggLIDW---RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 154 ALYHDPALILADEPTASL---DTEKAYEVVKLLakesKEKNKAIIMVTHddRM---LKYCDKVYRMQDGEL 218
Cdd:COG1129 154 ALSRDARVLILDEPTASLterEVERLFRIIRRL----KAQGVAIIYISH--RLdevFEIADRVTVLRDGRL 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-218 |
9.32e-37 |
|
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: 126.56 E-value: 9.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfksVGFILQASNLipfltv 102
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH----VGYLPQDDEL------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 qqqlelvdhLTGSkekakanqLFDDLgitglkhqlpqeLSGGERQRAAIARALYHDPALILADEPTASLDT--EKA-YEV 179
Cdd:cd03246 88 ---------FSGS--------IAENI------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegERAlNQA 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 499604739 180 VKLLakesKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:cd03246 139 IAAL----KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-218 |
9.68e-37 |
|
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: 128.16 E-value: 9.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLQTPS--SGQLIIDGtdythlseKE 78
Cdd:cd03234 2 RVLPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdAISGRVEGGGttSGQILFNG--------QP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 79 RSRLRF-KSVGFILQASNLIPFLTVQQQLELVDHLTGSKEKAKAN-------QLFDDLGITGLKHQLPQELSGGERQRAA 150
Cdd:cd03234 74 RKPDQFqKCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIrkkrvedVLLRDLALTRIGGNLVKGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 151 IARALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDR--MLKYCDKVYRMQDGEL 218
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTL-SQLARRNRIVILTIHQPRsdLFRLFDRILLLSSGEI 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-199 |
9.72e-37 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 129.05 E-value: 9.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTktFQDGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIidgtdytHLSEKERS 80
Cdd:COG1119 1 DPLLELRNVT--VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV-------RLFGERRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 R-----LRfKSVGFI---LQAsNLIPFLTVqqqLELVdhLTGS------------KEKAKANQLFDDLGITGLKHQLPQE 140
Cdd:COG1119 70 GedvweLR-KRIGLVspaLQL-RFPRDETV---LDVV--LSGFfdsiglyreptdEQRERARELLELLGLAHLADRPFGT 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 141 LSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTH 199
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
1.23e-36 |
|
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: 129.00 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFqdGhheinALKATD---FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEK 77
Cdd:COG0411 2 DPLLEVRGLTKRF--G-----GLVAVDdvsLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 78 ERSRL---R-FksvgfilQASNLIPFLTVQQQLELVDHLTGSK---------------EKA---KANQLFDDLGITGLKH 135
Cdd:COG0411 75 RIARLgiaRtF-------QNPRLFPELTVLENVLVAAHARLGRgllaallrlprarreEREareRAEELLERVGLADRAD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 136 QLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQ 214
Cdd:COG0411 148 EPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVVLD 227
|
....
gi 499604739 215 DGEL 218
Cdd:COG0411 228 FGRV 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
16-217 |
1.48e-36 |
|
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: 127.55 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 16 GHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGgLQTPSSGQLIIDGTDYTHLSEKERSRLrfkSVGFILQAS 94
Cdd:cd03224 9 GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLkTIMG-LLPPRSGSIRFDGRDITGLPPHERARA---GIGYVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 NLIPFLTVQQQLELVDHlTGSKEKAKAN-----QLFDDLGitGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTA 169
Cdd:cd03224 85 RIFPELTVEENLLLGAY-ARRRAKRKARlervyELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499604739 170 SLDTEKAYEVVKLLAKESKEKnKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEG-VTILLVEQNaRFALEIADRAYVLERGR 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
23-218 |
2.05e-36 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 127.66 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfkSVGFILQASNLIPFLTV 102
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL---GIGYLPQEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQLELVDHLTGSKEK---AKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTeKAYEV 179
Cdd:cd03218 93 EENILAVLEIRGLSKKereEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP-IAVQD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499604739 180 VKLLAKESKEKNKAIIMVTHDDR-MLKYCDKVYRMQDGEL 218
Cdd:cd03218 172 IQKIIKILKDRGIGVLITDHNVReTLSITDRAYIIYEGKV 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-218 |
3.01e-36 |
|
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: 130.23 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKAtDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRFKSVGFILQASNLIPFLT 101
Cdd:TIGR02142 13 SLDA-DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLEL-VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVV 180
Cdd:TIGR02142 92 VRGNLRYgMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 499604739 181 KLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRV 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-219 |
1.48e-35 |
|
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: 124.92 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHeiNALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYThlseKERSRLR 83
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNLIPFLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFyarLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHD----DRMlkyCDKVYRMQDGELC 219
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSmdeaEAL---CDRIAIMSDGKLR 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
2.62e-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: 130.48 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHheiNALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKersr 81
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRFKSVGFILQAsnliPFL---TVQQQLEL------VDHLTGSKEKAKANQLFDDLGiTGLKHQL---PQELSGGERQRA 149
Cdd:TIGR02857 393 SWRDQIAWVPQH----PFLfagTIAENIRLarpdasDAEIREALERAGLDEFVAALP-QGLDTPIgegGAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 150 AIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRM 213
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-218 |
6.96e-35 |
|
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: 123.07 E-value: 6.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheinALKATDFSIEAGEFvAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLr 83
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksvGFILQASNLIPFLTVQQQLELVDHLTG---SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03264 75 ----GYLPQEFGVYPNFTVREFLDYIAWLKGipsKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIvEDVESLCNQVAVLNKGKL 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-216 |
7.30e-35 |
|
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: 126.75 E-value: 7.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTdyTHLSEKERSRL----RfkSVGFILQASNLIPFLTV 102
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE--VLQDSARGIFLpphrR--RIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQLELvdhltGSK--EKAKANQLFDD----LGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKA 176
Cdd:COG4148 95 RGNLLY-----GRKraPRAERRISFDEvvelLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499604739 177 YEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSlDEVARLADHVVLLEQG 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-219 |
7.45e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 124.04 E-value: 7.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 7 KQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR----L 82
Cdd:COG4604 5 KNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfksvgfilQASNLIPFLTVQqqlELV---------DHLTgSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIAR 153
Cdd:COG4604 81 R--------QENHINSRLTVR---ELVafgrfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRML-KYCDKVYRMQDGELC 219
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAsCYADHIVAMKDGRVV 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-210 |
9.22e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 125.61 E-value: 9.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATD---FSIEAGEFVAIIGPSGSGKSTF-LTIAGgLQTPSSGQLIIDGTDYTHLSEKERSRLRfKSVGFILQ---AS 94
Cdd:COG4608 30 VVKAVDgvsFDIRRGETLGLVGESGCGKSTLgRLLLR-LEEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQdpyAS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 nLIPFLTVQQQLE--LVDHLTGSKE--KAKANQLfddLGITGLK----HQLPQELSGGERQRAAIARALYHDPALILADE 166
Cdd:COG4608 108 -LNPRMTVGDIIAepLRIHGLASKAerRERVAEL---LELVGLRpehaDRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499604739 167 PTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKY-CDKV 210
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHiSDRV 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
2.07e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 123.25 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIdGTdyTHLSE-KERSRL 82
Cdd:PRK11247 13 LLLNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GT--APLAEaREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RFksvgfilQASNLIPFLTVQQQLELvdHLTGsKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALI 162
Cdd:PRK11247 86 MF-------QDARLLPWKKVIDNVGL--GLKG-QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 163 LADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-218 |
2.83e-34 |
|
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: 121.71 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLr 83
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksvGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03266 81 ----GFVSDSTGLYDRLTARENLEYFAGLYGLKGdelTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 161 LILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTHImQEVERLCDRVVVLHRGRV 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-221 |
4.18e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.59 E-value: 4.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheiNALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSekeRSRLR 83
Cdd:COG1132 340 IEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQAsnliPFL---TV------------QQQLElvdhltgskEKAKANQLFDDLgitglkHQLPQ--------- 139
Cdd:COG1132 414 -RQIGVVPQD----TFLfsgTIrenirygrpdatDEEVE---------EAAKAAQAHEFI------EALPDgydtvvger 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 140 --ELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHddRM--LKYCDKVYRMQD 215
Cdd:COG1132 474 gvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAH--RLstIRNADRILVLDD 549
|
....*.
gi 499604739 216 GELCQE 221
Cdd:COG1132 550 GRIVEQ 555
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-221 |
1.00e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.20 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVlTFKQVTKTFQDGH-HEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKER 79
Cdd:PRK13646 1 MTI-RFDNVSYTYQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 SRLRFKSVGFILQASNLIPFL-TVQQQLELvdhltGSKE--------KAKANQLFDDLGIT-GLKHQLPQELSGGERQRA 149
Cdd:PRK13646 80 IRPVRKRIGMVFQFPESQLFEdTVEREIIF-----GPKNfkmnldevKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 150 AIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQ 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-218 |
3.09e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 12 TFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKErsrLRfKSVGFIL 91
Cdd:PRK13632 14 SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE---IR-KKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 92 Q-ASNLIPFLTVQQQ----LElVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADE 166
Cdd:PRK13632 90 QnPDNQFIGATVEDDiafgLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499604739 167 PTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKyCDKVYRMQDGEL 218
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDmDEAIL-ADKVIVFSEGKL 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-218 |
3.38e-33 |
|
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: 117.80 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTktFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLT-IAGGLQtPSSGQLIIDGTDyTHLSEKERSrl 82
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLK-PQQGEITLDGVP-VSDLEKALS-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfKSVGFILQAsnliPFLtvqqqlelvdhltgskekakanqlFDdlgiTGLKHQLPQELSGGERQRAAIARALYHDPALI 162
Cdd:cd03247 75 --SLISVLNQR----PYL------------------------FD----TTLRNNLGRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 163 LADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVL--KDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
27-200 |
4.58e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 118.35 E-value: 4.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLT-IAGGLQTP--SSGQLIIDGTDYTHLSEKERSrlrfksVGFILQASNLIPFLTVQ 103
Cdd:COG4136 21 SLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQRR------IGILFQDDLLFPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 104 QQL--ELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVK 181
Cdd:COG4136 95 ENLafALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170
....*....|....*....
gi 499604739 182 LLAKESKEKNKAIIMVTHD 200
Cdd:COG4136 175 FVFEQIRQRGIPALLVTHD 193
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-218 |
5.15e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.35 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 10 TKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfkSVGF 89
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR----RLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 90 ILQaSNLIP-FLTVQqqlELVD-----HLT-----GSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:PRK11231 81 LPQ-HHLTPeGITVR---ELVAygrspWLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHDlNQASRYCDHLVVLANGHV 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-216 |
6.38e-33 |
|
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: 118.72 E-value: 6.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYThlsEKERSRLrfksvgFILQASNLIPFLTV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT---EPGPDRM------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQLEL-VD----HLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAY 177
Cdd:TIGR01184 72 RENIALaVDrvlpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499604739 178 EVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-220 |
6.48e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 121.34 E-value: 6.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVlTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERs 80
Cdd:PRK10851 1 MSI-EIANIKKSF--GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfkSVGFILQASNLIPFLTVQQQ-------LELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIAR 153
Cdd:PRK10851 75 -----KVGFVFQHYALFRHMTVFDNiafgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNIEQ 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-218 |
7.40e-33 |
|
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: 117.27 E-value: 7.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQ--DGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTI-AGGLQTPS-SGQLIIDGTDythlSE 76
Cdd:cd03213 1 GVTLSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAlAGRRTGLGvSGEVLINGRP----LD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 77 KERSRlrfKSVGFILQASNLIPFLTVQQQLELVDHLTGskekakanqlfddlgitglkhqlpqeLSGGERQRAAIARALY 156
Cdd:cd03213 77 KRSFR---KIIGYVPQDDILHPTLTVRETLMFAAKLRG--------------------------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 157 HDPALILADEPTASLDTEKAYEVVKLLAKESKEkNKAIIMVTHDDR--MLKYCDKVYRMQDGEL 218
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSseIFELFDKLLLLSQGRV 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-216 |
9.19e-33 |
|
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: 124.09 E-value: 9.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfkSVGFIlqasnliPfltv 102
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR----HIGYL-------P---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 qQQLELVDhltGS------------KEKA-KANQLfddLGITGLKHQLPQ-----------ELSGGERQRAAIARALYHD 158
Cdd:COG4618 413 -QDVELFD---GTiaeniarfgdadPEKVvAAAKL---AGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 159 PALILADEPTASLDT--EKAyevvkLLA--KESKEKNKAIIMVTHDDRMLKYCDKVYRMQDG 216
Cdd:COG4618 486 PRLVVLDEPNSNLDDegEAA-----LAAaiRALKARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-218 |
1.41e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.82 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKST-FLTIAGgLQTPSSGQLIIDGTDYTHLSEKER 79
Cdd:COG1137 1 MMTLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTtFYMIVG-LVKPDSGRIFLDGEDITHLPMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 SRLrfkSVGFILQ-ASnlIpF--LTVQQQ----LELVDhLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIA 152
Cdd:COG1137 76 ARL---GIGYLPQeAS--I-FrkLTVEDNilavLELRK-LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 153 RALYHDPALILADEPTASLDTEKAYEVVKLLAKeSKEKNKAIIMVTHDDR-MLKYCDKVYRMQDGEL 218
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRH-LKERGIGVLITDHNVReTLGICDRAYIISEGKV 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
2.31e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.22 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKErsrlr 83
Cdd:cd03216 1 LELRGITKRFGGVK----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksvgfilqasnlipfltvqqqlelvdhltgskekAKAnqlfddLGItGLKHQLpqelSGGERQRAAIARALYHDPALIL 163
Cdd:cd03216 72 -----------------------------------ARR------AGI-AMVYQL----SVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 164 ADEPTASLD---TEKAYEVVKLLakesKEKNKAIIMVTHddRM---LKYCDKVYRMQDGEL 218
Cdd:cd03216 106 LDEPTAALTpaeVERLFKVIRRL----RAQGVAVIFISH--RLdevFEIADRVTVLRDGRV 160
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-217 |
3.02e-32 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.10 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 13 FQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTF-LTIAGgLQtPSSGQLIIDGTDYTHLSEKERSRLRfKSVGFIL 91
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLR-LI-PSEGEIRFDGQDLDGLSRRALRPLR-RRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 92 Q---ASnLIPFLTVQQQLE--LVDH---LTGSKEKAKANQLFDDLGIT-GLKHQLPQELSGGERQRAAIARALYHDPALI 162
Cdd:COG4172 369 QdpfGS-LSPRMTVGQIIAegLRVHgpgLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 163 LADEPTASLD-TEKAyEVVKLLAKESKEKNKAIIMVTHDDRMLKY-CDKVYRMQDGE 217
Cdd:COG4172 448 VLDEPTSALDvSVQA-QILDLLRDLQREHGLAYLFISHDLAVVRAlAHRVMVMKDGK 503
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-216 |
5.36e-32 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 118.67 E-value: 5.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTF--QDGhhEINALKATDFSIEAGEFVAIIGPSGSGKS-TFLTIAGGLQTPS--SGQLIIDGTDYTHLS 75
Cdd:PRK09473 10 DALLDVKDLRVTFstPDG--DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 76 EKERSRLRFKSVGFILQ--ASNLIPFLTVQQQLELVDHLTGSKEKAKANQ----LFDDLGITGLKHQL---PQELSGGER 146
Cdd:PRK09473 88 EKELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEesvrMLDAVKMPEARKRMkmyPHEFSGGMR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 147 QRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLK-YCDKVYRMQDG 216
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgICDKVLVMYAG 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-218 |
6.36e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.79 E-value: 6.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 12 TFQDGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRfksvGFIL 91
Cdd:PRK13548 9 SVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR----AVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 92 QASNL-IPFlTVQQ--QLELVDHLTGSKE-KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARAL------YHDPAL 161
Cdd:PRK13548 83 QHSSLsFPF-TVEEvvAMGRAPHGLSRAEdDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 162 ILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDdrmL----KYCDKVYRMQDGEL 218
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHD---LnlaaRYADRIVLLHQGRL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
16-217 |
6.41e-32 |
|
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: 115.85 E-value: 6.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 16 GHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGgLQTPSSGQLIIDGTDYTHLSEKERSRLrfkSVGFILQAS 94
Cdd:COG0410 12 GYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLkAISG-LLPPRSGSIRFDGEDITGLPPHRIARL---GIGYVPEGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 NLIPFLTVQQQLELVDHLTGSKEKAKAN-----QLFDDLGitGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTA 169
Cdd:COG0410 88 RIFPSLTVEENLLLGAYARRDRAEVRADlervyELFPRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499604739 170 SLD---TEKAYEVVKLLAKEskekNKAIIMVTHDDRM-LKYCDKVYRMQDGE 217
Cdd:COG0410 166 GLApliVEEIFEIIRRLNRE----GVTILLVEQNARFaLEIADRAYVLERGR 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-218 |
1.38e-31 |
|
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: 114.24 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFqdghHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKersrlr 83
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 FKSVGFILQASNLIPFLTVQQQLELVDHLTGsKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALIL 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLG-IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 164 ADEPTASLDTEKAYEVVKLLAKESKEkNKAIIMVTHddrML----KYCDKVYRMQDGEL 218
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSH---LLseiqKVADRIGIINKGKL 204
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-221 |
1.95e-31 |
|
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: 114.63 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSekeRSRLRfK 85
Cdd:cd03254 5 FENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR-S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 SVGFILQAsnliPFL---TVQQQLELVDHLTGSKEKAKANQL--FDDLGIT---GLKHQLPQE---LSGGERQRAAIARA 154
Cdd:cd03254 78 MIGVVLQD----TFLfsgTIMENIRLGRPNATDEEVIEAAKEagAHDFIMKlpnGYDTVLGENggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 155 LYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-218 |
3.25e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 115.11 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQdgHHEinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQT-PSSGQLIIDGTDYTHLSEKERS 80
Cdd:PRK09984 3 TIIRVEKLAKTFN--QHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgDKSAGSHIELLGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 RLRFKS---VGFILQASNLIPFLTVQQQLeLVDHLTGS------------KEKAKANQLFDDLGITGLKHQLPQELSGGE 145
Cdd:PRK09984 79 RDIRKSranTGYIFQQFNLVNRLSVLENV-LIGALGSTpfwrtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 146 RQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHV 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-220 |
