|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-230 |
1.19e-131 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 370.14 E-value: 1.19e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAK 95
Cdd:COG1136 7 LRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLRRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG1136 87 HIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:COG1136 167 LADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-230 |
4.20e-123 |
|
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: 348.33 E-value: 4.20e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAK 95
Cdd:cd03255 3 LKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
16-230 |
1.60e-92 |
|
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: 271.61 E-value: 1.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAK 95
Cdd:COG4181 11 LRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPfhKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG4181 91 HVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGR 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
16-230 |
1.29e-89 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 263.84 E-value: 1.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:COG2884 4 FENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLElVDRMPKRVLELEDGR 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
17-230 |
3.61e-83 |
|
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: 247.26 E-value: 3.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAKH 96
Cdd:TIGR02211 5 ENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 VGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQ 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
16-224 |
2.28e-78 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 236.52 E-value: 2.28e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDaeaskirak 95
Cdd:COG1116 10 LRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 176 LADEPTGNLDS----KSGDVIIKILKelslEQNKTIIVVTHN-FEITKVADRII 224
Cdd:COG1116 161 LMDEPFGALDAltreRLQDELLRLWQ----ETGKTVLFVTHDvDEAVFLADRVV 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
16-230 |
6.67e-77 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 232.25 E-value: 6.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAK 95
Cdd:COG3638 5 LRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hVGFVFQTFNLIPWLTALENVEIAL--------AISGYpFHKR-KRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIAR 166
Cdd:COG3638 82 -IGMIFQQFNLVPRLSVLTNVLAGRlgrtstwrSLLGL-FPPEdRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 167 ALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLaRRYADRIIGLRDGR 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-230 |
9.84e-76 |
|
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: 229.00 E-value: 9.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEvVKRICDRVAVMEKGE 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-230 |
4.48e-75 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 230.73 E-value: 4.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG1135 83 KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG1135 163 LCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDvVRRICDRVAVLENGR 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
16-226 |
4.85e-75 |
|
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: 226.58 E-value: 4.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlddaeaskiRAK 95
Cdd:cd03293 3 VRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------PGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 176 LADEPTGNLDS----KSGDVIIKILKelslEQNKTIIVVTHNFE--ITkVADRIIYL 226
Cdd:cd03293 154 LLDEPFSALDAltreQLQEELLDIWR----ETGKTVLLVTHDIDeaVF-LADRVVVL 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
16-230 |
5.48e-75 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 227.18 E-value: 5.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISkLDDAEASKIRAK 95
Cdd:COG1126 4 IENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hVGFVFQTFNLIPWLTALENVEIALAISgypfHKRKR-----RSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALAN 170
Cdd:COG1126 79 -VGMVFQQFNLFPHLTVLENVTLAPIKV----KKMSKaeaeeRAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 171 NPDVILADEPTGNLD-SKSGDViIKILKELSlEQNKTIIVVTHnfEIT---KVADRIIYLHDGR 230
Cdd:COG1126 154 EPKVMLFDEPTSALDpELVGEV-LDVMRDLA-KEGMTMVVVTH--EMGfarEVADRVVFMDGGR 213
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
23-230 |
7.74e-75 |
|
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: 226.05 E-value: 7.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaKHVGFVFQ 102
Cdd:TIGR02982 11 YGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR-RRIGYIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 103 TFNLIPWLTALENVEIALAISGYPFHK-RKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPT 181
Cdd:TIGR02982 90 AHNLLGFLTARQNVQMALELQPNLSYQeARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1491196576 182 GNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR02982 170 AALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGK 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-226 |
1.88e-74 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 224.80 E-value: 1.88e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAK 95
Cdd:TIGR03608 1 LKNISKKFGDKVI----LDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNFEITKVADRIIYL 226
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-230 |
3.84e-74 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 236.93 E-value: 3.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAK 95
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQAERVIEIRDGE 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-230 |
1.08e-73 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 223.92 E-value: 1.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAKH 96
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 VGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGR 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-230 |
3.10e-73 |
|
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: 221.62 E-value: 3.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaskIRA 94
Cdd:cd03259 2 ELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP------PER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGR 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-230 |