3.95e-31 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.83 E-value: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRFKSVGFILQASNLIPFLT 101
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLELVDHLTGSKEKAKANQLFDDLGITGLK---HQLPQELSGGERQRAAIARALYHDPALILADEPTASLD----TE 174
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLEnyaHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499604739 175 KAYEVVKLLAKEskekNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:PRK10070 203 MQDELVKLQAKH----QRTIVFISHDlDEAMRIGDRIAIMQNGEVVQ 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-200 |
4.97e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.86 E-value: 4.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFqDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERsrl 82
Cdd:PRK11607 19 LLEIRNLTKSF-DGQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfkSVGFILQASNLIPFLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:PRK11607 92 ---PINMMFQSYALFPHMTVEQNIAFglkQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499604739 160 ALILADEPTASLDTE----KAYEVVKLLAKeskeKNKAIIMVTHD 200
Cdd:PRK11607 169 KLLLLDEPMGALDKKlrdrMQLEVVDILER----VGVTCVMVTHD 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-222 |
9.85e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.01 E-value: 9.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDG-----HHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLS 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 76 EKERSRLRfKSVGFILQ----ASNliPFLTVQQQL-ELVDHLTGSKE---KAKANQLFDDLGIT-GLKHQLPQELSGGER 146
Cdd:PRK10419 81 RAQRKAFR-RDIQMVFQdsisAVN--PRKTVREIIrEPLRHLLSLDKaerLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 147 QRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRML-KYCDKVYRMQDGELCQER 222
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVETQ 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-218 |
1.16e-30 |
|
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: 117.83 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLRfKSVGFILQASNLIPFlTV 102
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAD---LKQWDRETFG-KHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQL-ELVDHLTGSK--EKAKANQLFD-----------DLGITGlkhqlpQELSGGERQRAAIARALYHDPALILADEPT 168
Cdd:TIGR01842 409 AENIaRFGENADPEKiiEAAKLAGVHElilrlpdgydtVIGPGG------ATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499604739 169 ASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:TIGR01842 483 SNLDEEGEQALANAI-KALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-218 |
1.27e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 112.81 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 13 FQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGtdytHLSEKERSRLRfKSVGFIL- 91
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFL-RRIGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 92 QASNLIPFLTVQQQLELVDHLTG-SKEKAKAN--QLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPT 168
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYDlPPARFKKRldELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499604739 169 ASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRL 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-200 |
1.57e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 112.28 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL 82
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfKSVGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:PRK10908 78 R-RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGddiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD 200
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLF-EEFNRVGVTVLMATHD 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-217 |
2.10e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.60 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 19 EINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYThlseKERSRLRF--KSVGFILQASNL 96
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT----DKKVKLSDirKKVGLVFQYPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 97 IPFL-TVQQQLELVDHLTGSKEKAKANQLFDDLGITGL-----KHQLPQELSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:PRK13637 95 QLFEeTIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499604739 171 LDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGK 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-218 |
2.20e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 117.23 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHeiNALKATDFSIEAGEFVAIIGPSGSGKSTFLtiagGLQT----PSSGQLIIDGTDYTHLSEker 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTrawdPQQGEILLNGQPIADYSE--- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 SRLRfksvgfilqasNLIPFLTvqQQLE-----LVDHLTGSKEKAKANQLFDDLGITGLKHQLPQE-------------L 141
Cdd:PRK11160 410 AALR-----------QAISVVS--QRVHlfsatLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDkglnawlgeggrqL 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 142 SGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-200 |
2.93e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 114.07 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKS-TFLTIAGGLQTP---SSGQLIIDGTDYTHLSE 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 77 KERSRLRFKSVGFILQ--ASNLIPFLTVQQQL--ELVDHLTGSKE--KAKANQLFDDLGITGLKHQL---PQELSGGERQ 147
Cdd:PRK11022 81 KERRNLVGAEVAMIFQdpMTSLNPCYTVGFQImeAIKVHQGGNKKtrRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499604739 148 RAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-217 |
3.55e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.10 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGH-HEINALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLqTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:COG1101 2 LELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLnAIAGSL-PPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LrfksVGFILQ------ASNLipflTVQQQLELVDH----------LTgSKEKAKANQLFDDLGItGLKHQLPQE---LS 142
Cdd:COG1101 81 Y----IGRVFQdpmmgtAPSM----TIEENLALAYRrgkrrglrrgLT-KKRRELFRELLATLGL-GLENRLDTKvglLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 143 GGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDdrM---LKYCDKVYRMQDGE 217
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN--MeqaLDYGNRLIMMHEGR 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-200 |
4.91e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.97 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHheINalKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERs 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVV--IS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfkSVGFILQASNLIPFLTVQQQLELVDHLTGSKE---KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYH 157
Cdd:PRK11000 76 -----GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKeeiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499604739 158 DPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-216 |
7.01e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 114.17 E-value: 7.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERS 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 RLrfksVGFILQASNLIPFLTVQQQLEL--VDHLT-----GSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIAR 153
Cdd:PRK09536 77 RR----VASVPQDTSLSFEFDVRQVVEMgrTPHRSrfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 154 ALYHDPALILADEPTASLDTEKA---YEVVKLLAkeskEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQvrtLELVRRLV----DDGKTAVAAIHDlDLAARYCDELVLLADG 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-221 |
7.72e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.71 E-value: 7.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKST-FLTIAGGLQtPSSGQLIIDGTDythLSEKERSRLRF-KSVGFILQASNLIPF 99
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTlFLHFNGILK-PTSGEVLIKGEP---IKYDKKSLLEVrKTVGIVFQNPDDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 100 L-TVQQQLELVDHLTGSKEKAKANQLFDDL---GITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEK 175
Cdd:PRK13639 93 ApTVEEDVAFGPLNLGLSKEEVEKRVKEALkavGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499604739 176 AYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK13639 173 ASQIMKLL-YDLNKEGITIIISTHDvDLVPVYADKVYVMSDGKIIKE 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
1.99e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.88 E-value: 1.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGH-HEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYT-HLSEKERSR 81
Cdd:PRK13634 3 ITFQKVEHRYQYKTpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRfKSVGFILQASNLIPF-LTVQQQLELVDHLTGSKE---KAKANQLfddLGITGLKHQL----PQELSGGERQRAAIAR 153
Cdd:PRK13634 83 LR-KKVGIVFQFPEHQLFeETVEKDICFGPMNFGVSEedaKQKAREM---IELVGLPEELlarsPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKG 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-221 |
3.75e-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: 108.86 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheiNALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLR 83
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD---IREVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNL--------IPFLTVQQQLELVdhltgsKEKAKANQLFDD-----------LGITGLKhqlpqeLSGG 144
Cdd:cd03253 75 -RAIGVVPQDTVLfndtigynIRYGRPDATDEEV------IEAAKAAQIHDKimrfpdgydtiVGERGLK------LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 145 ERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-220 |
5.23e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.58 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERs 80
Cdd:PRK09452 12 SPLVELRGISKSF--DGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfksvgfilqasnliPFLTVQQQLELVDHLT-------GSKEKAKANQ-----LFDDLGITGLKH---QLPQELSGGE 145
Cdd:PRK09452 87 -----------------HVNTVFQSYALFPHMTvfenvafGLRMQKTPAAeitprVMEALRMVQLEEfaqRKPHQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 146 RQRAAIARALYHDPALILADEPTASLDtekaYEVVKLLAKESKEKNKAI----IMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALD----YKLRKQMQNELKALQRKLgitfVFVTHDqEEALTMSDRIVVMRDGRIEQ 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
8-200 |
5.31e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.44 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 8 QVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTF---LTIaggLQTPSSGQLIIDGTDYTHLSEKERSRLRf 84
Cdd:PRK11308 16 PVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLarlLTM---IETPTGGELYYQGQDLLKADPEAQKLLR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 85 KSVGFILQ---ASnLIPFLTVQQQLE--LVDH--LTGSKEKAKANQLfddLGITGLK----HQLPQELSGGERQRAAIAR 153
Cdd:PRK11308 92 QKIQIVFQnpyGS-LNPRKKVGQILEepLLINtsLSAAERREKALAM---MAKVGLRpehyDRYPHMFSGGQRQRIAIAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-200 |
1.28e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.16 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGqliidgtdythlsekERSRLRFKSVGFILQASNLIPFL- 100
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG---------------TVRRAGGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 -TVQQQLE--------LVDHLTGSKEKAKANQLfDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASL 171
Cdd:NF040873 72 lTVRDLVAmgrwarrgLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180
....*....|....*....|....*....
gi 499604739 172 DTEKAYEVVKLLAKESKEKnKAIIMVTHD 200
Cdd:NF040873 151 DAESRERIIALLAEEHARG-ATVVVVTHD 178
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-222 |
1.54e-28 |
|
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: 107.07 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTP----SSGQLIIDGTDYTHLSekersrLRFKSVGFILQA--SNLIPFL 100
Cdd:TIGR02770 6 NLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLS------IRGRHIATIMQNprTAFNPLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 TVQQQLE---LVDHLTGSKEKAKANQLFDDLGITGLK---HQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTE 174
Cdd:TIGR02770 80 TMGNHAIetlRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499604739 175 KAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYC-DKVYRMQDGELCQER 222
Cdd:TIGR02770 160 NQARVLKLLRELRQLFGTGILLITHDLGVVARIaDEVAVMDDGRIVERG 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-220 |
1.72e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 109.12 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 38 IIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSrlrfksVGFILQASNLIPFLTVQQQLEL---VDHLTG 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH------INMVFQSYALFPHMTVEENVAFglkMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 115 SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDtekaYEVVKLLAKESKEKNKAI 194
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD----KKLRDQMQLELKTIQEQL 150
|
170 180 190
....*....|....*....|....*....|.
gi 499604739 195 ----IMVTHDDR-MLKYCDKVYRMQDGELCQ 220
Cdd:TIGR01187 151 gitfVFVTHDQEeAMTMSDRIAIMRKGKIAQ 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-200 |
1.97e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 107.75 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 16 GHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYT---------HLSEKERSRLRFKS 86
Cdd:PRK10619 16 GEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 87 VGFILQASNLIPFLTVQQQLE----LVDHLTGSKEKAKANQLFDDLGITG-LKHQLPQELSGGERQRAAIARALYHDPAL 161
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVLENVMeapiQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 499604739 162 ILADEPTASLDTEKAYEVVKLLAKESkEKNKAIIMVTHD 200
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHE 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-214 |
2.34e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 13 FQDGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSeKERSRlrfKSVGFILQ 92
Cdd:PRK10247 15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-PEIYR---QQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 93 AsnliPFL---TVQQQLELVDHLTGSKEKAKAnqLFDDLGITGLKHQLPQ----ELSGGERQRAAIARALYHDPALILAD 165
Cdd:PRK10247 89 T----PTLfgdTVYDNLIFPWQIRNQQPDPAI--FLDDLERFALPDTILTkniaELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499604739 166 EPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQ 214
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-200 |
4.18e-28 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 110.53 E-value: 4.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfksVGFILQASNLipF-L 100
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHL--FdT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 TVQQQLELV------DHLTGSKEKAKANQLFDDL--GITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLD 172
Cdd:TIGR02868 424 TVRENLRLArpdatdEELWAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 499604739 173 TEKAYEVVKLLAKESKEknKAIIMVTHD 200
Cdd:TIGR02868 504 AETADELLEDLLAALSG--RTVVLITHH 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-222 |
4.85e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.57 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKS-TFLTIAGGLQTPS----SGQLIIDGTDYTHLS 75
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 76 EKERSRLRFKSVGFILQA--SNLIPFLTVQQQLE--LVDHLTGSKEKAKANQL--FDDLGITGLKHQL---PQELSGGER 146
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYevLSLHRGMRREAARGEILncLDRVGIRQAAKRLtdyPHQLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 147 QRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRML-KYCDKVYRMQDGElCQER 222
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGR-CVEQ 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-216 |
6.43e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.86 E-value: 6.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDG--TDYthlSEKERS 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDY---SRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 RLRfKSVGFILQA-SNLIPFLTVQQQLE---LVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALY 156
Cdd:PRK13636 79 KLR-ESVGMVFQDpDNQLFSASVYQDVSfgaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 157 HDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-221 |
7.40e-28 |
|
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: 105.14 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYThlseKERSRLRfKSVGFILQASNLIPFLT 101
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR-RRIGIVFQDLSVDDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLELVDHLTG---SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYE 178
Cdd:cd03265 90 GWENLYIHARLYGvpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499604739 179 VVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:cd03265 170 VWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRIIAE 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-200 |
8.09e-28 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.94 E-value: 8.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSeKERsrlrfksvGFILQASNLIPFLT 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AER--------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLELVDHLTG---SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYE 178
Cdd:PRK11248 87 VQDNVAFGLQLAGvekMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 499604739 179 VVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-218 |
9.15e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.36 E-value: 9.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQdghhEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERS 80
Cdd:PRK10895 1 MATLTAKNLAKAYK----GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 RlrfKSVGFILQASNLIPFLTVQQQ----LELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALY 156
Cdd:PRK10895 77 R---RGIGYLPQEASIFRRLSVYDNlmavLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 157 HDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDR-MLKYCDKVYRMQDGEL 218
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRII-EHLRDSGLGVLITDHNVReTLAVCERAYIVSQGHL 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-218 |
1.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.98 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGH-HEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSE-KERSR 81
Cdd:PRK13649 3 INLQNVSYTYQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRfKSVGFILQasnlIPFLTVQQQLELVDHLTG------SKEKAKANQLfDDLGITGLKHQL----PQELSGGERQRAAI 151
Cdd:PRK13649 83 IR-KKVGLVFQ----FPESQLFEETVLKDVAFGpqnfgvSQEEAEALAR-EKLALVGISESLfeknPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 152 ARALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTH--DDrMLKYCDKVYRMQDGEL 218
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLF-KKLHQSGMTIVLVTHlmDD-VANYADFVYVLEKGKL 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-217 |
1.36e-27 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 104.62 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTktFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLR 83
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNL--------IPFLTVQQQLELVDHltgSKEKAKANQLFDDL--------GITGLKhqlpqeLSGGERQ 147
Cdd:cd03251 76 -RQIGLVSQDVFLfndtvaenIAYGRPGATREEVEE---AARAANAHEFIMELpegydtviGERGVK------LSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 148 RAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGE 217
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTIENADRIVVLEDGK 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-217 |
2.02e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 103.51 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLr 83
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP---LDIAARNRI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksvGFILQASNLIPFLTVQQQLELVDHLTG-SKEKAKAN--QLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPA 160
Cdd:cd03269 73 ----GYLPEERGLYPKMKVIDQLVYLAQLKGlKKEEARRRidEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 161 LILADEPTASLDTEKAyEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:cd03269 149 LLILDEPFSGLDPVNV-ELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKGR 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-220 |
2.09e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 106.32 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 17 HHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTD-YthlseKERSRLRfKSVGFIL-QAS 94
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpF-----KRRKEFA-RRIGVVFgQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 NLIPFLTVQQQLELVDHLTG-SKEKAKAN--QLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASL 171
Cdd:COG4586 106 QLWWDLPAIDSFRLLKAIYRiPDAEYKKRldELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499604739 172 DTEKAYEVVKLLAKESKEKNKAIIMVTHDdrmlkycdkvyrMQDGE-LCQ 220
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHD------------MDDIEaLCD 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-172 |
2.11e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.85 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERs 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfkSVGFILQASNLIPFLTVQQQLELvdhltGSK----EKAKANQLFDD----LGITGLKHQLPQELSGGERQRAAIA 152
Cdd:PRK11650 77 -----DIAMVFQNYALYPHMSVRENMAY-----GLKirgmPKAEIEERVAEaariLELEPLLDRKPRELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 499604739 153 RALYHDPALILADEPTASLD 172
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-218 |
2.25e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.94 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 7 KQVTKTFQDGH-HEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLII---DGTDYTHLSEKER--- 79
Cdd:PRK13651 6 KNIVKIFNKKLpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKvle 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 ----SRLRFKSVGFILQASNLI----PFLTVQ--QQLELVDHLTG------SKEKAKANQLfDDLGITGLKHQL----PQ 139
Cdd:PRK13651 86 klviQKTRFKKIKKIKEIRRRVgvvfQFAEYQlfEQTIEKDIIFGpvsmgvSKEEAKKRAA-KYIELVGLDESYlqrsPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 140 ELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF-DNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKI 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-221 |
2.74e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.68 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 16 GHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfkSVGFILQASN 95
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 96 LIPFLTVQqqlELVDH---------LTGSKEKAKA-NQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILAD 165
Cdd:PRK10253 92 TPGDITVQ---ELVARgryphqplfTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 166 EPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKIVAQ 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-216 |
4.96e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.56 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 7 KQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfkS 86
Cdd:PRK09700 9 AGIGKSFGPVH----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 87 VGFILQASNLIPFLTVQQQLELVDHLTG----------SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALY 156
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 157 HDPALILADEPTASLdTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:PRK09700 162 LDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-221 |
5.25e-27 |
|
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: 103.33 E-value: 5.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTktFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLR 83
Cdd:cd03252 1 ITFEHVR--FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD---LALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQaSNLIPFLTVQQQLELVDHLTGSKEKAKANQLfddLGITGLKHQLPQ-----------ELSGGERQRAAIA 152
Cdd:cd03252 76 -RQVGVVLQ-ENVLFNRSIRDNIALADPGMSMERVIEAAKL---AGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 153 RALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-218 |
6.33e-27 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 103.38 E-value: 6.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLqTPSSGQLIIDGTDYTHLSEKERSRLRfksvGFILQASNLIPFLTVQQQLE 107
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 108 LVDHLTGSKEKAKA--NQLFDDLGITGLKHQLPQELSGGERQRAAIARALYH-------DPALILADEPTASLDTekAYE 178
Cdd:COG4138 92 LHQPAGASSEAVEQllAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV--AQQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499604739 179 VV--KLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG4138 170 AAldRLL-RELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-221 |
1.07e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.22 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfKSVGFILQASNLIPFLT 101
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR---AGIAYVPQGREIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLELVDHLTGSKEK---AKANQLFDDLgiTGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASL------D 172
Cdd:TIGR03410 92 VEENLLTGLAALPRRSRkipDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIqpsiikD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499604739 173 TEKayeVVKLLAkesKEKNKAIIMV-THDDRMLKYCDKVYRMQDGELCQE 221
Cdd:TIGR03410 170 IGR---VIRRLR---AEGGMAILLVeQYLDFARELADRYYVMERGRVVAS 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-220 |
1.13e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.85 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLqtPSSGQLIIDGTDythLSEKERSRLRfKSVGFILQASNLiPFLTVQQQ 105
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLnALLGFL--PYQGSLKINGIE---LRELDPESWR-KHLSWVGQNPQL-PHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 106 LELVDH------LTGSKEKAKANQLFDDLGiTGLKHQLPQE---LSGGERQRAAIARALYHDPALILADEPTASLDTEKA 176
Cdd:PRK11174 443 VLLGNPdasdeqLQQALENAWVSEFLPLLP-QGLDTPIGDQaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499604739 177 YEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:PRK11174 522 QLVMQALNAAS--RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-216 |
1.43e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 106.67 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 30 IEAGEFVAIIGPSGSGKSTFLTIAGGLQTPS---SGQLIIDGTDYTHLSEKERSrlrfksvGFILQASNLIPFLTVQQQL 106
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS-------AYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ------ELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQE------LSGGERQRAAIARALYHDPALILADEPTASLDTE 174
Cdd:TIGR00955 121 mfqahlRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499604739 175 KAYEVVKLLaKESKEKNKAIIMVTHDDRMLKYC--DKVYRMQDG 216
Cdd:TIGR00955 201 MAYSVVQVL-KGLAQKGKTIICTIHQPSSELFElfDKIILMAEG 243
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-216 |
1.46e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 104.57 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQvtktfQDGHHEINAlkatDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSG------QLIIDGTDYTHL 74
Cdd:PRK11144 1 MLELNFKQ-----QLGDLCLTV----NLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEKGICL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 75 S-EKERsrlrfksVGFILQASNLIPFLTVQQQLelvdhLTGSKEKAKANqlFDD----LGITGLKHQLPQELSGGERQRA 149
Cdd:PRK11144 72 PpEKRR-------IGYVFQDARLFPHYKVRGNL-----RYGMAKSMVAQ--FDKivalLGIEPLLDRYPGSLSGGEKQRV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 150 AIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:PRK11144 138 AIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSlDEILRLADRVVVLEQG 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-218 |
3.45e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 101.79 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 32 AGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfkSVGFILQASNLIPFLTVQqqlELVD- 110
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQLPAAEGMTVR---ELVAi 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 111 -----HLT----GSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVK 181
Cdd:PRK10575 109 grypwHGAlgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 499604739 182 LLAKESKEKNKAIIMVTHDDRM-LKYCDKVYRMQDGEL 218
Cdd:PRK10575 189 LVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEM 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-210 |
8.95e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.34 E-value: 8.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDgHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHlseKERSRl 82
Cdd:COG4152 1 MLELKGLTKRFGD-KT---AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfksVGFILQASNLIPFLTVQQQLELVDHLTG-SKEKAKAN--QLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDP 159
Cdd:COG4152 73 ----IGYLPEERGLYPKMKVGEQLVYLARLKGlSKAEAKRRadEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 160 ALILADEPTASLDTEKAyEVVKLLAKESKEKNKAIIMVTHD----DRMlkyCDKV 210
Cdd:COG4152 149 ELLILDEPFSGLDPVNV-ELLKDVIRELAAKGTTVIFSSHQmelvEEL---CDRI 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-218 |
1.99e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVlTFKQVTKTFQDGH-HEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYT-HLSEKE 78
Cdd:PRK13641 1 MSI-KFENVDYIYSPGTpMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 79 RSRLRfKSVGFILQASNLIPFL-TVQQQLELVDHLTGSKEKAKANQLFDDLGITGLKHQL----PQELSGGERQRAAIAR 153
Cdd:PRK13641 80 LKKLR-KKVSLVFQFPEAQLFEnTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisksPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLF-KDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-218 |
2.50e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 102.96 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 20 INALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLII----DGTDYTHLSEKERSRLRfKSVGFILQASN 95
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGRAK-RYIGILHQEYD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 96 LIPFLTVQQQLELVDHLTGSKEKAKANQL-------FDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPT 168
Cdd:TIGR03269 376 LYPHRTVLDNLTEAIGLELPDELARMKAVitlkmvgFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499604739 169 ASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:TIGR03269 456 GTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
1-199 |
3.38e-25 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 99.85 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTfKQVTKTFQdghhEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERs 80
Cdd:TIGR03522 1 MSIRV-SSLTKLYG----TQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQ- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rlrfKSVGFILQASNLIPFLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYH 157
Cdd:TIGR03522 75 ----RNIGYLPEHNPLYLDMYVREYLQFiagIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIH 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499604739 158 DPALILADEPTASLDTEKAYEVVKLLAkeSKEKNKAIIMVTH 199
Cdd:TIGR03522 151 DPKVLILDEPTTGLDPNQLVEIRNVIK--NIGKDKTIILSTH 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-218 |
4.24e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.49 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGhhEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTP---SSGQLIIDGTDythLSEKE 78
Cdd:PRK13640 4 NIVEFKHVSFTYPDS--KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGIT---LTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 79 RSRLRFKsVGFILQ-ASNLIPFLTVQQQLEL-VDHLTGSKEKAK--ANQLFDDLGITGLKHQLPQELSGGERQRAAIARA 154
Cdd:PRK13640 79 VWDIREK-VGIVFQnPDNQFVGATVGDDVAFgLENRAVPRPEMIkiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 155 LYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-218 |
5.79e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 96.35 E-value: 5.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRF-------KSVGFILQAS---NL 96
Cdd:cd03215 20 SFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIayvpedrKREGLVLDLSvaeNI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 97 IpfltvqqqlelvdhltgskekakanqlfddlgitglkhqLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKA 176
Cdd:cd03215 100 A---------------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499604739 177 YEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:cd03215 141 AEIYRLI-RELADAGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-220 |
7.35e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.79 E-value: 7.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDgHHEINALkatDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERsrlr 83
Cdd:PRK11432 7 VVLKNITKRFGS-NTVIDNL---NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fkSVGFILQASNLIPFLTVQQQLELVDHLTG-SKEKAK-----ANQLFDdlgITGLKHQLPQELSGGERQRAAIARALYH 157
Cdd:PRK11432 79 --DICMVFQSYALFPHMSLGENVGYGLKMLGvPKEERKqrvkeALELVD---LAGFEDRYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 158 DPALILADEPTASLDT-------EKAYEVVKLLAKESkeknkaiIMVTHDD-RMLKYCDKVYRMQDGELCQ 220
Cdd:PRK11432 154 KPKVLLFDEPLSNLDAnlrrsmrEKIRELQQQFNITS-------LYVTHDQsEAFAVSDTVIVMNKGKIMQ 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-218 |
9.38e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 9.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIdgtdythlsekeRSRLRfk 85
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------------PKGLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 sVGFILQASNLIPFLTV--------------QQQLELVDHLTGSKEK---------------------AKANQLFDDLGI 130
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVldtvldgdaelralEAELEELEAKLAEPDEdlerlaelqeefealggweaeARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 131 TGLKHQLP-QELSGGERQRAAIARALYHDPALILADEPTASLDtekaYEVVKLLAKESKEKNKAIIMVTHD----DRMlk 205
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDryflDRV-- 215
|
250
....*....|...
gi 499604739 206 yCDKVYRMQDGEL 218
Cdd:COG0488 216 -ATRILELDRGKL 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-221 |
9.91e-25 |
|
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: 96.44 E-value: 9.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLQ-TPSSGQLIIDGTDYTHLSEKERSRLrfkSVGFILQASNLIPFL 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAkTIMGHPKyEVTEGEILFKGEDITDLPPEERARL---GIFLAFQYPPEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 TVQQQLELVDhltgskekakanqlfddlgitglkhqlpQELSGGERQRAAIARALYHDPALILADEPTASLDTEkAYEVV 180
Cdd:cd03217 93 KNADFLRYVN----------------------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID-ALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499604739 181 KLLAKESKEKNKAIIMVTHDDRMLKYC--DKVYRMQDGELCQE 221
Cdd:cd03217 144 AEVINKLREEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKS 186
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
1.77e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.57 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 20 INALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYThlseKERSRLRFKSVGFILQASNLIPF 99
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT----KENIREVRKFVGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 100 -LTVQQQLELVDHLTGSKEKAKANQL---FDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEK 175
Cdd:PRK13652 93 sPTVEQDIAFGPINLGLDEETVAHRVssaLHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499604739 176 AYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVAY 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-218 |
2.87e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.39 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 19 EINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDgtDYTHLSE----KERSRLRfKSVGFILQAS 94
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG--DYAIPANlkkiKEVKRLR-KEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 NLIPFL-TVQQQLELVD-HLTGSKEKA--KANQLFDDLGI-TGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTA 169
Cdd:PRK13645 100 EYQLFQeTIEKDIAFGPvNLGENKQEAykKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499604739 170 SLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-218 |
3.06e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 96.78 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTF--QDG---HHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGT-----DY 71
Cdd:PRK15112 3 TLLEVRNLSKTFryRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 72 THLSekERSRLRFKSvgfilQASNLIPFLTVQQQLELVDHL-TGSKEKAKANQLFDDLGITGLK----HQLPQELSGGER 146
Cdd:PRK15112 83 SYRS--QRIRMIFQD-----PSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLpdhaSYYPHMLAPGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 147 QRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKY-CDKVYRMQDGEL 218
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEV 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-215 |
3.28e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.60 E-value: 3.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythlsekers 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 rLRFKS--------VGFILQASNLIPFLTVQQQLEL---------VDHltgSKEKAKANQLFDDLGI-----TGLKHqlp 138
Cdd:PRK11288 68 -MRFASttaalaagVAIIYQELHLVPEMTVAENLYLgqlphkggiVNR---RLLNYEAREQLEHLGVdidpdTPLKY--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 139 qeLSGGERQRAAIARALYHDPALILADEPTASL---DTEKAYEVVKLLakesKEKNKAIIMVTHddRMlkycDKVYRMQD 215
Cdd:PRK11288 141 --LSIGQRQMVEIAKALARNARVIAFDEPTSSLsarEIEQLFRVIREL----RAEGRVILYVSH--RM----EEIFALCD 208
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-217 |
3.33e-24 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 95.23 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEIN-ALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLQtPSSGQLIIDGtdythlsekersr 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLsALLGELE-KLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 lrfkSVGFILQAsnliPFL---TVQQQLelvdhLTGSK------EKA-KANQLFDDL--------------GITglkhql 137
Cdd:cd03250 67 ----SIAYVSQE----PWIqngTIRENI-----LFGKPfdeeryEKViKACALEPDLeilpdgdlteigekGIN------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 138 pqeLSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGE 217
Cdd:cd03250 128 ---LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-199 |
3.43e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.14 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGL-----QTPSSGQLIIDGTDythLS 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQD---IF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 76 EKERSRLRfKSVGFILQASNLIPFLTVQQQLEL---VDHLTGSK-----------EKAkanQLFDDLgitglKHQL---P 138
Cdd:PRK14247 74 KMDVIELR-RRVQMVFQIPNPIPNLSIFENVALglkLNRLVKSKkelqervrwalEKA---QLWDEV-----KDRLdapA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 139 QELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEknKAIIMVTH 199
Cdd:PRK14247 145 GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTH 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-221 |
4.01e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 4.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 16 GHHEinALKATDFSIEAGEFVAIIGPSGSGKSTfltiaGGLQ----TPSSGQLIIDGTDYTHLSEKE----RSRLRfksV 87
Cdd:PRK15134 297 DHNV--VVKNISFTLRPGETLGLVGESGSGKST-----TGLAllrlINSQGEIWFDGQPLHNLNRRQllpvRHRIQ---V 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 88 GFILQASNLIPFLTVQQQLE--LVDH---LTGSKEKAKANQLFDDLGI-TGLKHQLPQELSGGERQRAAIARALYHDPAL 161
Cdd:PRK15134 367 VFQDPNSSLNPRLNVLQIIEegLRVHqptLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 162 ILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLK-YCDKVYRMQDGELCQE 221
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRaLCHQVIVLRQGEVVEQ 507
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-216 |
7.09e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.13 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 19 EInaLKATDFSIEAGEFVAIIGPSGSGKSTF-LTIAG-GLQTPSSGQLIIDGTDYTHLSEKERSRL----------RFKS 86
Cdd:COG0396 14 EI--LKGVNLTIKPGEVHAIMGPNGSGKSTLaKVLMGhPKYEVTSGSILLDGEDILELSPDERARAgiflafqypvEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 87 VG---FILQASNLI--PFLTVQQQLELVdhltgsKEKAKANQLFDDLgitgLKHQLPQELSGGERQRAAIARALYHDPAL 161
Cdd:COG0396 92 VSvsnFLRTALNARrgEELSAREFLKLL------KEKMKELGLDEDF----LDRYVNEGFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 162 ILADEPTASLDTEkAYEVVKLLAKESKEKNKAIIMVTHDDRMLKY--CDKVYRMQDG 216
Cdd:COG0396 162 AILDETDSGLDID-ALRIVAEGVNKLRSPDRGILIITHYQRILDYikPDFVHVLVDG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-218 |
9.84e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.46 E-value: 9.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 18 HEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLII-----------DGTDYTHLSEKERS--RLRf 84
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnHELITNPYSKKIKNfkELR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 85 KSVGFILQASNLIPFL-TVQQQL-----ELVDHLTGSKEKAKANqlfddLGITGLKHQL----PQELSGGERQRAAIARA 154
Cdd:PRK13631 116 RRVSMVFQFPEYQLFKdTIEKDImfgpvALGVKKSEAKKLAKFY-----LNKMGLDDSYlersPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 155 LYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
1.15e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.20 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTktFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTdytHLSEKERSR 81
Cdd:PRK13648 6 SIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRfKSVGFILQ-ASNLIPFLTVQQQLE--LVDHLTGSKE-KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYH 157
Cdd:PRK13648 81 LR-KHIGIVFQnPDNQFVGSIVKYDVAfgLENHAVPYDEmHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 158 DPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-216 |
1.77e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 7 KQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKE-RSRlrfk 85
Cdd:PRK13647 8 EDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSK---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 sVGFILQ-------ASNL---IPFLTVQQQLelvdhlTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARAL 155
Cdd:PRK13647 81 -VGLVFQdpddqvfSSTVwddVAFGPVNMGL------DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 156 YHDPALILADEPTASLDTEKAYEVVKLLAKESKEkNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDvDLAAEWADQVIVLKEG 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-217 |
2.61e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKST-------FLTIAGGlqTPSSGQLII-----DGTD 70
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGG--LVQCDKMLLrrrsrQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 71 YTHLSEKERSRLRFKSVGFILQA--SNLIPFLTVQQQ----LELVDHLTGSKEKAKANQLFDDLGITGLKHQL---PQEL 141
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQiaesIRLHQGASREEAMVEAKRMLDQVRIPEAQTILsryPHQL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 142 SGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRML-KYCDKVYRMQDGE 217
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGE 246
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-218 |
2.81e-23 |
|
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: 97.09 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDghHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKE-RSRL 82
Cdd:TIGR02203 331 VEFRNVTFRYPG--RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RFKSVGFIL----QASNLIPFLTVQQQLELVDHltgSKEKAKANQLFDDLGItGLKHQLPQE---LSGGERQRAAIARAL 155
Cdd:TIGR02203 409 ALVSQDVVLfndtIANNIAYGRTEQADRAEIER---ALAAAYAQDFVDKLPL-GLDTPIGENgvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 156 YHD-PALILaDEPTASLDTEKAYEVVKLLakESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:TIGR02203 485 LKDaPILIL-DEATSALDNESERLVQAAL--ERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-213 |
3.64e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 95.16 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATD---FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRfKSVGFILQ---ASn 95
Cdd:PRK15079 33 TLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQdplAS- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 96 LIPFLTV----QQQLELV-DHLTGSKEKAKANQLFDDLGI-TGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTA 169
Cdd:PRK15079 111 LNPRMTIgeiiAEPLRTYhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499604739 170 SLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKY-CDKVYRM 213
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-218 |
8.10e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 92.30 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLqTPSSGQLIIDGTDYTHLSEKERSRLRfksvGFILQASNLIPFLTVQQ--Q 105
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQylT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 106 LELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQR---AA----IARALYHDPALILADEPTASLD-TEKA- 176
Cdd:PRK03695 92 LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlAAvvlqVWPDINPAGQLLLLDEPMNSLDvAQQAa 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499604739 177 -YEVVKLLAkeskEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK03695 172 lDRLLSELC----QQGIAVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-221 |
9.70e-23 |
|
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: 92.22 E-value: 9.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 19 EINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLRfKSVGFILQASNLIP 98
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD---IRDLNLRWLR-SQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 99 fLTVQQQLELVDH-LTGSKEKAKANQLFDDLGITGLKHQLPQE-------LSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:cd03249 91 -GTIAENIRYGKPdATDEEVEEAAKKANIHDFIMSLPDGYDTLvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499604739 171 LDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:cd03249 170 LDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQ 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-221 |
9.76e-23 |
|
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: 95.64 E-value: 9.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQT--PSSGQLII--------------- 66
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 67 -DGT--------------DYTHLSEKERSRLRfKSVGFILQASnlipFLTVQQQLELVD-----HLTGSKEKAKANQLFD 126
Cdd:TIGR03269 77 kVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRT----FALYGDDTVLDNvlealEEIGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 127 DLGITGLKHQ---LPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTH-DDR 202
Cdd:TIGR03269 152 LIEMVQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwPEV 231
|
250
....*....|....*....