9.67e-71 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 216.18 E-value: 9.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAKHVG 98
Cdd:PRK10584 12 LKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILAD 178
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
16-230 |
1.88e-70 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 214.80 E-value: 1.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:TIGR02673 4 FHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLeQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
16-230 |
2.90e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 212.62 E-value: 2.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlddaEASKIRaK 95
Cdd:COG1131 3 VRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG1131 74 RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLeEAERLCDRVAIIDKGR 208
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
16-230 |
4.05e-69 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 216.12 E-value: 4.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLddaEASKiRak 95
Cdd:COG3842 8 LENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL---PPEK-R-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 176 LADEPTGNLDSKS----GDVIIKILKELsleqNKTIIVVTHNFE--ITkVADRIIYLHDGR 230
Cdd:COG3842 158 LLDEPLSALDAKLreemREELRRLQREL----GITFIYVTHDQEeaLA-LADRIAVMNDGR 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
16-230 |
2.13e-68 |
|
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: 210.05 E-value: 2.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGiLDKPTTGKVFFLGKDISKLDDAEAsKIRA 94
Cdd:cd03257 4 VKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARaILG-LLKPTSGSIIFDGKDLLKLSRRLR-KIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQ----TFNliPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLG---DRLHHRPTELSGGEQQRVAIARA 167
Cdd:cd03257 82 KEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 168 LANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGvVAKIADRVAVMYAGK 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-230 |
4.76e-68 |
|
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: 208.48 E-value: 4.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiRAK 95
Cdd:cd03225 2 LKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQ-----TFNLipwlTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALAN 170
Cdd:cd03225 76 KVGLVFQnpddqFFGP----TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-230 |
3.11e-67 |
|
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: 208.65 E-value: 3.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGK-GRLAVKALD-------------------NVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVF 75
Cdd:cd03294 3 IKGLYKIFGKnPQKAFKLLAkgkskeeilkktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 76 FLGKDISKLDDAEASKIRAKHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELS 155
Cdd:cd03294 83 IDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 156 GGEQQRVAIARALANNPDVILADEPTGNLDSksgdvIIKI-----LKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALDP-----LIRRemqdeLLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDG 237
|
.
gi 1491196576 230 R 230
Cdd:cd03294 238 R 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-230 |
4.11e-67 |
|
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: 206.80 E-value: 4.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVFFLGKDISKLDdaeASKIRa 94
Cdd:COG1122 3 LENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnGLL-KPTSGEVLVDGKDITKKN---LRELR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQT-----FNLipwlTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALA 169
Cdd:COG1122 75 RKVGLVFQNpddqlFAP----TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 170 NNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDlVAELADRVIVLDDGR 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
16-230 |
1.55e-66 |
|
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: 205.88 E-value: 1.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:cd03256 3 VENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIAL--------AISGyPFHKR-KRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIAR 166
Cdd:cd03256 79 QIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFG-LFPKEeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 167 ALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLaREYADRIVGLKDGR 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-230 |
2.04e-66 |
|
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: 204.30 E-value: 2.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlDDAEASKIRaKHVG 98
Cdd:cd03262 6 LHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR-QKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQTFNLIPWLTALENVEIAL-AISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTH--NFeITKVADRIIYLHDGR 230
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHemGF-AREVADRVIFMDDGR 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-230 |
4.39e-66 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 204.44 E-value: 4.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:COG1127 8 VRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIAL-AISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLdSAFAIADRVAVLADGK 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-230 |
1.97e-65 |
|
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: 210.92 E-value: 1.97e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYG-KGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRa 94
Cdd:COG1123 263 VRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELR- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQtfN----LIPWLTALENVEIALAISG-YPFHKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARAL 168
Cdd:COG1123 342 RRVQMVFQ--DpyssLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRyIADRVAVMYDGR 482
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-230 |
1.65e-64 |
|
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: 200.60 E-value: 1.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeASKIRaK 95
Cdd:cd03295 3 FENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDR--LHHRPTELSGGEQQRVAIARALANNPD 173
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGE 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
17-230 |
3.76e-64 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 199.83 E-value: 3.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKGrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaKH 96