gi 499604739 203 MLKYCDKVYRMQDGELCQE 221
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEE 250
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-221 |
1.33e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.36 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGhheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRl 82
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfKSVGFILQASNlIPFL--TVQQQLELVDH---LTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYH 157
Cdd:PRK13644 77 --KLVGIVFQNPE-TQFVgrTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 158 DPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERI-KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-205 |
1.75e-22 |
|
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: 90.50 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGtdyTHLSEKERSRLRfkSVGFILQASNLIPFLTVQQQL 106
Cdd:TIGR01189 20 SFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG---TPLAEQRDEPHE--NILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ELVDHLTGSkEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKayevVKLLA-- 184
Cdd:TIGR01189 95 HFWAAIHGG-AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG----VALLAgl 169
|
170 180
....*....|....*....|..
gi 499604739 185 -KESKEKNKAIIMVTHDDRMLK 205
Cdd:TIGR01189 170 lRAHLARGGIVLLTTHQDLGLV 191
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-218 |
1.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.10 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFqDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERS 80
Cdd:PRK13650 2 SNIIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 RLRFKsVGFILQ-ASNLIPFLTVQQQLEL------VDHltgSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIAR 153
Cdd:PRK13650 78 DIRHK-IGMVFQnPDNQFVGATVEDDVAFglenkgIPH---EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 154 ALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-210 |
1.80e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 93.05 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPS----SGQLIIDGTDYTHLSE 76
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 77 KERSRLRFKSVGFILQ--ASNLIPFLTVQQQLELV---DHLTGS--------KEKAKAnqLFDDLGITGLKHQL---PQE 140
Cdd:COG4170 81 RERRKIIGREIAMIFQepSSCLDPSAKIGDQLIEAipsWTFKGKwwqrfkwrKKRAIE--LLHRVGIKDHKDIMnsyPHE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 141 LSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKV 210
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTI 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-220 |
2.39e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.79 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLRfKSVGFILQASNLIPFLTV 102
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP---LVQYDHHYLH-RQVALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQLELVDHLTGSKEKAKANQLFDDLGITGLKH-------QLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEK 175
Cdd:TIGR00958 573 ENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNgydtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499604739 176 AYevvkLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:TIGR00958 653 EQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-216 |
2.68e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.49 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEINALkatDFSIEAGEFVAIIGPSGSGKSTFL-TIAGgLQTPSSGQLII-DGTDYTHLSEKersr 81
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDL---SLSLKPGERLLITGPSGSGKSTLLrAIAG-LWPYGSGRIARpAGARVLFLPQR---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 lrfksvgfilqasnliPFL---TVQQQLeLVDHLTGSKEKAKANQLFDDLGITGLKHQL------PQELSGGERQRAAIA 152
Cdd:COG4178 435 ----------------PYLplgTLREAL-LYPATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499604739 153 RALYHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDG 216
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREEL--PGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-221 |
3.37e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKS-TFLTIAGgLQTPSSGQLIIDGTDYTHLSEKERSRLRF-------KSVGFILQAS---N 95
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTeLARALFG-ADPADSGEIRLDGKPVRIRSPRDAIRAGIayvpedrKGEGLVLDLSireN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 96 LIpfLTVQQQLE---LVDHltgSKEKAKANQLFDDLGI-TGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASL 171
Cdd:COG1129 351 IT--LASLDRLSrggLLDR---RRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499604739 172 DTE-KA--YEVVKLLAKEskekNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:COG1129 426 DVGaKAeiYRLIRELAAE----GKAVIVISSElPELLGLSDRILVMREGRIVGE 475
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-221 |
4.37e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.23 E-value: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLRfKSVGFILQ-ASNLIPFL 100
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDVR-RQVGMVFQnPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 TVQQQL------------ELVDhltgskekaKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPT 168
Cdd:PRK13635 98 TVQDDVafglenigvpreEMVE---------RVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499604739 169 ASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-218 |
4.58e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.55 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTdythlsekersRL 82
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK-----------PV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RFKS--------VGFILQASNLIPFLTVqqqLE-----LVDHLTGSKEKAKANQLFDDLGIT-GLK---HQLPQELSGGE 145
Cdd:COG3845 70 RIRSprdaialgIGMVHQHFMLVPNLTV---AEnivlgLEPTKGGRLDRKAARARIRELSERyGLDvdpDAKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 146 RQRAAIARALYHDPA-LILaDEPTASL---DTEKAYEVVKLLAKEskekNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG3845 147 QQRVEILKALYRGARiLIL-DEPTAVLtpqEADELFEILRRLAAE----GKSIIFITHKlREVMAIADRVTVLRRGKV 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-221 |
5.41e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.92 E-value: 5.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYThlSEKERSRLRfKSVGFILQ-ASNLIPFL 100
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLWDIR-NKAGMVFQnPDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 TVQQQLELVDHLTG--SKE-KAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAY 177
Cdd:PRK13633 102 IVEEDVAFGPENLGipPEEiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499604739 178 EVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-201 |
6.69e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfksvgFILQASNLIPFLTVQQQL 106
Cdd:PRK13539 22 SFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH-------YLGHRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ELVDHLTGSKEKAKANQLfDDLGITGLKHqLP-QELSGGERQRAAIARAL-YHDPALILaDEPTASLDTeKAYEVVKLLA 184
Cdd:PRK13539 95 EFWAAFLGGEELDIAAAL-EAVGLAPLAH-LPfGYLSAGQKRRVALARLLvSNRPIWIL-DEPTAALDA-AAVALFAELI 170
|
170
....*....|....*..
gi 499604739 185 KESKEKNKAIIMVTHDD 201
Cdd:PRK13539 171 RAHLAQGGIVIAATHIP 187
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-199 |
8.38e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.10 E-value: 8.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFL--------TIAGglqTPSSGQLIIDGTD-YThlSEKERSRLRfKSVGFILQ 92
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmndLIPG---ARVEGEILLDGEDiYD--PDVDVVELR-RRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 93 ASNLIPF--------------LTVQQQL-ELVdhltgskEKA--KANqLFDDLgitglKHQLPQ---ELSGGERQRAAIA 152
Cdd:COG1117 100 KPNPFPKsiydnvayglrlhgIKSKSELdEIV-------EESlrKAA-LWDEV-----KDRLKKsalGLSGGQQQRLCIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499604739 153 RALYHDPALILADEPTASLD---TEKAYEVVKLLAKESkeknkAIIMVTH 199
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDpisTAKIEELILELKKDY-----TIVIVTH 211
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-218 |
1.11e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 92.64 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 33 GEFVAIIGPSGSGKSTFLT-IAGGLQTPS-SGQLIIDGTDYThlsekersRLRFKSVGFILQASNLIPFLTVQQQL---- 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANNRKPT--------KQILKRTGFVTQDDILYPHLTVRETLvfcs 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 --ELVDHLTGSKEKAKANQLFDDLGITG-----LKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEV 179
Cdd:PLN03211 166 llRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190
....*....|....*....|....*....|....*....
gi 499604739 180 VKLLAKESkEKNKAIIMVTHddrmlKYCDKVYRMQDGEL 218
Cdd:PLN03211 246 VLTLGSLA-QKGKTIVTSMH-----QPSSRVYQMFDSVL 278
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-220 |
2.89e-21 |
|
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: 87.55 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 21 NALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSekeRSRLRfKSVGFILQ-------- 92
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SRISIIPQdpvlfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 93 -ASNLIPFlTVQQQLELVDHLtgskEKAKANQLFDDLGItGLKHQLPQE---LSGGERQRAAIARALYHDPALILADEPT 168
Cdd:cd03244 94 iRSNLDPF-GEYSDEELWQAL----ERVGLKEFVESLPG-GLDTVVEEGgenLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499604739 169 ASLDTEKAYEVVKLLakESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03244 168 ASVDPETDALIQKTI--REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-218 |
3.90e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQ-DGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRFKSVGFILQasnlIPFLTVQQQLELVDHLTG------SKEKAKANQLfDDLGITGLKHQL----PQELSGGERQRAAI 151
Cdd:PRK13643 81 PVRKKVGVVFQ----FPESQLFEETVLKDVAFGpqnfgiPKEKAEKIAA-EKLEMVGLADEFweksPFELSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 152 ARALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTH-DDRMLKYCDKVYRMQDGEL 218
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHI 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-220 |
5.52e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.42 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYThLSEKERSRLR 83
Cdd:PRK10522 323 LELRNVTFAYQDNGF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-AEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 FKSVgfilqasnlipFLTVQqqleLVDHLTGSKEKAKANQLFDD-LGITGLKHQLPQE--------LSGGERQRAAIARA 154
Cdd:PRK10522 399 FSAV-----------FTDFH----LFDQLLGPEGKPANPALVEKwLERLKMAHKLELEdgrisnlkLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 155 LYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-176 |
8.69e-21 |
|
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: 89.88 E-value: 8.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTktFQ-DGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKErsrL 82
Cdd:COG5265 358 VRFENVS--FGyDPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---L 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfKSVGfilqasnLIPFLTV------------------QQQLElvdhltgskEKAKANQLfDDL------------GITG 132
Cdd:COG5265 431 R-AAIG-------IVPQDTVlfndtiayniaygrpdasEEEVE---------AAARAAQI-HDFieslpdgydtrvGERG 492
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499604739 133 LKhqlpqeLSGGERQRAAIARALYHDPALILADEPTASLD--TEKA 176
Cdd:COG5265 493 LK------LSGGEKQRVAIARTLLKNPPILIFDEATSALDsrTERA 532
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-218 |
2.72e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.55 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 16 GHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRL--------RFKsV 87
Cdd:COG3845 267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLG-R 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 88 GFILQAS---NLIpfLTVQQQLELVDH--LTGSKEKAKANQLFDDLGI-TGLKHQLPQELSGGERQRAAIARALYHDPAL 161
Cdd:COG3845 346 GLVPDMSvaeNLI--LGRYRRPPFSRGgfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 162 ILADEPTASLDTEKAYEVVKLLAKEsKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:COG3845 424 LIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDlDEILALSDRIAVMYEGRI 480
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-201 |
3.09e-20 |
|
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: 84.47 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLRfkSVGFILQASNLIPFLTVQQQL 106
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP---LDFQRDSIAR--GLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ELV--DHLTGSKEKAkanqlFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLA 184
Cdd:cd03231 95 RFWhaDHSDEQVEEA-----LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*..
gi 499604739 185 KESkEKNKAIIMVTHDD 201
Cdd:cd03231 170 GHC-ARGGMVVLTTHQD 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-217 |
3.89e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.36 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHheinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYT-----HLSEKE 78
Cdd:PRK11701 7 LSVRGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 79 RSRLRFKSVGFILQ--ASNLIPFLT----VQQQLELVDHLTGSKEKAKANQLFDDLGITGLK-HQLPQELSGGERQRAAI 151
Cdd:PRK11701 83 RRRLLRTEWGFVHQhpRDGLRMQVSaggnIGERLMAVGARHYGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 152 ARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD---DRMLKycDKVYRMQDGE 217
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlavARLLA--HRLLVMKQGR 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
33-200 |
5.08e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.59 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 33 GEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSekeRSRL---RfKSVGFILQASNLIPFLTVQQQLE-- 107
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMS---RSRLytvR-KRMSMLFQSGALFTDMNVFDNVAyp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 108 LVDHLTGSKEKAKANQL--FDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLak 185
Cdd:PRK11831 109 LREHTQLPAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLI-- 186
|
170
....*....|....*....
gi 499604739 186 esKEKNKAI----IMVTHD 200
Cdd:PRK11831 187 --SELNSALgvtcVVVSHD 203
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
28-220 |
5.96e-20 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 87.64 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLRfKSVGFILQASNLIPfLTVQQQLE 107
Cdd:TIGR01192 356 FEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGID---INTVTRESLR-KSIATVFQDAGLFN-RSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 108 L------VDHLTGSKEKAKANQLFDDL--GITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEV 179
Cdd:TIGR01192 431 LgregatDEEVYEAAKAAAAHDFILKRsnGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARV 510
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499604739 180 VKllAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:TIGR01192 511 KN--AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIE 549
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-222 |
6.04e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDghHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRLR 83
Cdd:PRK11176 342 IEFRNVTFTYPG--KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASNLipFL-TVQQQLELVDHLTGSKEK----AKANQLFDdlGITGLKHQLPQE-------LSGGERQRAAI 151
Cdd:PRK11176 417 -NQVALVSQNVHL--FNdTIANNIAYARTEQYSREQieeaARMAYAMD--FINKMDNGLDTVigengvlLSGGQRQRIAI 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 152 ARALYHD-PALILaDEPTASLDTEKAYEVVKLLakESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCqER 222
Cdd:PRK11176 492 ARALLRDsPILIL-DEATSALDTESERAIQAAL--DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIV-ER 559
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-217 |
7.26e-20 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 86.01 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTP----SSGQLIIDGTDYTHLSE 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 77 KERSRLRFKSVGFILQ--ASNLIPFLTVQQQLelVDHLTGSKEKA-----------KANQLFDDLGITGLK---HQLPQE 140
Cdd:PRK15093 81 RERRKLVGHNVSMIFQepQSCLDPSERVGRQL--MQNIPGWTYKGrwwqrfgwrkrRAIELLHRVGIKDHKdamRSFPYE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 141 LSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRML-KYCDKVYRMQDGE 217
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINVLYCGQ 236
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-206 |
7.28e-20 |
|
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: 84.77 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKersrLRFKSVGfilqasnlipflTV 102
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY----IKADYEG------------TV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQLELV--DHLTGSKEKakaNQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVV 180
Cdd:cd03237 79 RDLLSSItkDFYTHPYFK---TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180
....*....|....*....|....*.
gi 499604739 181 KLLAKESKEKNKAIIMVTHDDRMLKY 206
Cdd:cd03237 156 KVIRRFAENNEKTAFVVEHDIIMIDY 181
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-206 |
8.81e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.85 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 19 EINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDgtdythlsekersrlrfksvgfilqasnlIP 98
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------------------VP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 99 FLTVQQQLELVDHLTGSKEKAKANQLfddLGITGLKH-----QLPQELSGGERQRAAIARALYHDPALILADEPTASLDT 173
Cdd:COG2401 93 DNQFGREASLIDAIGRKGDFKDAVEL---LNAVGLSDavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190
....*....|....*....|....*....|...
gi 499604739 174 EKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKY 206
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVATHHYDVIDD 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-218 |
9.43e-20 |
|
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: 83.74 E-value: 9.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHH------------------EINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLI 65
Cdd:cd03220 1 IELENVSKSYPTYKGgssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 66 IDGTDythlsekeRSRLRFkSVGFilqasnlIPFLTVQQQLELVDHLTGSKeKAKANQLFDD-LGITGLKH--QLP-QEL 141
Cdd:cd03220 81 VRGRV--------SSLLGL-GGGF-------NPELTGRENIYLNGRLLGLS-RKEIDEKIDEiIEFSELGDfiDLPvKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 142 SGGERQRAAIARALYHDPALILADEPTASLDT---EKAYEVVkllaKESKEKNKAIIMVTHDDRMLK-YCDKVYRMQDGE 217
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAafqEKCQRRL----RELLKQGKTVILVSHDPSSIKrLCDRALVLEKGK 219
|
.
gi 499604739 218 L 218
Cdd:cd03220 220 I 220
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
28-218 |
1.27e-19 |
|
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: 84.11 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTD-----YTHLSEKERSRLRFKSVGFILQASNLIPFLTV 102
Cdd:TIGR02323 24 FDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMRTEWGFVHQNPRDGLRMRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQLELVDHL--TGSKE----KAKANQLFDDLGI-TGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEK 175
Cdd:TIGR02323 104 SAGANIGERLmaIGARHygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499604739 176 AYEVVKLLAKESKEKNKAIIMVTHD---DRMLkyCDKVYRMQDGEL 218
Cdd:TIGR02323 184 QARLLDLLRGLVRDLGLAVIIVTHDlgvARLL--AQRLLVMQQGRV 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-218 |
1.49e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MS-VLTFKQVTKTFQ------------------DGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSS 61
Cdd:COG1134 1 MSsMIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 62 GQLIIDGtdythlsekersrlrfkSVGFILQ-ASNLIPFLTVQQQLELVDHLTG-SKEKAKAnqLFDDlgI---TGLKHQ 136
Cdd:COG1134 81 GRVEVNG-----------------RVSALLElGAGFHPELTGRENIYLNGRLLGlSRKEIDE--KFDE--IvefAELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 137 LPQEL---SGGERQRAAIARALYHDPALILADEPTASLDT---EKAYEVVkllaKESKEKNKAIIMVTHDDRMLK-YCDK 209
Cdd:COG1134 140 IDQPVktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqKKCLARI----RELRESGRTVIFVSHSMGAVRrLCDR 215
|
....*....
gi 499604739 210 VYRMQDGEL 218
Cdd:COG1134 216 AIWLEKGRL 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-217 |
1.53e-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: 86.42 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSS--GQLIIDGTDY--THLSEKE 78
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 79 RsrlrfKSVGFILQASNLIPFLTVQQQLELVDHLTGSKEKA-------KANQLFDDLGITGLKHQLP-QELSGGERQRAA 150
Cdd:TIGR02633 77 R-----AGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMaynamylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 151 IARALYHDPALILADEPTASLdTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSL-TEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-206 |
2.55e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 85.63 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEA-------GEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTdythLSEKERsrlrfksvgFILQASNLipf 99
Cdd:PRK13409 352 DFSLEVeggeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK----ISYKPQ---------YIKPDYDG--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 100 lTVQQQLELV-DHLTGSKEKakaNQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYE 178
Cdd:PRK13409 416 -TVEDLLRSItDDLGSSYYK---SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180
....*....|....*....|....*...
gi 499604739 179 VVKLLAKESKEKNKAIIMVTHDDRMLKY 206
Cdd:PRK13409 492 VAKAIRRIAEEREATALVVDHDIYMIDY 519
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-220 |
3.79e-19 |
|
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: 81.69 E-value: 3.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLS-EKERSRLrfksvGFILQASNLIPFl 100
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSL-----TIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 TVQQQLELVDHLTGSkekakanQLFDDLGIT--GLKhqlpqeLSGGERQRAAIARALYHDPALILADEPTASLDTEKAYE 178
Cdd:cd03369 97 TIRSNLDPFDEYSDE-------EIYGALRVSegGLN------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499604739 179 VVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03369 164 IQKTIREEF--TNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-215 |
7.80e-19 |
|
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: 79.89 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIdgtdythlSEKERsrlrfksVGFILQAsnliPFLTv 102
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------PEGED-------LLFLPQR----PYLP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 qqqlelvdhlTGSkekakanqlfddlgitgLKHQL--P--QELSGGERQRAAIARALYHDPALILADEPTASLDTE---K 175
Cdd:cd03223 77 ----------LGT-----------------LREQLiyPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEEsedR 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499604739 176 AYEVVkllakesKEKNKAIIMVTHDDRMLKYCDKVYRMQD 215
Cdd:cd03223 130 LYQLL-------KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-217 |
1.07e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDghHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYthlsekersrlr 83
Cdd:cd03221 1 IELENLSKTYGG--KLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksVGFILQasnlipfltvqqqlelvdhltgskekakanqlfddlgitglkhqlpqeLSGGERQRAAIARALYHDPALIL 163
Cdd:cd03221 65 ---IGYFEQ------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 164 ADEPTASLDTEKayevVKLLAKESKEKNKAIIMVTHDDRML-KYCDKVYRMQDGE 217
Cdd:cd03221 94 LDEPTNHLDLES----IEALEEALKEYPGTVILVSHDRYFLdQVATKIIELEDGK 144
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-217 |
1.20e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.83 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQtPS---SGQLIIDGTD--YTHLSEK 77
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEElqASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 78 ERsrlrfKSVGFILQASNLIPFLTVQQQLELVDHLTGS------KEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAI 151
Cdd:PRK13549 80 ER-----AGIAIIHQELALVKELSVLENIFLGNEITPGgimdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 152 ARALYHDPALILADEPTASLdTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:PRK13549 155 AKALNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-174 |
1.30e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSekeRSRLRfKSVGFILQASNLIPfLT 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDAGLFN-RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQL----------ELVDHLtgskEKAKANQLFD--DLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTA 169
Cdd:PRK13657 425 IEDNIrvgrpdatdeEMRAAA----ERAQAHDFIErkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
....*
gi 499604739 170 SLDTE 174
Cdd:PRK13657 501 ALDVE 505
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-210 |
1.77e-18 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 80.28 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGtdythlsekERSRLRFKSVGFILQASNL---IPFLTVQQ 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---------ASPGKGWRHIGYVPQRHEFawdFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 105 QLELVDHLTG------SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYE 178
Cdd:TIGR03771 72 VMSGRTGHIGwlrrpcVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190
....*....|....*....|....*....|...
gi 499604739 179 VVKLLAKESKEKNkAIIMVTHD-DRMLKYCDKV 210
Cdd:TIGR03771 152 LTELFIELAGAGT-AILMTTHDlAQAMATCDRV 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-216 |
2.30e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.79 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 20 INALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfksvGFIL--QASNLI 97
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL-----GIYLvpQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 98 PFLTVQQQLeLVDHLTGSKEKAKANQLFDDLGItglkhQLPQELSGG-----ERQRAAIARALYHDPALILADEPTASL- 171
Cdd:PRK15439 99 PNLSVKENI-LFGLPKRQASMQKMKQLLAALGC-----QLDLDSSAGslevaDRQIVEILRGLMRDSRILILDEPTASLt 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499604739 172 --DTEKAYEVVKLLakesKEKNKAIIMVTHDDRML-KYCDKVYRMQDG 216
Cdd:PRK15439 173 paETERLFSRIREL----LAQGVGIVFISHKLPEIrQLADRISVMRDG 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-204 |
2.69e-18 |
|
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: 82.91 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 29 SIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTdythLSEKERsrlrfksvgFILQASNLipflTVQQQLEL 108
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK----ISYKPQ---------YISPDYDG----TVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 109 V--DHLTGSKEKakaNQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKE 186
Cdd:COG1245 425 AntDDFGSSYYK---TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180
....*....|....*....|....*.
gi 499604739 187 SKEKNKAIIMVTHD--------DRML 204
Cdd:COG1245 502 AENRGKTAMVVDHDiylidyisDRLM 527
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-199 |
3.99e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 3.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDgHHEINALkatDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSR 81
Cdd:PRK13537 6 APIDFRNVEKRYGD-KLVVDGL---SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 lrfksVGFILQASNLIPFLTVQQQLELVDH---LTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHD 158
Cdd:PRK13537 82 -----VGVVPQFDNLDPDFTVRENLLVFGRyfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499604739 159 PALILADEPTASLDTEK---AYEVVK-LLAkeskeKNKAIIMVTH 199
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQArhlMWERLRsLLA-----RGKTILLTTH 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-216 |
4.36e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.03 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTKTFQDgHHEINALKatdFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTdythlSEKERSRLRFK 85
Cdd:PRK13536 44 LAGVSKSYGD-KAVVNGLS---FTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV-----PVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 SVGFILQASNLIPFLTVQQQLELVDHLTGSKEKAKANQLFDDLGITGLKHQLP---QELSGGERQRAAIARALYHDPALI 162
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADarvSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499604739 163 LADEPTASLDTEKAY----EVVKLLAkeskeKNKAIIMVTH----DDRMlkyCDKVYRMQDG 216
Cdd:PRK13536 195 ILDEPTTGLDPHARHliweRLRSLLA-----RGKTILLTTHfmeeAERL---CDRLCVLEAG 248
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
7.48e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.15 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQdghhEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLsekERS 80
Cdd:PRK11614 3 KVMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 RLRFKSVGFILQASNLIPFLTVQQQLEL----VDHLTGSKEKAKANQLFDDLgiTGLKHQLPQELSGGERQRAAIARALY 156
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLAMggffAERDQFQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 157 HDPALILADEPT---ASLDTEKAYEVVKLLakesKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK11614 154 SQPRLLLLDEPSlglAPIIIQQIFDTIEQL----REQGMTIFLVEQNaNQALKLADRGYVLENGHVVLE 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-222 |
7.61e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 7.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDghheINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRl 82
Cdd:PRK10762 4 LLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfKSVGFILQASNLIPFLTVQQQL----ELVDHLTG---SKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARAL 155
Cdd:PRK10762 79 --AGIGIIHQELNLIPQLTIAENIflgrEFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 156 YHDPALILADEPTASL-DTEKA--YEVVkllaKESKEKNKAIIMVTHddRM---LKYCDKVYRMQDGELCQER 222
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETEslFRVI----RELKSQGRGIVYISH--RLkeiFEICDDVTVFRDGQFIAER 223
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-174 |
7.88e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 78.35 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGtdyTHLSEKERSRLrfksVGFILQASNLIPFLTVQQQL 106
Cdd:PRK13543 31 DFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRF----MAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 107 ELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARaLYHDPA-LILADEPTASLDTE 174
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPApLWLLDEPYANLDLE 171
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-218 |
1.10e-17 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 78.28 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 6 FKQVTKTFQDGHHeINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDG---TDYTHlsEKERSRL 82
Cdd:cd03248 14 FQNVTFAYPTRPD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpiSQYEH--KYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RFKSVGFILQASNLIPFLTVQQQLELVDHLTGSKEKAKANQLfddlgITGLKHQLPQE-------LSGGERQRAAIARAL 155
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSF-----ISELASGYDTEvgekgsqLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 156 YHDPALILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWP--ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-218 |
1.20e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKStfLTIAGGLQ------TPSSGQLIIDGTDYthlsekERSRLRFKSVGFILQA--SNLIP 98
Cdd:PRK10418 23 SLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPV------APCALRGRKIATIMQNprSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 99 FLTVQQQ-LELVDHLTGSKEKAKANQLFDDLGITGLKHQL---PQELSGGERQRAAIARALYHDPALILADEPTASLDTE 174
Cdd:PRK10418 95 LHTMHTHaRETCLALGKPADDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499604739 175 KAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYC-DKVYRMQDGEL 218
Cdd:PRK10418 175 AQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRI 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-220 |
1.80e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.55 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDY---THLSEKERSRLRfKSVGFILQASNLIPF 99
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLR-KEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 100 LTVQQQLELVDHLTGSKEKAKANQLFDD-LGITGLKHQL-------PQELSGGERQRAAIARALYHDPALILADEPTASL 171
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEEcLRKVGLWKEVydrlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499604739 172 DTEKAYEVVKLLAKESKEknKAIIMVTHD-DRMLKYCDKVYRMQDGELCQ 220
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNpQQVARVADYVAFLYNGELVE 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-221 |
2.56e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 19 EINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTdytHLSEKERSRLRfKSVGFILQ-ASNLI 97
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLR-RKIGMVFQnPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 98 PFLTVQQQLELVDHLTGSKEK---AKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTE 174
Cdd:PRK13642 95 VGATVEDDVAFGMENQGIPREemiKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499604739 175 KAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-218 |
3.11e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.76 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 19 EINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGlqTPS----SGQLIIDGTDYTHLSEKERSRLrfksvGFIL--Q 92
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHL-----GIFLafQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 93 ASNLIPFLTVQQQLELVdhlTGSKEKAKANQLFD---------------DLGITGLKHQLPQELSGGERQRAAIARALYH 157
Cdd:CHL00131 92 YPIEIPGVSNADFLRLA---YNSKRKFQGLPELDplefleiineklklvGMDPSFLSRNVNEGFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 158 DPALILADEPTASLDTEkAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYC--DKVYRMQDGEL 218
Cdd:CHL00131 169 DSELAILDETDSGLDID-ALKIIAEGINKLMTSENSIILITHYQRLLDYIkpDYVHVMQNGKI 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-200 |
9.43e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 19 EINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRfKSVGFILQA--SNL 96
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 97 IPFLTV----QQQLELVDHLTGSKEKAKANQLFDDLGITGlKH--QLPQELSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:PRK10261 415 DPRQTVgdsiMEPLRVHGLLPGKAAAARVAWLLERVGLLP-EHawRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190
....*....|....*....|....*....|
gi 499604739 171 LDTEKAYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHD 523
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-218 |
1.14e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDghHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLQtPSSGQLIIdGTdythlsekersR 81
Cdd:COG0488 315 VLELEGLSKSYGD--KTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLkLLAGELE-PDSGTVKL-GE-----------T 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRfksVGFILQA-SNLIPFLTVQQqlELVDHLTGSKEKaKANQLFDDLGITGLKHQLP-QELSGGERQRAAIARALYHDP 159
Cdd:COG0488 378 VK---IGYFDQHqEELDPDKTVLD--ELRDGAPGGTEQ-EVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 160 ALILADEPTASLDTE---------KAYEvvkllakeskeknKAIIMVTHDDRML-KYCDKVYRMQDGEL 218
Cdd:COG0488 452 NVLLLDEPTNHLDIEtlealeealDDFP-------------GTVLLVSHDRYFLdRVATRILEFEDGGV 507
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-200 |
1.24e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVL-TFKQVTKTFqdGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLiidgtdythlseKER 79
Cdd:PRK09544 1 MTSLvSLENVSVSF--GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 SRLRfksVGFILQASNLIPF--LTVQQQLEL-----VDHLTGSKEKAKANQLFDdlgitglkhQLPQELSGGERQRAAIA 152
Cdd:PRK09544 65 GKLR---IGYVPQKLYLDTTlpLTVNRFLRLrpgtkKEDILPALKRVQAGHLID---------APMQKLSGGETQRVLLA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499604739 153 RALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-199 |
1.37e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.03 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGL-----QTPSSGQLIIDGTDyTHLSEKERSRLRfKSVGFILQASNLI 97
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRN-IYSPDVDPIEVR-REVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 98 PFLTVQQQLEL---VDHLTGSKEKA--------KANQLFDDLgitglKHQL---PQELSGGERQRAAIARALYHDPALIL 163
Cdd:PRK14267 98 PHLTIYDNVAIgvkLNGLVKSKKELdervewalKKAALWDEV-----KDRLndyPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 499604739 164 ADEPTASLDTEKAYEVVKLLAKESKEknKAIIMVTH 199
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTH 206
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-217 |
1.53e-16 |
|
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: 74.61 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTiAGGLQTPS----SGQLIIDGTDYTHLSE 76
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLK-ALANRTEGnvsvEGDIHYNGIPYKEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 77 KERSRLRFKSvgfilQASNLIPFLTVQQQLELVdhltgskEKAKANQLFDdlGItglkhqlpqelSGGERQRAAIARALY 156
Cdd:cd03233 80 KYPGEIIYVS-----EEDVHFPTLTVRETLDFA-------LRCKGNEFVR--GI-----------SGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 157 HDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTH--DDRMLKYCDKVYRMQDGE 217
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGR 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-200 |
4.43e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.14 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIID-----------------GTDYTHLSE--------- 76
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprnveGTVYDFVAEgieeqaeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 77 KERSRLRfKSVGFILQASNLIPFLTVQQQLelvDHLTGSKEKAKANQLFDDLGITGlkHQLPQELSGGERQRAAIARALY 156
Cdd:PRK11147 99 KRYHDIS-HLVETDPSEKNLNELAKLQEQL---DHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499604739 157 HDPALILADEPTASLDTekayEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-221 |
5.05e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRF-------KSVGFILQAS------ 94
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLvylpedrQSSGLYLDAPlawnvc 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 ----NLIPFLtvqqqlelvdhLTGSKEKAKANQLFDDLGITgLKH--QLPQELSGGERQRAAIARALYHDPALILADEPT 168
Cdd:PRK15439 364 althNRRGFW-----------IKPARENAVLERYRRALNIK-FNHaeQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 169 ASLDT---EKAYEVVKLLAKEskekNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK15439 432 RGVDVsarNDIYQLIRSIAAQ----NVAVLFISSDlEEIEQMADRVLVMHQGEISGA 484
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-199 |
5.11e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.59 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 7 KQVTKTFQD-GHHEINALKATDFSieaGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYthlsEKERSRLRfK 85
Cdd:TIGR01257 932 KNLVKIFEPsGRPAVDRLNITFYE---NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-Q 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 SVGFILQASNLIPFLTVQQQLELVDHLTG-SKEKAK--ANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALI 162
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGrSWEEAQleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190
....*....|....*....|....*....|....*..
gi 499604739 163 LADEPTASLDTEKAYEVVKLLAKesKEKNKAIIMVTH 199
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLK--YRSGRTIIMSTH 1118
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-200 |
8.78e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.92 E-value: 8.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLqTPSSGQLIIDG-TDYTHLSEKER----SRLRfKSVGFILQASNLI 97
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrVEFFNQNIYERrvnlNRLR-RQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 98 P---FLTVQQQLELVD-----HLTGSKEKA-KANQLFDDLgitglKHQLPQ---ELSGGERQRAAIARALYHDPALILAD 165
Cdd:PRK14258 101 PmsvYDNVAYGVKIVGwrpklEIDDIVESAlKDADLWDEI-----KHKIHKsalDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....*
gi 499604739 166 EPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-206 |
1.94e-15 |
|
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: 74.44 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 31 EAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQL--------IID---GT---DY-THLSEKErsrlrfKSVGFILQASN 95
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGTelqDYfKKLANGE------IKVAHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 96 LIPFL---TVQQQLELVDhltgskEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLD 172
Cdd:COG1245 171 LIPKVfkgTVRELLEKVD------ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|....