Cdd:TIGR02315 5 ENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 VGFVFQTFNLIPWLTALENVEIA-LAISGY------PFHKR-KRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARAL 168
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrLGYKPTwrsllgRFSEEdKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLaKKYADRIVGLKAGE 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
15-230 |
7.84e-64 |
|
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: 196.64 E-value: 7.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAeaSKIRA 94
Cdd:cd03229 2 ELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE--LPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIALaisgypfhkrkrrsrellesvglgdrlhhrptelSGGEQQRVAIARALANNPDV 174
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
16-230 |
5.80e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 200.30 E-value: 5.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiRak 95
Cdd:COG3839 6 LENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----R-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG3839 76 NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQvEAMTLADRIAVMNDGR 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-230 |
2.22e-62 |
|
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: 194.16 E-value: 2.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaKHVG 98
Cdd:cd03292 6 VTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILAD 178
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSLeQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELvDTTRHRVIALERGK 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
16-230 |
6.42e-61 |
|
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: 191.18 E-value: 6.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:cd03261 3 LRGLTKSFGGRTV----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIAL-AISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLdTAFAIADRIAVLYDGK 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-230 |
7.91e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 191.94 E-value: 7.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKrICDRVAVIDAGR 218
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
16-230 |
3.29e-59 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 189.15 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVkalDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeASKIRaK 95
Cdd:COG1125 4 FENVTKRYPDGTVAV---DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD---PVELR-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGL-GDRLHHR-PTELSGGEQQRVAIARALANNPD 173
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdPEEYRDRyPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 174 VILADEPTGNLD----SKSGDVIIKILKELsleqNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG1125 157 ILLMDEPFGALDpitrEQLQDELLRLQREL----GKTIVFVTHDIdEALKLGDRIAVMREGR 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-230 |
4.51e-59 |
|
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: 186.93 E-value: 4.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiRAK 95
Cdd:COG1124 4 VRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----FRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQ----TFNliPWLTALENVEIALAISGYPfhKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARALAN 170
Cdd:COG1124 80 RVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAvVAHLCDRVAVMQNGR 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
33-230 |
1.01e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 184.63 E-value: 1.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeASKIRaKHVGFVFQTFNLIPwlta 112
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR-RQVAYVPQEPALWG---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 lENVEIALAisgYPFHKRKR-----RSRELLESVGLGDR-LHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDS 186
Cdd:COG4619 88 -GTVRDNLP---FPFQLRERkfdreRALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1491196576 187 KSGDVIIKILKELSLEQNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:COG4619 164 ENTRRVEELLREYLAEEGRAVLWVSHDpEQIERVADRVLTLEAGR 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-230 |
2.45e-58 |
|
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: 192.43 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDKP--TTGKVFFLGKDISKLDDAeaskI 92
Cdd:COG1123 7 VRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGgrISGEVLLDGRDLLELSEA----L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 93 RAKHVGFVFQTF--NLIPwLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALAN 170
Cdd:COG1123 81 RGRRIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGvVAEIADRVVVMDDGR 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
15-230 |
2.79e-58 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 188.05 E-value: 2.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDI-SKLDdaeaskIR 93
Cdd:COG1118 4 EVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLP------PR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 AKHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPD 173
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHN----FEitkVADRIIYLHDGR 230
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqeeaLE---LADRVVVMNQGR 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-230 |
5.14e-58 |
|
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: 184.96 E-value: 5.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKG-RLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIR 93
Cdd:TIGR04521 2 KLKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 aKHVGFVFQ-----TFNLipwlTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARA 167
Cdd:TIGR04521 82 -KKVGLVFQfpehqLFEE----TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 168 LANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEdVAEYADRVIVMHKGK 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
16-230 |
9.42e-58 |
|
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: 182.77 E-value: 9.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-----GILDKPTTGKVFFLGKDISKLDDaEAS 90
Cdd:cd03260 3 LRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDV-DVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 91 KIRAKhVGFVFQTFNLIPwLTALENVEIALAISGY-PFHKRKRRSRELLESVGLGDRLHHR--PTELSGGEQQRVAIARA 167
Cdd:cd03260 78 ELRRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 168 LANNPDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELK--KEYTIVIVTHNMQqAARVADRTAFLLNGR 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-230 |