gi 499604739 173 TEKAYEVVKLLaKESKEKNKAIIMVTHDDRMLKY 206
Cdd:COG1245 245 IYQRLNVARLI-RELAEEGKYVLVVEHDLAILDY 277
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-208 |
3.02e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHheiNALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIdgtdythLSEKERSR 81
Cdd:PRK15056 5 AGIVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI-------LGQPTRQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 82 LRFKSVGFILQASNL---IPFLtVQQQLEL--VDHLTG-SKEKAKANQLFDD----LGITGLKHQLPQELSGGERQRAAI 151
Cdd:PRK15056 75 LQKNLVAYVPQSEEVdwsFPVL-VEDVVMMgrYGHMGWlRRAKKRDRQIVTAalarVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 152 ARALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHD-DRMLKYCD 208
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLL-RELRDEGKTMLVSTHNlGSVTEFCD 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-217 |
4.18e-15 |
|
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: 72.20 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLiidgtdythlseKERSRLRFKS-VGFILQAS---NLI- 97
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------------KHSGRISFSSqFSWIMPGTikeNIIf 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 98 -------PFLTVQQQLELVDHLTGSKEkaKANQLFDDLGITglkhqlpqeLSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:cd03291 121 gvsydeyRYKSVVKACQLEEDITKFPE--KDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499604739 171 LD--TEKA-YE--VVKLLAkeskekNKAIIMVTHDDRMLKYCDKVYRMQDGE 217
Cdd:cd03291 190 LDvfTEKEiFEscVCKLMA------NKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-216 |
5.14e-15 |
|
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: 73.41 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLiidgtdythlseKERSRLRFKS-VGFILQAS---NLIP 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------KHSGRISFSPqTSWIMPGTikdNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 99 FLT--------VQQQLELVDHLTGSKEKAKAnqLFDDLGITglkhqlpqeLSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:TIGR01271 510 GLSydeyrytsVIKACQLEEDIALFPEKDKT--VLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499604739 171 LD--TEKA-YE--VVKLLAkeskekNKAIIMVTHDDRMLKYCDKVYRMQDG 216
Cdd:TIGR01271 579 LDvvTEKEiFEscLCKLMS------NKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-185 |
5.80e-15 |
|
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: 70.35 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 2 SVLTFKQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPS--SGQLIIDGtdythlSEKER 79
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING------RPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 SRLRfkSVGFILQASNLIPFLTVQQQLELVDHLTGskekakanqlfddlgitglkhqlpqeLSGGERQRAAIARALYHDP 159
Cdd:cd03232 76 NFQR--STGYVEQQDVHSPNLTVREALRFSALLRG--------------------------LSVEQRKRLTIGVELAAKP 127
|
170 180
....*....|....*....|....*.
gi 499604739 160 ALILADEPTASLDTEKAYEVVKLLAK 185
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKK 153
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-218 |
5.83e-15 |
|
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: 72.91 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEIN-ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDythLSEKERSRL 82
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 RfksvgfilqasNLipFLTVQQQLELVDHLTGSKEK---AKANQLFDDLgitGLKHQLP--------QELSGGERQRAAI 151
Cdd:COG4615 405 R-----------QL--FSAVFSDFHLFDRLLGLDGEadpARARELLERL---ELDHKVSvedgrfstTDLSQGQRKRLAL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499604739 152 ARALYHD-PALILaDEPTASLDTE---KAYEvvKLLAkESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGEL 218
Cdd:COG4615 469 LVALLEDrPILVF-DEWAADQDPEfrrVFYT--ELLP-ELKARGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-206 |
6.23e-15 |
|
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: 71.24 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 33 GEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQL--------IIDGTDYTHLsEKERSRLRFKSVGFIL--QASNLIPFLTV 102
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFRGSEL-QNYFTKLLEGDVKVIVkpQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 103 QQQLELvdhLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKL 182
Cdd:cd03236 105 GKVGEL---LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181
|
170 180
....*....|....*....|....
gi 499604739 183 LAKESKEKNkAIIMVTHDDRMLKY 206
Cdd:cd03236 182 IRELAEDDN-YVLVVEHDLAVLDY 204
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
7-216 |
8.93e-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: 70.44 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 7 KQVTKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRFk 85
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 86 SVGFILQASNLIPfLTVQQQLELVDHLTGSKEKA--KANQLFDDLGIT--GLKHQLPQE---LSGGERQRAAIARALYHD 158
Cdd:cd03290 80 SVAYAAQKPWLLN-ATVEENITFGSPFNKQRYKAvtDACSLQPDIDLLpfGDQTEIGERginLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 159 PALILADEPTASLDTEKAYEVVKL-LAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDG 216
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-172 |
1.34e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKST---FLTiagGLQTPSSGQ--LI---IDGTDYthlsekeRSRLRfksVGFILQASNLIP 98
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTtmkMLT---GLLPASEGEawLFgqpVDAGDI-------ATRRR---VGYMSQAFSLYG 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 99 FLTVQQQLEL---VDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLD 172
Cdd:NF033858 353 ELTVRQNLELharLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-216 |
1.49e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfKSVGFILQASNLIPFLT 101
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR---MGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLELVDH-------LTG---------SKEKA--KANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALIL 163
Cdd:PRK11300 97 VIENLLVAQHqqlktglFSGllktpafrrAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499604739 164 ADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRM-LKYCDKVYRMQDG 216
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLvMGISDRIYVVNQG 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-206 |
4.39e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 33 GEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQL--------IID---GT---DY-THLSEKErsrlrfKSVGFILQASNLI 97
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKrfrGTelqNYfKKLYNGE------IKVVHKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 98 PFL---TVQQQLELVDhltgskEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTE 174
Cdd:PRK13409 173 PKVfkgKVRELLKKVD------ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180 190
....*....|....*....|....*....|..
gi 499604739 175 KAYEVVKLLAKESkeKNKAIIMVTHDDRMLKY 206
Cdd:PRK13409 247 QRLNVARLIRELA--EGKYVLVVEHDLAVLDY 276
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-218 |
4.52e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.03 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFL-TI--AGGL--QTPSSGQLIIDGTD-YTHLSEKERSRlrfKSVGFILQASN 95
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrSInrMNDLnpEVTITGSIVYNGHNiYSPRTDTVDLR---KEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 96 LIPFlTVQQQLELVDHLTGSKEKAKANQLFDdlgiTGLK------------HQLPQELSGGERQRAAIARALYHDPALIL 163
Cdd:PRK14239 97 PFPM-SIYENVVYGLRLKGIKDKQVLDEAVE----KSLKgasiwdevkdrlHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 164 ADEPTASLDTEKAYEVVKLLAkeSKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLL--GLKDDYTMLLVTRSmQQASRISDRTGFFLDGDL 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-220 |
6.85e-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: 70.36 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 12 TFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGtdythlsekersrlrfkSVGFIL 91
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------------SVAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 92 QASnLIPFLTVQQQLELVDHLTGSKEKA--KANQLFDDLGI--TGLKHQLPQE---LSGGERQRAAIARALYHDPALILA 164
Cdd:TIGR00957 706 QQA-WIQNDSLRENILFGKALNEKYYQQvlEACALLPDLEIlpSGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 165 DEPTASLDTEKAYEVV-KLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-174 |
1.09e-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: 69.19 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDgHHEINALkatDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTdyTHLSEKERSRl 82
Cdd:TIGR03719 322 VIEAENLTKAFGD-KLLIDDL---SFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET--VKLAYVDQSR- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfksvgfilqaSNLIPFLTVQQQL-ELVDHLTGSKEKAKANQLFDDLGITGLKHQ-LPQELSGGERQRAAIARALYHDPA 160
Cdd:TIGR03719 395 -----------DALDPNKTVWEEIsGGLDIIKLGKREIPSRAYVGRFNFKGSDQQkKVGQLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|....
gi 499604739 161 LILADEPTASLDTE 174
Cdd:TIGR03719 464 VLLLDEPTNDLDVE 477
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-201 |
1.40e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRfksvgFILQASNLIPFLTVQQQL 106
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL-----YLGHQPGIKTELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ELVDHLTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAkE 186
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLA-Q 174
|
170
....*....|....*
gi 499604739 187 SKEKNKAIIMVTHDD 201
Cdd:PRK13538 175 HAEQGGMVILTTHQD 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-200 |
1.41e-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: 68.81 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHeinALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDgTDYThlsekersrl 82
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfksVGFILQASNLIPFLTVQQQLE-----LVDHLTG------------------SKEKAKANQLFDDLGITGLKHQLPQ 139
Cdd:TIGR03719 70 ----VGYLPQEPQLDPTKTVRENVEegvaeIKDALDRfneisakyaepdadfdklAAEQAELQEIIDAADAWDLDSQLEI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 140 ---------------ELSGGERQRAAIARALYHDPALILADEPTASLDTEKayevVKLLAKESKEKNKAIIMVTHD 200
Cdd:TIGR03719 146 amdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-218 |
2.05e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFSIEAgeFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGT--DYthlSEKERSRLRfKSVGFILQASNLIPFLT-VQ 103
Cdd:PRK13638 23 DFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDY---SKRGLLALR-QQVATVFQDPEQQIFYTdID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 104 QQLELVDHLTGSKEKAKANQLFDDLGIT---GLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVV 180
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEITRRVDEALTLVdaqHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 499604739 181 KLLAKESKEKNKAIIMvTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK13638 177 AIIRRIVAQGNHVIIS-SHDiDLIYEISDAVYVLRQGQI 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-198 |
2.68e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAG---GLQTPSSGQLIIDGtdytHLSEKERSRLRFKSVgFILQASNLIP 98
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASntdGFHIGVEGVITYDG----ITPEEIKKHYRGDVV-YNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 99 FLTVQQQLELVDHL-------TGSKEKAKANQLFD-DLGITGLKH--------QLPQELSGGERQRAAIARALYHDPALI 162
Cdd:TIGR00956 152 HLTVGETLDFAARCktpqnrpDGVSREEYAKHIADvYMATYGLSHtrntkvgnDFVRGVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190
....*....|....*....|....*....|....*.
gi 499604739 163 LADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVT 198
Cdd:TIGR00956 232 CWDNATRGLDSATALEFIRAL-KTSANILDTTPLVA 266
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-200 |
4.88e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQ--TPS---SGQLIIDGTDyTHLSEKERSRLRfKSVGFILQASNL 96
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlIPGfrvEGKVTFHGKN-LYAPDVDPVEVR-RRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 97 IP------------FLTVQQQL-ELVDhlTGSKEKAKANQLFDDLGITGLkhqlpqELSGGERQRAAIARALYHDPALIL 163
Cdd:PRK14243 103 FPksiydniaygarINGYKGDMdELVE--RSLRQAALWDEVKDKLKQSGL------SLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 499604739 164 ADEPTASLDTEKAYEVVKLLaKESKEKnKAIIMVTHD 200
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELM-HELKEQ-YTIIIVTHN 209
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-206 |
7.81e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.58 E-value: 7.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTF-LTIAGGLQ-TPSSGQLIIDGTDYTHLSEKERSR----LRFK--------SVG 88
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDyEVTGGTVEFKGKDLLELSPEDRAGegifMAFQypveipgvSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 89 FILQAS-NLIPFLTVQQQLELVDHLTGSKEKAKANQLFDDLgitgLKHQLPQELSGGERQRAAIARALYHDPALILADEP 167
Cdd:PRK09580 97 FFLQTAlNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDL----LTRSVNVGFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 499604739 168 TASLDTEkAYEVVKLLAKESKEKNKAIIMVTHDDRMLKY 206
Cdd:PRK09580 173 DSGLDID-ALKIVADGVNSLRDGKRSFIIVTHYQRILDY 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-217 |
8.64e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 20 INALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfKSVGFILQASNLIPF 99
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 100 LTVQQQLEL---------VDHltgSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:PRK10982 88 RSVMDNMWLgryptkgmfVDQ---DKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499604739 171 LdTEKAYEVVKLLAKESKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGE 217
Cdd:PRK10982 165 L-TEKEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-221 |
9.00e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 15 DGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIA-GGLQTPSSGQLIIDGTdythlsekersrlrfksVGFILQA 93
Cdd:PLN03130 625 DSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMlGELPPRSDASVVIRGT-----------------VAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 94 SnLIPFLTVQQQLelvdhLTGSK-EKAKANQLFDdlgITGLKHQLPQ--------------ELSGGERQRAAIARALYHD 158
Cdd:PLN03130 688 S-WIFNATVRDNI-----LFGSPfDPERYERAID---VTALQHDLDLlpggdlteigergvNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499604739 159 PALILADEPTASLDTEKAYEVVKLLAKEsKEKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVFDKCIKD-ELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-221 |
1.55e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRlrfKSVGFILQA---SNLIPFLTVQQ 104
Cdd:PRK09700 284 FSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVK---KGMAYITESrrdNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 105 QLELVDHL------------TGSKEKAKANQLFDDLGITGlkHQLPQ---ELSGGERQRAAIARALYHDPALILADEPTA 169
Cdd:PRK09700 361 NMAISRSLkdggykgamglfHEVDEQRTAENQRELLALKC--HSVNQnitELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499604739 170 SLDTEKAYEVVKLLAKESkEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLA-DDGKVILMVSSElPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-221 |
3.75e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.96 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSG-----QLIIDGTDYTHLSEKERSRLRfksVGFILQASNLI 97
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRR---VGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 98 PFLTVQQQLELV--DHLTGSKE-KAKANQLFDDLGI-TGLKHQL---PQELSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:PRK14271 114 PMSIMDNVLAGVraHKLVPRKEfRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 171 LD---TEKAYEVVKLLAKEskeknKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK14271 194 LDpttTEKIEEFIRSLADR-----LTVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-208 |
9.62e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 17 HHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYthlsEKERSRLRfKSVGFILQASNL 96
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 97 IPFLTVQQQLELVDHL-TGSKEKAKANQLFDdlgitgLKHQLPQE---LSGGERQRAAIARALYHDPALILADEPTASLD 172
Cdd:PRK13540 86 NPYLTLRENCLYDIHFsPGAVGITELCRLFS------LEHLIDYPcglLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 499604739 173 tEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCD 208
Cdd:PRK13540 160 -ELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-208 |
9.93e-12 |
|
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: 61.18 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 21 NALKATDFSIEAGEFVAIIGPSGSGKSTFLTiaGGLQTPSSGQLIIDGTDYTHlsekersrlrfKSVGFILQASNLIpfl 100
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFLPKFSR-----------NKLIFIDQLQFLI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 tvqqqlelvdhltgskekakanqlfdDLGITGLK-HQLPQELSGGERQRAAIARALYHDP--ALILADEPTASLDTEKAY 177
Cdd:cd03238 73 --------------------------DVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|.
gi 499604739 178 EVVKLLaKESKEKNKAIIMVTHDDRMLKYCD 208
Cdd:cd03238 127 QLLEVI-KGLIDLGNTVILIEHNLDVLSSAD 156
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-204 |
1.03e-11 |
|
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: 60.46 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 33 GEFVAIIGPSGSGKSTFL-TIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRFKSVGFilqasnlipfltvqqqlelvdh 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLArALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 112 ltgskekakanqlfddlgitglkhqlpqELSGGERQRAAIARALYHDPALILADEPTASLDTE-----KAYEVVKLLAKE 186
Cdd:smart00382 60 ----------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLLLL 111
|
170
....*....|....*...
gi 499604739 187 SKEKNKAIIMVTHDDRML 204
Cdd:smart00382 112 KSEKNLTVILTTNDEKDL 129
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-217 |
1.82e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVtKTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGT-------------- 69
Cdd:PTZ00265 383 IQFKNV-RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrsk 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 70 ------DYTHLSEKERSRLRF-----KSVGFILQASNLIPFLTVQQQ-------------LELVDHLTGSKE--KAKAN- 122
Cdd:PTZ00265 462 igvvsqDPLLFSNSIKNNIKYslyslKDLEALSNYYNEDGNDSQENKnkrnscrakcagdLNDMSNTTDSNEliEMRKNy 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 123 QLFDDLGITGLKHQ---------LP-----------QELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKL 182
Cdd:PTZ00265 542 QTIKDSEVVDVSKKvlihdfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270
....*....|....*....|....*....|....*
gi 499604739 183 LAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGE 217
Cdd:PTZ00265 622 INNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-218 |
2.05e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 17 HHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLQTPS-------SGQLIIDGTDYTHLSEKERSRLRfksvG 88
Cdd:PRK13547 13 HRAI--LRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLR----A 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 89 FILQASN-LIPFlTVQQQLEL--VDHLTGSKEKAK-----ANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYH--- 157
Cdd:PRK13547 87 VLPQAAQpAFAF-SAREIVLLgrYPHARRAGALTHrdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 158 ------DPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRM-LKYCDKVYRMQDGEL 218
Cdd:PRK13547 166 phdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRIAMLADGAI 233
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-217 |
5.80e-11 |
|
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: 59.12 E-value: 5.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 5 TFKQVTKTFQDGHHEInalKATDFSieAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQliidgtdythlSEKERSRLRF 84
Cdd:cd03222 2 LYPDCVKRYGVFFLLV---ELGVVK--EGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-----------DEWDGITPVY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 85 KsvgfilqasnlipfltvqqqlelvdhltgskekakanqlfddlgitglkhqlPQ--ELSGGERQRAAIARALYHDPALI 162
Cdd:cd03222 66 K----------------------------------------------------PQyiDLSGGELQRVAIAAALLRNATFY 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 163 LADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDGE 217
Cdd:cd03222 94 LFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-200 |
1.49e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 38 IIGPSGSGKSTFLTIAGGLQTPSSGQLIIDgTDYThlsekersrlrfksVGFILQASNLIPFLTVQQQLELvdhltGSKE 117
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK--------------VGYLPQEPQLDPEKTVRENVEE-----GVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 118 KAKA----NQL----------FDDL--------------GITGLKHQLPQ---------------ELSGGERQRAAIARA 154
Cdd:PRK11819 98 VKAAldrfNEIyaayaepdadFDALaaeqgelqeiidaaDAWDLDSQLEIamdalrcppwdakvtKLSGGERRRVALCRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499604739 155 LYHDPALILADEPTASLDTEKayevVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAES----VAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
11-220 |
1.56e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.11 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 11 KTFQDGHHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKE-RSRLrfksvgf 89
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRL------- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 90 ilQASNLIPFL---TV------------QQQLElvdhltgskEKAKANQLFDDLgitglkHQLPQ-----------ELSG 143
Cdd:PRK10789 392 --AVVSQTPFLfsdTVannialgrpdatQQEIE---------HVARLASVHDDI------LRLPQgydtevgergvMLSG 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499604739 144 GERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEknKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:PRK10789 455 GQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-210 |
1.70e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 24 KATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKER------------------------ 79
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQdyqgdeeqnvgmknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 ----SRLRFKSVGFIL------------QASNLipFLTVQQQ-----LELVDHLTGSKEKAKANQL--------FDDLgI 130
Cdd:PTZ00265 1265 gsgeDSTVFKNSGKILldgvdicdynlkDLRNL--FSIVSQEpmlfnMSIYENIKFGKEDATREDVkrackfaaIDEF-I 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 131 TGLKHQLP-------QELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRM 203
Cdd:PTZ00265 1342 ESLPNKYDtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIAS 1421
|
....*..