1.11e-57 |
|
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: 185.64 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTL-LNIMGILDKP--TTGKVFFLGKDISKLDDAEASKIRAK 95
Cdd:COG0444 7 LKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGLLPPPgiTSGEILFDGEDLLKLSEKELRKIRGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQ----TFNliPWLTALENVEIALAI-SGYPFHKRKRRSRELLESVGLGD---RLHHRPTELSGGEQQRVAIARA 167
Cdd:COG0444 87 EIQMIFQdpmtSLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 168 LANNPDVILADEPTGNLdsksgDV-----IIKILKELSLEQNKTIIVVTHNFEITK-VADRII--YLhdGR 230
Cdd:COG0444 165 LALEPKLLIADEPTTAL-----DVtiqaqILNLLKDLQRELGLAILFITHDLGVVAeIADRVAvmYA--GR 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
16-230 |
4.05e-57 |
|
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: 181.28 E-value: 4.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavkALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiraK 95
Cdd:cd03300 3 LENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:cd03300 73 PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGK 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-215 |
6.42e-57 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 181.98 E-value: 6.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlDDAEaskiRak 95
Cdd:COG4525 6 VRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD----R-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hvGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE 215
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
23-230 |
1.42e-56 |
|
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: 180.62 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDDAEaskiRAKHVGFVF 101
Cdd:COG1120 11 YGGRPV----LDDVSLSLPPGEVTALLGPNGSGKSTLLRaLAGLL-KPSSGEVLLDGRDLASLSRRE----LARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 102 QTFNLIPWLTALENVEIALaisgYPFHKRKRRS--------RELLESVGLGDrLHHRP-TELSGGEQQRVAIARALANNP 172
Cdd:COG1120 82 QEPPAPFGLTVRELVALGR----YPHLGLFGRPsaedreavEEALERTGLEH-LADRPvDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLLKDGR 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-230 |
4.53e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 179.13 E-value: 4.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 18 SVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGkdISKLDDAEASKIRAKHV 97
Cdd:PRK09493 6 NVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQTFNLIPWLTALENVEIAlaisgyPFHKR-------KRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALAN 170
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFG------PLRVRgaskeeaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAeKVASRLIFIDKGR 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
32-230 |
4.92e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 179.13 E-value: 4.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKlddaeaskiRAKHVGFVFQTFNlIPW- 109
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPPRR---------ARRRIGYVPQRAE-VDWd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 --LTALENVEIALAISGYPFHKRKRRSR----ELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGN 183
Cdd:COG1121 90 fpITVRDVVLMGRYGRRGLFRRPSRADReavdEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1491196576 184 LDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG1121 170 VDAATEEALYELLRELR-REGKTILVVTHDLGaVREYFDRVLLLNRGL 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
16-230 |
3.45e-55 |
|
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: 176.47 E-value: 3.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDdaeASKIRA 94
Cdd:cd03219 3 VRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNlISGFL-RPTSGSVLFDGEDITGLP---PHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIA-LAISGYPFHKRKRRS---------RELLESVGLGDRLHHRPTELSGGEQQRVAI 164
Cdd:cd03219 75 LGIGRTFQIPRLFPELTVLENVMVAaQARTGSGLLLARARReereareraEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 165 ARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDvVMSLADRVTVLDQGR 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
15-230 |
3.69e-55 |
|
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: 175.91 E-value: 3.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskira 94
Cdd:cd03301 2 ELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQvEAMTMADRIAVMNDGQ 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-230 |
5.73e-55 |
|
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: 176.77 E-value: 5.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDdaeASKIRA 94
Cdd:COG0411 7 VRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNlITGFY-RPTSGRILFDGRDITGLP---PHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIAL----------AISGYPFHKRK-----RRSRELLESVGLGDRLHHRPTELSGGEQ 159
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVLVAAharlgrgllaALLRLPRARREerearERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 160 QRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDlVMGLADRIVVLDFGR 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
19-230 |
3.70e-54 |
|
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: 174.06 E-value: 3.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGRlavkALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaskIRAKHVG 98
Cdd:cd03296 8 VSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQTFNLIPWLTALENVEIALAI----SGYPFHKRKRRSRELLESV---GLGDRLhhrPTELSGGEQQRVAIARALANN 171
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVqldWLADRY---PAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQeEALEVADRVVVMNKGR 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
16-230 |
5.80e-54 |
|
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: 171.43 E-value: 5.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKlddaEASKIRa 94
Cdd:cd03230 3 VRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKiILGLL-KPDSGEIKVLGKDIKK----EPEEVK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVeialaisgypfhkrkrrsrellesvglgdrlhhrptELSGGEQQRVAIARALANNPDV 174
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILeEAERLCDRVAILNNGR 172
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
16-230 |
6.20e-54 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 177.15 E-value: 6.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAeaskirAK 95