gi 499604739 204 LKYCDKV 210
Cdd:PTZ00265 1422 IKRSDKI 1428
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-219 |
2.76e-10 |
|
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: 59.07 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 17 HHEINA-LKATD---FSIEAGEFVAIIGPSGSGKSTFLT-IAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRFKSVGFIL 91
Cdd:TIGR02633 266 WDVINPhRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 92 QASNLIPFLTVQQQLEL--VDHLTG-SKEKAKANQLFDDLGITGLKHQ-----LP-QELSGGERQRAAIARALYHDPALI 162
Cdd:TIGR02633 346 KRHGIVPILGVGKNITLsvLKSFCFkMRIDAAAELQIIGSAIQRLKVKtaspfLPiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 163 LADEPTASLDTEKAYEVVKLLAKESKEkNKAIIMVTHD-DRMLKYCDKVYRMQDGELC 219
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSElAEVLGLSDRVLVIGEGKLK 482
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-199 |
7.30e-10 |
|
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: 58.49 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 30 IEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTD-YTHLSEKErsrlrfKSVGFILQASNLIPFLTVQQQLEL 108
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVH------QNMGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 109 VDHLTG--SKEKAK-ANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAK 185
Cdd:TIGR01257 2036 YARLRGvpAEEIEKvANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170
....*....|....
gi 499604739 186 ESKEkNKAIIMVTH 199
Cdd:TIGR01257 2116 IIRE-GRAVVLTSH 2128
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-221 |
9.26e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGtdythlsekerSRLRFKSV------GFIL-----QASNL 96
Cdd:PRK11288 274 FSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-----------KPIDIRSPrdairaGIMLcpedrKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 97 IPFLTVQQQLELV---DHLT------GSKEKAKANQLFDDLGI-TGLKHQLPQELSGGERQRAAIARALYHDPALILADE 166
Cdd:PRK11288 343 IPVHSVADNINISarrHHLRagclinNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 167 PTASLDT-EKA--YEVVKLLAkeskEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK11288 423 PTRGIDVgAKHeiYNVIYELA----AQGVAVLFVSSDlPEVLGVADRIVVMREGRIAGE 477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-221 |
1.44e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLT-IAGGLQTPSSGQLIIDGtdythlsekersrlrfkSVGFILQASnLIPFLT 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-----------------SVAYVPQVS-WIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLelvdhLTGSK-EKAKANQLFDdlgITGLKHQLPQ--------------ELSGGERQRAAIARALYHDPALILADE 166
Cdd:PLN03232 695 VRENI-----LFGSDfESERYWRAID---VTALQHDLDLlpgrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 167 PTASLDTEKAYEVVKLLAKESKeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQE 221
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDEL-KGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-206 |
1.46e-09 |
|
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: 57.07 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDgtdythlsekERSRLrFksvgFILQAsnliPFLTV---QQ 104
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----------AKGKL-F----YVPQR----PYMTLgtlRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 105 QLELVDHLTGSKEKAKANQ-LFDDLGITGLKHQLPQE------------LSGGERQRAAIARALYHDPALILADEPTA-- 169
Cdd:TIGR00954 534 QIIYPDSSEDMKRRGLSDKdLEQILDNVQLTHILEREggwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSav 613
|
170 180 190
....*....|....*....|....*....|....*..
gi 499604739 170 SLDTEKAyevvklLAKESKEKNKAIIMVTHDDRMLKY 206
Cdd:TIGR00954 614 SVDVEGY------MYRLCREFGITLFSVSHRKSLWKY 644
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
23-176 |
3.62e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.88 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEkerSRLRfKSVGFILQ-----ASNLI 97
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLR-QGVAMVQQdpvvlADTFL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 98 PFLT---------VQQQLELVDhlTGSKEKAKANQLFDDLGITGlkhqlpQELSGGERQRAAIARALYHDPALILADEPT 168
Cdd:PRK10790 433 ANVTlgrdiseeqVWQALETVQ--LAELARSLPDGLYTPLGEQG------NNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170
....*....|
gi 499604739 169 ASLD--TEKA 176
Cdd:PRK10790 505 ANIDsgTEQA 514
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
13-213 |
4.00e-09 |
|
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: 53.90 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 13 FQDGHHEINAlKATDFSIEAGEFVAIIGPSGSGKSTFLtiagglqtpssgqliidgtdythlsekersrlrfKSVGFILq 92
Cdd:cd03227 2 IVLGRFPSYF-VPNDVTFGEGSLTIITGPNGSGKSTIL----------------------------------DAIGLAL- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 93 asnlipflTVQQQLELVdhltGSKEKAKANQLFDDLGITGLKHQLpqelSGGERQRAAIARALYH---DPA-LILADEPT 168
Cdd:cd03227 46 --------GGAQSATRR----RSGVKAGCIVAAVSAELIFTRLQL----SGGEKELSALALILALaslKPRpLYILDEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499604739 169 ASLDTEKAYEVVKLLAKESKEKNKAIImVTHDDRMLKYCDKVYRM 213
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAELADKLIHI 153
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-168 |
4.86e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLT-IAGG--LQTpssGQLIIDGTDYThlSEKERSRLRFKsVGFILQ--ASNL 96
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSlIAGArkIQQ---GRVEVLGGDMA--DARHRRAVCPR-IAYMPQglGKNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 97 IPFLTVQQQLE----LVDHltGSKE-KAKANQLfddLGITGLkhqLP------QELSGGERQRAAIARALYHDPALILAD 165
Cdd:NF033858 90 YPTLSVFENLDffgrLFGQ--DAAErRRRIDEL---LRATGL---APfadrpaGKLSGGMKQKLGLCCALIHDPDLLILD 161
|
...
gi 499604739 166 EPT 168
Cdd:NF033858 162 EPT 164
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-204 |
5.98e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 24 KATDFSIEAGEFVAIIGPSGSGKSTFLT-IAGGLQtPSSG--------------QLIIDGTDYthlsekersrlrfkSVG 88
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKlISGELQ-PSSGtvfrsakvrmavfsQHHVDGLDL--------------SSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 89 FILQASNLIPFLTVQQqleLVDHLtGSkekakanqlfddLGITG-LKHQLPQELSGGERQRAAIARALYHDPALILADEP 167
Cdd:PLN03073 591 PLLYMMRCFPGVPEQK---LRAHL-GS------------FGVTGnLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
170 180 190
....*....|....*....|....*....|....*..
gi 499604739 168 TASLDTEKAYEVVKLLAKeskeKNKAIIMVTHDDRML 204
Cdd:PLN03073 655 SNHLDLDAVEALIQGLVL----FQGGVLMVSHDEHLI 687
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-190 |
9.26e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 1 MSVLTFKQvtKTFQdgHHEINALKATDFSIEAGEFVAIIGPSGSGKSTF-LTIAGGLqTPSSGQLIIDGTDYTHLS-EKE 78
Cdd:PRK10938 1 MSSLQISQ--GTFR--LSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALaRALAGEL-PLLSGERQSQFSHITRLSfEQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 79 RsrlrfKSVGFILQASN---LIPF-----LTVQQQLELvdhltGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAA 150
Cdd:PRK10938 76 Q-----KLVSDEWQRNNtdmLSPGeddtgRTTAEIIQD-----EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499604739 151 IARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEK 190
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG 185
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-212 |
1.14e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.99 E-value: 1.14e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 141 LSGGERQ------RAAIARALYHDPALILADEPTASLDTEKAYEV-VKLLAKESKEKNKAIIMVTHDDRMLKYCDKVYR 212
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESlAEIIEERKSQKNFQLIVITHDEELVDAADHIYR 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-174 |
1.91e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKErsrLRFKsVGFILQAS-------- 94
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD---LRFK-ITIIPQDPvlfsgslr 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 -NLIPFLTVQQQ-----LELVdHLTGskekakanqlFDDLGITGLKHQLPQ---ELSGGERQRAAIARALYHDPALILAD 165
Cdd:TIGR00957 1378 mNLDPFSQYSDEevwwaLELA-HLKT----------FVSALPDKLDHECAEggeNLSVGQRQLVCLARALLRKTKILVLD 1446
|
....*....
gi 499604739 166 EPTASLDTE 174
Cdd:TIGR00957 1447 EATAAVDLE 1455
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-218 |
2.48e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKS-TFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLRFKSVGFILQASNLIPFLTVQQQL 106
Cdd:PRK13549 283 FSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDGIVPVMGVGKNI 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 107 ELV--------DHLTGSKEKAKANQLFDDLGITGLKHQLP-QELSGGERQRAAIARALYHDPALILADEPTASLDTEKAY 177
Cdd:PRK13549 363 TLAaldrftggSRIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKY 442
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499604739 178 EVVKLLAKESKEkNKAIIMVTHD-DRMLKYCDKVYRMQDGEL 218
Cdd:PRK13549 443 EIYKLINQLVQQ-GVAIIVISSElPEVLGLSDRVLVMHEGKL 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-174 |
2.90e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDghheiNAL-KATDFSIEAGEFVAIIGPSGSGKST-FLTIAgGLQTPSSGQLIIDGTdyTHLSEKERS 80
Cdd:PRK11819 324 VIEAENLSKSFGD-----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTlFKMIT-GQEQPDSGTIKIGET--VKLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 81 RlrfksvgfilqaSNLIPFLTVQQQL-ELVDHLT-GSKE-KAKANqlfddLGITGLKHQLPQ----ELSGGERQRAAIAR 153
Cdd:PRK11819 396 R------------DALDPNKTVWEEIsGGLDIIKvGNREiPSRAY-----VGRFNFKGGDQQkkvgVLSGGERNRLHLAK 458
|
170 180
....*....|....*....|.
gi 499604739 154 ALYHDPALILADEPTASLDTE 174
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVE 479
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-207 |
3.39e-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: 53.38 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTpSSGQLIIDGTDYTHLS-EKERsrl 82
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTlQTWR--- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfKSVGFILQAsnlIPFLTVQQQLELVDHLTGSKEKAKanQLFDDLGITGLKHQLPQE-----------LSGGERQRAAI 151
Cdd:TIGR01271 1292 --KAFGVIPQK---VFIFSGTFRKNLDPYEQWSDEEIW--KVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCL 1364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499604739 152 ARALYHDPALILADEPTASLDTeKAYEVVKLLAKESKeKNKAIIMVTHDDRMLKYC 207
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSF-SNCTVILSEHRVEALLEC 1418
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-209 |
5.63e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGtdythlsekersrlrfkSVGFILQASNLIPFLT 101
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------------SAALIAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLELVDHLTG-SKEKAK--ANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLD---TEK 175
Cdd:PRK13545 102 GIENIELKGLMMGlTKEKIKeiIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqtfTKK 181
|
170 180 190
....*....|....*....|....*....|....*
gi 499604739 176 AYEVVkllaKESKEKNKAIIMVTHDDRMLK-YCDK 209
Cdd:PRK13545 182 CLDKM----NEFKEQGKTIFFISHSLSQVKsFCTK 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-216 |
1.27e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTD-------------YTHLSEKERSR--LRFKSVGFILQ 92
Cdd:PRK10982 269 FDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKinnhnaneainhgFALVTEERRSTgiYAYLDIGFNSL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 93 ASNLIPFLTvqqQLELvdhLTGSKEKAKANQLFDDLGITGLKHQLP-QELSGGERQRAAIARALYHDPALILADEPTASL 171
Cdd:PRK10982 349 ISNIRNYKN---KVGL---LDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499604739 172 DTEKAYEVVKLLAKESKeKNKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:PRK10982 423 DVGAKFEIYQLIAELAK-KDKGIIIISSEmPELLGITDRILVMSNG 467
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-199 |
1.46e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 33 GEFVAIIGPSGSGKSTFLTIAGGLQTpssGQLIIDGTDYTHLSEKERSRLRfkSVGFILQASNLIPFLTVQQQLELVDHL 112
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVNGRPLDSSFQR--SIGYVQQQDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 113 TGSKEKAKA------NQLFDDLGITGLKHQL---PQE-LSGGERQRAAIARALYHDPALIL-ADEPTASLDTEKAYEVVK 181
Cdd:TIGR00956 864 RQPKSVSKSekmeyvEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170
....*....|....*...
gi 499604739 182 LLAKESKEkNKAIIMVTH 199
Cdd:TIGR00956 944 LMRKLADH-GQAILCTIH 960
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-210 |
1.48e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 1.48e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 141 LSGGERQRAAIARALYHDPALI--LADEPTASL---DTEKAYEVVKLLakesKEKNKAIIMVTHDDRMLKYCDKV 210
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLhpqDTHKLINVIKKL----RDQGNTVLLVEHDEQMISLADRI 547
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-220 |
1.55e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.62 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTpSSGQLIIDGTDYTHLSEKERSrlr 83
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fKSVGFILQASnLIPFLTVQQQLElvdhLTGSKEKAKANQLFDDLGITGLKHQLPQE-----------LSGGERQRAAIA 152
Cdd:cd03289 77 -KAFGVIPQKV-FIFSGTFRKNLD----PYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 153 RALYHDPALILADEPTASLDTeKAYEVVKLLAKESKeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAF-ADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-174 |
2.84e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGhheiNALKATDFSIEAGEFVAIIGPSGSGKSTFL-TIAGGLQtPSSGQLiidgtdytHLSEKersrl 82
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLrTLVGELE-PDSGTV--------KWSEN----- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 rfKSVGFILQasnlipfltvqqqlelvDHltgSKEKAKANQLF-----------DDLGITGLKHQL----------PQEL 141
Cdd:PRK15064 382 --ANIGYYAQ-----------------DH---AYDFENDLTLFdwmsqwrqegdDEQAVRGTLGRLlfsqddikksVKVL 439
|
170 180 190
....*....|....*....|....*....|...
gi 499604739 142 SGGERQRAAIARALYHDPALILADEPTASLDTE 174
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-218 |
3.27e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKErsrLRfKSVGFILQAS-------- 94
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LR-KVLGIIPQAPvlfsgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 -NLIPF-----LTVQQQLELVdHLtgsKEKAKANQLfddlgitGLKHQLPQ---ELSGGERQRAAIARALYHDPALILAD 165
Cdd:PLN03130 1331 fNLDPFnehndADLWESLERA-HL---KDVIRRNSL-------GLDAEVSEageNFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 166 EPTASLDTEKAyevvKLLAKESKEKNKAIIM--VTHDDRMLKYCDKVYRMQDGEL 218
Cdd:PLN03130 1400 EATAAVDVRTD----ALIQKTIREEFKSCTMliIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-200 |
4.69e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 39 IGPSGSGKSTFLTIAGGLQTPSSGQLIID-----GT---------DYTHLS------------EKERSRLRfksvgfilq 92
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKlrqdqfafeEFTVLDtvimghtelwevKQERDRIY--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 93 aSNliPFLTVQQQLELVD------HLTGSKEKAKANQLFDDLGITGLKHQLP-QELSGGERQRAAIARALYHDPALILAD 165
Cdd:PRK15064 104 -AL--PEMSEEDGMKVADlevkfaEMDGYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLD 180
|
170 180 190
....*....|....*....|....*....|....*
gi 499604739 166 EPTASLDTekayEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK15064 181 EPTNNLDI----NTIRWLEDVLNERNSTMIIISHD 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-199 |
6.70e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFqdghHEINALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQtPS---SGQLIIDGT--DYTHLSEK 77
Cdd:NF040905 1 ILEMRGITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcRFKDIRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 78 ERsrlrfKSVGFILQASNLIPFLTVQQQLELvdhltgSKEKAK------------ANQLFDDLGITGLKHQLPQELSGGE 145
Cdd:NF040905 76 EA-----LGIVIIHQELALIPYLSIAENIFL------GNERAKrgvidwnetnrrARELLAKVGLDESPDTLVTDIGVGK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499604739 146 RQRAAIARALYHDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTH 199
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLL-LELKAQGITSIIISH 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-172 |
1.05e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGG--LQTPS-----------SGQLIID-----G--TDYTHLSEKERSRL 82
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhPQGYSndltlfgrrrgSGETIWDikkhiGyvSSSLHLDYRVSTSV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 83 R-------FKSVGFILQASNlipfltVQQQLelvdhltgskekakANQLFDDLGITGLKHQLP-QELSGGERQRAAIARA 154
Cdd:PRK10938 356 RnvilsgfFDSIGIYQAVSD------RQQKL--------------AQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRA 415
|
170
....*....|....*...
gi 499604739 155 LYHDPALILADEPTASLD 172
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLD 433
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-220 |
1.52e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLrfksVGFILQAS-------- 94
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPvlfsgtvr 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 -NLIPFlTVQQQLELVDHLtgskEKAKANQLFDD--LGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASL 171
Cdd:PLN03232 1328 fNIDPF-SEHNDADLWEAL----ERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499604739 172 DTekayEVVKLLAKESKEKNKAIIM--VTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:PLN03232 1403 DV----RTDSLIQRTIREEFKSCTMlvIAHRLNTIIDCDKILVLSSGQVLE 1449
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-216 |
1.81e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIidgtdythlseKERSRLRFKSVGFILQA---SNlIPF 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-----------AERSIAYVPQQAWIMNAtvrGN-ILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 100 LTVQQQLELVDHLTGSKEKAKANQLfddlgITGLKHQLPQE---LSGGERQRAAIARALYHDPALILADEPTASLDT--- 173
Cdd:PTZ00243 744 FDEEDAARLADAVRVSQLEADLAQL-----GGGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhvg 818
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499604739 174 EKAYEVVKLLAKESKEKnkaiIMVTHDDRMLKYCDKVYRMQDG 216
Cdd:PTZ00243 819 ERVVEECFLGALAGKTR----VLATHQVHVVPRADYVVALGDG 857
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
23-220 |
1.83e-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: 47.21 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 23 LKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLS-EKERSRLrfksvGFILQAsnliPFL- 100
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSRL-----SIILQD----PILf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 101 --TVQQQLElvdhltgSKEKAKANQLFDDLGITGLKH---QLP-----------QELSGGERQRAAIARALYHDPALILA 164
Cdd:cd03288 108 sgSIRFNLD-------PECKCTDDRLWEALEIAQLKNmvkSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 165 DEPTASLD--TEKAYEVVKLLAKeskeKNKAIIMVTHDDRMLKYCDKVYRMQDGELCQ 220
Cdd:cd03288 181 DEATASIDmaTENILQKVVMTAF----ADRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
102-199 |
1.99e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLELVDHLTGskeKAKANQLFDDLGITG-LKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVV 180
Cdd:PLN03073 308 IYKRLELIDAYTA---EARAASILAGLSFTPeMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLE 384
|
90
....*....|....*....
gi 499604739 181 KLLAKESkeknKAIIMVTH 199
Cdd:PLN03073 385 TYLLKWP----KTFIVVSH 399
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-221 |
2.43e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 28 FSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKER--------SRLRfKSVGFILQASnlipf 99
Cdd:PRK10762 273 FTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivyiSEDR-KRDGLVLGMS----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 100 ltVQQQLEL--VDHLT---GSKEKAKANQLFDD----LGI-TGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTA 169
Cdd:PRK10762 347 --VKENMSLtaLRYFSragGSLKHADEQQAVSDfirlFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499604739 170 SLDTEKAYEVVKLLAKeSKEKNKAIIMVTHD-DRMLKYCDKVYRMQDGELCQE 221
Cdd:PRK10762 425 GVDVGAKKEIYQLINQ-FKAEGLSIILVSSEmPEVLGMSDRILVMHEGRISGE 476
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-172 |
2.62e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 4 LTFKQVTKTFQDGHHEInaLKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGTDYTHLSEKERSRLr 83
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ- 1385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 84 fksVGFILQ---------ASNLIPFLT-----VQQQLELVdhltGSKEKAKAnqlfDDLGITGLKHQLPQELSGGERQRA 149
Cdd:PTZ00243 1386 ---FSMIPQdpvlfdgtvRQNVDPFLEassaeVWAALELV----GLRERVAS----ESEGIDSRVLEGGSNYSVGQRQLM 1454
|
170 180
....*....|....*....|....
gi 499604739 150 AIARALY-HDPALILADEPTASLD 172
Cdd:PTZ00243 1455 CMARALLkKGSGFILMDEATANID 1478
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-210 |
2.83e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.48 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 20 INALKATDFSIEAGEFVAIIGPSGSGKST--FLTIAgglqtpSSGQLiidgtDY-THLSEKERSRLRFKSVGFILQASNL 96
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSlaFDTIY------AEGQR-----RYvESLSAYARQFLGQMDKPDVDSIEGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 97 IPFLTVQQQL-------------ELVDHLtgskekakaNQLFDDLGIT---------GLKHQLP----QELSGGERQRAA 150
Cdd:cd03270 77 SPAIAIDQKTtsrnprstvgtvtEIYDYL---------RLLFARVGIRerlgflvdvGLGYLTLsrsaPTLSGGEAQRIR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 151 IARALYH--DPALILADEPTASL---DTEKAYEVVKLLakesKEKNKAIIMVTHDDRMLKYCDKV 210
Cdd:cd03270 148 LATQIGSglTGVLYVLDEPSIGLhprDNDRLIETLKRL----RDLGNTVLVVEHDEDTIRAADHV 208
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-200 |
3.44e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 29 SIEAGEFVAIIGPSGSGKSTFLTI--------AGGLQTPSSGQLI----------IDGTDYTHLSEKERSRLRFKsvgfi 90
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALlkneisadGGSYTFPGNWQLAwvnqetpalpQPALEYVIDGDREYRQLEAQ----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 91 LQASNLI----PFLTVQQQLELVDHLTgskEKAKANQLFDDLGITGLKHQLP-QELSGGERQRAAIARALYHDPALILAD 165
Cdd:PRK10636 98 LHDANERndghAIATIHGKLDAIDAWT---IRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190
....*....|....*....|....*....|....*
gi 499604739 166 EPTASLDtekaYEVVKLLAKESKEKNKAIIMVTHD 200
Cdd:PRK10636 175 EPTNHLD----LDAVIWLEKWLKSYQGTLILISHD 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-218 |
5.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 33 GEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLiidgtdytHLSEKERsrlrfksVGFIlqasnlipfltVQQQLEL---- 108
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI--------GLAKGIK-------LGYF-----------AQHQLEFlrad 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 109 ---VDHLTGSKEKAKANQLFDDLGITGLK----HQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEVVK 181
Cdd:PRK10636 392 espLQHLARLAPQELEQKLRDYLGGFGFQgdkvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE 471
|
170 180 190
....*....|....*....|....*....|....*...
gi 499604739 182 LLAkeskEKNKAIIMVTHDDRMLK-YCDKVYRMQDGEL 218
Cdd:PRK10636 472 ALI----DFEGALVVVSHDRHLLRsTTDDLYLVHDGKV 505
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-218 |
5.59e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 22 ALKATDFSIEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDGtdythlsekersrlrfkSVGFILQASNLIPFLT 101
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------------EVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 102 VQQQLELVDHLTGSKEKaKANQL------FDDLGitGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEK 175
Cdd:PRK13546 102 GIENIEFKMLCMGFKRK-EIKAMtpkiieFSELG--EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499604739 176 AYevvKLLAK--ESKEKNKAIIMVTHDDRMLK-YCDKVYRMQDGEL 218
Cdd:PRK13546 179 AQ---KCLDKiyEFKEQNKTIFFVSHNLGQVRqFCTKIAWIEGGKL 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-181 |
6.64e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 33 GEFVAIIGPSGSGKSTFLTIAGGLQTPS--SGQLIIDGtdythLSEKERSRLRFKsvGFILQASNLIPFLTVQQQLELVD 110
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG-----FPKKQETFARIS--GYCEQNDIHSPQVTVRESLIYSA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 111 HLTGSKEKAKANQL-----------FDDL--------GITGLkhqlpqelSGGERQRAAIARALYHDPALILADEPTASL 171
Cdd:PLN03140 979 FLRLPKEVSKEEKMmfvdevmelveLDNLkdaivglpGVTGL--------STEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170
....*....|
gi 499604739 172 DTEKAYEVVK 181
Cdd:PLN03140 1051 DARAAAIVMR 1060
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
141-221 |
1.15e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 141 LSGGERQRAAIARALYHDPALILADEPTASLDTEKAYE---VVKLLAKESkeknKAIIMVTHD-DRMLKYCDKVYRMQDG 216
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEiytIINELAAEG----KGVIVISSElPELLGMCDRIYVMNEG 480
|
....*
gi 499604739 217 ELCQE 221
Cdd:NF040905 481 RITGE 485
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-212 |
1.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 138 PQELSGGERQ------RAAIARALYHD-------PALILaDEPTASLDTEKAYEVVKLLAKESKEKNKAIIMVTHDDRML 204
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDELV 857
|
....*...
gi 499604739 205 KYCDKVYR 212
Cdd:PRK02224 858 GAADDLVR 865
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
112-179 |
2.31e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 2.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499604739 112 LTGSKEKAKANQLFDDLGITGLKHQLPQELSGGERQRAAIARALYHDPALILADEPTASLDTEKAYEV 179
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
127-211 |
2.42e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 127 DLGITGLKHQLPQ---ELSGGERQ------RAAIARALYHDPALILADEPTASLDTEKAYEVVKLLAKESKEKN--KAII 195
Cdd:PRK01156 785 DFNITVSRGGMVEgidSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdiPQVI 864
|
90
....*....|....*.
gi 499604739 196 MVTHDDRMLKYCDKVY 211
Cdd:PRK01156 865 MISHHRELLSVADVAY 880
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-208 |
2.82e-04 |
|
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: 40.68 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 20 INALKATDFSIEAGEFVAIIGPSGSGKSTFL--TIAGGLQTPSSGQLI-------IDGTD-------------------- 70
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndTLYPALARRLHLKKEqpgnhdrIEGLEhidkvividqspigrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 71 ---YTHLSEKERS------------------RLRFKSVGFILQasnlipfLTVQQQLELVDHLTGSKEKAKANQlfdDLG 129
Cdd:cd03271 88 patYTGVFDEIRElfcevckgkrynretlevRYKGKSIADVLD-------MTVEEALEFFENIPKIARKLQTLC---DVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 130 ITGLKhqLPQ---ELSGGERQRAAIARALyHDPA----LILADEPTASL---DTEKAYEVVKLLAkeskEKNKAIIMVTH 199
Cdd:cd03271 158 LGYIK--LGQpatTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLhfhDVKKLLEVLQRLV----DKGNTVVVIEH 230
|
....*....
gi 499604739 200 DDRMLKYCD 208
Cdd:cd03271 231 NLDVIKCAD 239
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-174 |
4.21e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 27 DFS--IEAGEFVAIIGPSGSGKSTFLTIAGGLQTPSSGQLIIDgtdyTHLSekersrlrfksVGFILQ-ASNLIPFLTVq 103
Cdd:PRK11147 337 DFSaqVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLE-----------VAYFDQhRAELDPEKTV- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 104 qqlelVDHLTGSKEKAKAN--------QLFDDL-----GITGLKhqlpqELSGGERQRAAIARALYHDPALILADEPTAS 170
Cdd:PRK11147 401 -----MDNLAEGKQEVMVNgrprhvlgYLQDFLfhpkrAMTPVK-----ALSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
....
gi 499604739 171 LDTE 174
Cdd:PRK11147 471 LDVE 474
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-50 |
7.93e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 7.93e-04
10 20 30
....*....|....*....|....*....|.
gi 499604739 20 INALKATDFSIEAGEFVAIIGPSGSGKSTFL 50
Cdd:PRK00349 622 ENNLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
148-217 |
8.55e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 148 RAAIARALYHDPALILADEPTASLDTEK----AYEVVKLLAKESKEKNKAIIMVTHDDRMLK------YCDKVYRMQDGE 217
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDEDFVEllgrseYVEKFYRLKKNE 1292
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-216 |
1.09e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499604739 141 LSGGERQRAAIARALY---HDPALILADEPTASLDTEKAYEVVKLLaKESKEKNKAIIMVTHDDRMLKYCDKVYRMQDG 216
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQL-RTLVSLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-50 |
1.35e-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: 1.35e-03
10 20 30
....*....|....*....|....*....|.
gi 499604739 20 INALKATDFSIEAGEFVAIIGPSGSGKSTFL 50
Cdd:TIGR00630 621 ENNLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| REC_PatA-like |
cd17602 |
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ... |
150-204 |
4.24e-03 |
|
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.
Pssm-ID: 381129 [Multi-domain] Cd Length: 102 Bit Score: 35.81 E-value: 4.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 499604739 150 AIARALYHDPALILADEPTASLDtekAYEVVKLLAKESKEKNKAIIMVTHDDRML 204
Cdd:cd17602 34 ALTTLLNSKPDLILIDIDMPDLD---GYELCSLLRKSSALKDTPIIMLTGKDGLV 85
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
24-211 |
5.15e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 36.67 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 24 KATDFSIEAGeFVAIIGPSGSGKSTF---------LTIAGGLQTPSSGQLIIDGTdythlseKERSRLRFKSVGFILQAS 94
Cdd:cd03278 14 DKTTIPFPPG-LTAIVGPNGSGKSNIidairwvlgEQSAKSLRGEKMSDVIFAGS-------ETRKPANFAEVTLTFDNS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 95 NLIPFLTVQQQlelVDHLTGSKEKAKAN-QLfddlgitglkhqlpqeLSGGERQRAAIAR--ALYH---DPALILaDEPT 168
Cdd:cd03278 86 DGRYSIISQGD---VSEIIEAPGKKVQRlSL----------------LSGGEKALTALALlfAIFRvrpSPFCVL-DEVD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499604739 169 ASLD---TEKAYEVVKLLAKESKeknkaIIMVTHDDRMLKYCDKVY 211
Cdd:cd03278 146 AALDdanVERFARLLKEFSKETQ-----FIVITHRKGTMEAADRLY 186
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
139-212 |
6.58e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 36.47 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 139 QELSGGERQRAAIA------RAlyhDPA-LILADEPTASLDTEKAYEVVKLLAKESkeKNKAIIMVTHDDRMLKYCDKVY 211
Cdd:cd03272 157 QQLSGGQKSLVALAlifaiqKC---DPApFYLFDEIDAALDAQYRTAVANMIKELS--DGAQFITTTFRPELLEVADKFY 231
|
.
gi 499604739 212 R 212
Cdd:cd03272 232 G 232
|
|
| TraI_TIGR |
TIGR02760 |
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome ... |
3-190 |
6.78e-03 |
|
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome complex. In the process of conjugative plasmid transfer the realaxosome binds to the plasmid at the oriT (origin of transfer) site. The relaxase protein TraI mediates the single-strand nicking and ATP-dependent unwinding (relaxation, helicase activity) of the plasmid molecule. These two activities reside in separate domains of the protein.
Pssm-ID: 274285 [Multi-domain] Cd Length: 1960 Bit Score: 37.19 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 3 VLTFKQVTKTFQDGHHEinalkATDFSIE-AGEFVAIIGPSGSGKSTFL--TIAGGLQTPSSGQLIIDGTDYTHLSEKEr 79
Cdd:TIGR02760 1010 VFLNLELLERLTHGQKQ-----AIHLIIStKDRFVAVQGLAGVGKTTMLesRYKPVLQAFESEQLQVIGLAPTHEAVGE- 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 80 srlrFKSVGfiLQASNLIPFLTVQQQ-----------LELVDH--LTGSKEKAKANQLFDDLG----ITGLKHQLpQELS 142
Cdd:TIGR02760 1084 ----LKSAG--VQAQTLDSFLTDISLyrnsggdfrntLFILDEssMVSNFQLTHATELVQKSGsravSLGDIAQL-QSLA 1156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499604739 143 GGERQRAAIARALYHDPAL--ILADEPTASLDtekayEVVKLLAKESKEK 190
Cdd:TIGR02760 1157 AGKPFELAITFDIIDTAIMkeIVRQNNSAELK-----AAHNSLDKRSNPK 1201
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-210 |
7.68e-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: 36.91 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 141 LSGGERQRAAIAR--------ALYhdpalILaDEPTASL---DTEKAYEVVKLLakesKEKNKAIIMVTHDDRMLKYCDK 209
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsgltgVLY-----VL-DEPSIGLhqrDNRRLINTLKRL----RDLGNTLIVVEHDEDTIRAADY 558
|
.
gi 499604739 210 V 210
Cdd:TIGR00630 559 V 559
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
12-50 |
7.80e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 7.80e-03
10 20 30
....*....|....*....|....*....|....*....
gi 499604739 12 TFqDGHheinalkatDFSIEAGEFVAIIGPSGSGKSTFL 50
Cdd:pfam13555 11 TF-DGH---------TIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
36-200 |
8.64e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.14 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 36 VAIIGPSGSGKSTFLT-IAGGL--QTPSSG----QLIIDGTDYTHLS---EKERSRLRFK------SVGFILQASNLIPF 99
Cdd:COG0419 26 NLIVGPNGAGKSTILEaIRYALygKARSRSklrsDLINVGSEEASVElefEHGGKRYRIErrqgefAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499604739 100 LTVQQQLELVDHLT---GSKEKAKANQLFDDLGITGLKHQL---------PQELSGGERQRAAIARALyhdpALILaDep 167
Cdd:COG0419 106 LKRLLGLEIYEELKerlKELEEALESALEELAELQKLKQEIlaqlsgldpIETLSGGERLRLALADLL----SLIL-D-- 178
|
170 180 190
....*....|....*....|....*....|...
gi 499604739 168 TASLDTEKAYEVVKLLakeskeknKAIIMVTHD 200
Cdd:COG0419 179 FGSLDEERLERLLDAL--------EELAIITHV 203
|
|
| |