Cdd:TIGR03265 7 IDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ------KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:TIGR03265 77 DYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:TIGR03265 157 LLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQeEALSMADRIVVMNHGV 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
16-230 |
2.47e-53 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 172.12 E-value: 2.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDIS---KLDDAEASKI 92
Cdd:COG4161 5 LKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 93 RAKhVGFVFQTFNLIPWLTALEN-VEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANN 171
Cdd:COG4161 81 RQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFArKVASQVVYMEKGR 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-230 |
7.58e-53 |
|
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: 170.81 E-value: 7.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlddaEASKIRaK 95
Cdd:COG4555 4 VENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK----EPREAR-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG4555 75 QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHImQEVEALCDRVVILHKGK 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
26-230 |
2.19e-51 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 167.67 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 26 GRLAVkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDIsKL-----------DDAEASKIRA 94
Cdd:COG4598 19 GDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLkpdrdgelvpaDRRQLQRIRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KhVGFVFQTFNLIPWLTALENVEIAlaisgyPFH--KRKR-----RSRELLESVGLGDRLHHRPTELSGGEQQRVAIARA 167
Cdd:COG4598 96 R-LGMVFQSFNLWSHMTVLENVIEA------PVHvlGRPKaeaieRAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 168 LANNPDVILADEPTGNLDSK-SGDViIKILKELSlEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPElVGEV-LKVMRDLA-EEGRTMLVVTHEMGFARdVSSHVVFLHQGR 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-226 |
3.52e-51 |
|
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: 165.40 E-value: 3.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDdaeaskira 94
Cdd:cd03235 2 VEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLL-KPTSGSIRVFGKPLEKER--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNlIPW---LTALENVEIALAISGYPFH----KRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARA 167
Cdd:cd03235 68 KRIGYVPQRRS-IDRdfpISVRDVVLMGLYGHKGLFRrlskADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 168 LANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHN-FEITKVADRIIYL 226
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-230 |
6.21e-51 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 165.96 E-value: 6.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGK--DISKLDDAEASKIR 93
Cdd:PRK11124 5 LNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 AKHVGFVFQTFNLIPWLTALEN-VEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNP 172
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVArKTASRVVYMENGH 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
33-230 |
1.00e-50 |
|
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: 165.20 E-value: 1.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDDAEaskiraKHVGFVFQTFNLIPWLT 111
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFI-KPDSGKILLNGKDITNLPPEK------RDISYVPQNYALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDV 191
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 192 IIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDFeEAWALADKVAIMLNGK 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
33-230 |
5.54e-50 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 163.77 E-value: 5.54e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTG--KVFFLGKDISKLDDAEASKIRA--KHVGFVFQTFNLIP 108
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtiRVGDITIDTARSLSQQKGLIRQlrQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WLTALENV-EIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSK 187
Cdd:PRK11264 99 HRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1491196576 188 -SGDVIIKIlKELSlEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:PRK11264 179 lVGEVLNTI-RQLA-QEKRTMVIVTHEMSFARdVADRAIFMDQGR 221
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
33-230 |
6.49e-50 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 166.40 E-value: 6.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiraKHVGFVFQTFNLIPWLTA 112
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEK------RGIAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVI 192
Cdd:NF040840 90 FENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1491196576 193 IKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHNFeEALSLADRVGIMLNGR 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
16-230 |
1.10e-49 |
|
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: 160.68 E-value: 1.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDdaeaSKIRA 94
Cdd:cd03214 2 VENLSVGYGGRTV----LDDLSLSIEAGEIVGILGPNGAGKSTLLKtLAGLL-KPSSGEILLDGKDLASLS----PKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQtfnlipwltalenveialaisgypfhkrkrrsreLLESVGLGDrLHHRP-TELSGGEQQRVAIARALANNPD 173
Cdd:cd03214 73 RKIAYVPQ----------------------------------ALELLGLAH-LADRPfNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGR 175
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
33-181 |
1.52e-49 |
|
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: 159.35 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDaeasKIRAKHVGFVFQTFNLIPWLTA 112
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 113 LENVEIALAISGYPFHKRKRRSRELLESVGLGD----RLHHRPTELSGGEQQRVAIARALANNPDVILADEPT 181
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-230 |
1.53e-48 |
|
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: 157.54 E-value: 1.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiRAK 95
Cdd:cd03228 3 FKNVSFSYPGR--PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES----LRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTfnliPWL---TALENVeialaisgypfhkrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANNP 172
Cdd:cd03228 77 NIAYVPQD----PFLfsgTIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALA--KGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-230 |
2.61e-48 |
|
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: 159.90 E-value: 2.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTL-LNIMGILdKPTTGKVFFLGkdISKLDDAEASKIRa 94
Cdd:TIGR04520 3 VENVSFSYPES--EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaKLLNGLL-LPTSGKVTVDG--LDTLDEENLWEIR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQT-FNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPD 173
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGK 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-230 |
3.91e-48 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 157.92 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlddaEASKIRAKh 96
Cdd:cd03265 4 ENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 VGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMeEAEQLCDRVAIIDHGR 209
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
31-230 |
6.11e-48 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 158.23 E-value: 6.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLL---NIMGILDKP--TTGKVFFLGKDI--SKLDDAEaskIRaKHVGFVFQT 103
Cdd:TIGR00972 15 EALKNINLDIPKNQVTALIGPSGCGKSTLLrslNRMNDLVPGvrIEGKVLFDGQDIydKKIDVVE---LR-RRVGMVFQK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 FNLIPwLTALENVEIALAISGY-PFHKRKRRSRELLESVGL----GDRLHHRPTELSGGEQQRVAIARALANNPDVILAD 178
Cdd:TIGR00972 91 PNPFP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALAVEPEVLLLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:TIGR00972 170 EPTSALDPIATGKIEELIQELK--KKYTIVIVTHNMQQAaRISDRTAFFYDGE 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-230 |
9.87e-48 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 161.65 E-value: 9.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 2 ETLAESKQKDLVYILDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDI 81
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFD----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 82 SKLDdAEAskiraKHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQR 161
Cdd:PRK09452 79 THVP-AEN-----RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 162 VAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE--ITkVADRIIYLHDGR 230
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEeaLT-MSDRIVVMRDGR 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-230 |
2.69e-47 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 162.88 E-value: 2.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVFFLGKDISKLDDAEAskiRA 94
Cdd:COG1129 7 MRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILsGVY-QPDSGEILLDGEPVRFRSPRDA---QA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRK---RRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANN 171
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRamrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLK-AQGVAIIYISHRLdEVFEIADRVTVLRDGR 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-230 |
2.82e-47 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 157.12 E-value: 2.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLL---NIMG--ILDKPTTGKVFFLGKDISKlDDAEASKIRaKHV 97
Cdd:COG1117 21 YGD----KQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNdlIPGARVEGEILLDGEDIYD-PDVDVVELR-RRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQTFNLIPwLTALENVEIALAISGYpfhKRKRRSREL----LESVGL----GDRLHHRPTELSGGEQQRVAIARALA 169
Cdd:COG1117 95 GMVFQKPNPFP-KSIYDNVAYGLRLHGI---KSKSELDEIveesLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 170 NNPDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELK--KDYTIVIVTHNMqQAARVSDYTAFFYLGE 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
15-230 |
2.85e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.07 E-value: 2.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRLavkaldNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskira 94
Cdd:COG3840 3 RLDDLTYRYGDFPL------RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:COG3840 71 RPVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGR 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
15-230 |
3.96e-47 |
|
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: 155.04 E-value: 3.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRlavkALDNVSFTVKRGeFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDaeasKIRa 94
Cdd:cd03264 2 QLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIVEdVESLCNQVAVLNKGK 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-229 |
2.10e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 157.55 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLddaeasKIRAK 95
Cdd:PRK10851 5 IANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL------HARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENveIALAISGYPFHKR------KRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALA 169
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDN--IAFGLTVLPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 170 NNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQeEAMEVADRVVVMSQG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-230 |
4.24e-46 |
|
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: 150.86 E-value: 4.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGrlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKirakHVG 98
Cdd:cd00267 5 LSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR----RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQtfnlipwltalenveialaisgypfhkrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANNPDVILAD 178
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPElAELAADRVIVLKDGK 157
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-230 |
8.79e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 155.27 E-value: 8.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 22 IYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKDISKLDDAEASKIRaKHVGFV 100
Cdd:COG4608 23 LFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRlLLRLEE-PTSGEILFDGQDITGLSGRELRPLR-RRMQMV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 101 FQ----TFNliPWLTALENVEIALAISG-YPFHKRKRRSRELLESVGLgDRLH-HR-PTELSGGEQQRVAIARALANNPD 173
Cdd:COG4608 101 FQdpyaSLN--PRMTVGDIIAEPLRIHGlASKAERRERVAELLELVGL-RPEHaDRyPHEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 174 VILADEPTGNLdsksgDV-----IIKILKELSLEQNKTIIVVTHNFEITK-VADRII--YLhdGR 230
Cdd:COG4608 178 LIVCDEPVSAL-----DVsiqaqVLNLLEDLQDELGLTYLFISHDLSVVRhISDRVAvmYL--GK 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-230 |
1.42e-45 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 151.57 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaK 95
Cdd:PRK10908 4 FEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGlISRRSYRMLTLSDGH 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-230 |
2.46e-44 |
|
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: 148.28 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlDDAEASKirak 95
Cdd:cd03266 4 ADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLR-ALGKCILFSTHIMqEVERLCDRVVVLHRGR 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
33-229 |
3.19e-44 |
|
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: 148.38 E-value: 3.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISklddaEASKIRAkhvgFVFQTFNLIPWLTA 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-----EPGPDRM----VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENveIALAISGYPFHKRKRRSRELLES----VGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKS 188
Cdd:TIGR01184 72 REN--IALAVDRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1491196576 189 GDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-230 |
4.61e-44 |
|
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: 147.58 E-value: 4.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDDAEaskiRAKH-VGFV 100
Cdd:cd03224 10 YGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLL-PPRSGSIRFDGRDITGLPPHE----RARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 101 FQTFNLIPWLTALENVEIALaisgypFHKRKRRSRELLESV-----GLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGA------YARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFAlEIADRAYVLERGR 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-230 |
6.31e-44 |
|
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: 147.06 E-value: 6.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 35 NVSFTVKrGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGkdiSKLDDAEASKI---RAKHVGFVFQTFNLIPWLT 111
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRKKINlppQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIalaisGYPFH---KRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKS 188
Cdd:cd03297 92 VRENLAF-----GLKRKrnrEDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1491196576 189 GDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLsEAEYLADRIVVMEDGR 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
32-215 |
1.28e-43 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 147.54 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKdisKLDDAEASKirakhvGFVFQTFNLIPWLT 111
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPGAER------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDV 191
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....
gi 1491196576 192 IIKILKELSLEQNKTIIVVTHNFE 215
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIE 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
15-230 |
1.96e-43 |
|
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: 146.11 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlddaEASKIRa 94
Cdd:cd03263 2 QIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQtFNLIPW-LTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPD 173
Cdd:cd03263 75 QSLGYCPQ-FDALFDeLTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMdEAEALCDRIAIMSDGK 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-230 |
2.78e-43 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 149.48 E-value: 2.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 7 SKQKDLVyILDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKldd 86
Cdd:PRK11432 1 MTQKNFV-VLKNITKRFGSNTV----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 87 aeaSKIRAKHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESV---GLGDRLhhrPTELSGGEQQRVA 163
Cdd:PRK11432 73 ---RSIQQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVdlaGFEDRY---VDQISGGQQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 164 IARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDqSEAFAVSDTVIVMNKGK 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-230 |
2.84e-43 |
|
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: 152.92 E-value: 2.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKT-TLLNIMGILDKP---TTGKVFFLGKDISKLDDAEASKIRAKHVG 98
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRIRGNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQTfnliPwLTAL-----------ENVEIALAISGypfHKRKRRSRELLESVGLGD---RLHHRPTELSGGEQQRVAI 164
Cdd:COG4172 96 MIFQE----P-MTSLnplhtigkqiaEVLRLHRGLSG---AAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 165 ARALANNPDVILADEPTGNLdsksgDV-----IIKILKELSLEQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:COG4172 168 AMALANEPDLLIADEPTTAL-----DVtvqaqILDLLKDLQRELGMALLLITHDLGVvRRFADRVAVMRQGE 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
16-230 |
4.68e-43 |
|
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: 144.54 E-value: 4.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAeaskiRAK 95
Cdd:COG4133 5 AENLSCRRGERLL----FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-----YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFhkRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG4133 76 RLAYLGHADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNfEITKVADRIIYLHDGR 230
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQ-PLELAAARVLDLGDFK 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
23-230 |
5.52e-43 |
|
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: 145.12 E-value: 5.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDdaeASKIRAKHVGFVF 101
Cdd:COG0410 13 YGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLP---PHRIARLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 102 QTFNLIPWLTALENVEIALAIsgypfHKRKRRSRELLESVG-----LGDRLHHRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:COG0410 85 EGRRIFPSLTVEENLLLGAYA-----RRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 177 ADEPTgnldskSG------DVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG0410 160 LDEPS------LGlaplivEEIFEIIRRLN-REGVTILLVEQNARfALEIADRAYVLERGR 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
48-230 |
6.54e-43 |
|
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: 147.64 E-value: 6.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 48 VMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLddaeASKIRakHVGFVFQTFNLIPWLTALENVEIALAISGYPF 127
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV----PPHLR--HINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 128 HKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTI 207
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....
gi 1491196576 208 IVVTHN-FEITKVADRIIYLHDGR 230
Cdd:TIGR01187 155 VFVTHDqEEAMTMSDRIAIMRKGK 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-230 |
8.58e-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: 153.45 E-value: 8.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKDISKLDDAEaskIRaKHVGFVFQTfnliPWL 110
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKlLLGLYE-PTSGRILIDGIDLRQIDPAS---LR-RQIGVVLQD----VFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 ---TALENveIALAISGYPFHkrkrRSRELLESVGLGDRLHHRP-----------TELSGGEQQRVAIARALANNPDVIL 176
Cdd:COG2274 561 fsgTIREN--ITLGDPDATDE----EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-230 |
8.88e-43 |
|
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: 143.90 E-value: 8.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGRlavkALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAeaskirAKHVG 98
Cdd:cd03268 6 LTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------LRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQTFNLIPWLTALENVEIALAISGypfhKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILAD 178
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLLG----IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 179 EPTGNLDSKSgdviIKILKELSL---EQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03268 152 EPTNGLDPDG----IKELRELILslrDQGITVLISSHLLsEIQKVADRIGIINKGK 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-230 |
1.29e-42 |
|
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: 151.45 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKDISKLDDAEaskiR 93
Cdd:COG4988 338 ELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNlLLGFLP-PYSGSILINGVDLSDLDPAS----W 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 AKHVGFVFQTfnliPWL---TALENveIALAisgypfhkRKRRSRE----LLESVGLGD-------RLHHRPTE----LS 155
Cdd:COG4988 410 RRQIAWVPQN----PYLfagTIREN--LRLG--------RPDASDEeleaALEAAGLDEfvaalpdGLDTPLGEggrgLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 156 GGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQADRILVLDDGR 548
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-230 |
1.56e-42 |
|
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: 150.99 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 22 IYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTL-LNIMGILdkPTTGKVFFLGKDISKLDDAEASKIRaKHVGFV 100
Cdd:COG4172 291 LFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLR-RRMQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 101 FQ----TFNliPWLTALENVEIALAISGYPFHKRKRRSR--ELLESVGLGDRLHHR-PTELSGGEQQRVAIARALANNPD 173
Cdd:COG4172 368 FQdpfgSLS--PRMTVGQIIAEGLRVHGPGLSAAERRARvaEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 174 VILADEPTGNLdsksgDV-----IIKILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:COG4172 446 LLVLDEPTSAL-----DVsvqaqILDLLRDLQREHGLAYLFISHDLAVVRaLAHRVMVMKDGK 503
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-229 |
2.44e-42 |
|
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: 142.78 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlddaeasKIRAK 95
Cdd:cd03226 2 IENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-------KERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIpwLTAlENVEIALAISGYPFHKRKRRSRELLESVGLgDRLHHR-PTELSGGEQQRVAIARALANNPDV 174
Cdd:cd03226 72 SIGYVMQDVDYQ--LFT-DSVREELLLGLKELDAGNEQAETVLKDLDL-YALKERhPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDG 229
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEfLAKVCDRVLLLANG 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-230 |
3.33e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 141.26 E-value: 3.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEAS-KIRAKH--------VGFVF 101
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlKVADKNqlrllrtrLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 102 QTFNLIPWLTALENV-EIALAISGYPFHKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARALANNPDVILADE 179
Cdd:PRK10619 99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 180 PTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARhVSSHVIFLHQGK 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-229 |
3.54e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 145.18 E-value: 3.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 2 ETLAESKQKDLVYILDSVTK--IYGKGRLAVKALDnVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGK 79
Cdd:PRK10070 12 KIFGEHPQRAFKYIEQGLSKeqILEKTGLSLGVKD-ASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 80 DISKLDDAEASKIRAKHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQ 159
Cdd:PRK10070 91 DIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMR 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 160 QRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK10070 171 QRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNG 241
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
32-230 |
9.91e-41 |
|
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: 146.45 E-value: 9.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKDISKLDDAEaskIRAkHVGFVFQTfnliPWL 110
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLD-PQSGSITLGGVDLRDLDEDD---LRR-RIAVVPQR----PHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 ---TALENVEIAlaisgypfhkRKRRS----RELLESVGLGDRLHHRP-----------TELSGGEQQRVAIARALANNP 172
Cdd:COG4987 421 fdtTLRENLRLA----------RPDATdeelWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRLAGLERMDRILVLEDGR 546
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
32-230 |
1.34e-40 |
|
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: 142.55 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDnVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDiskLDDAEASKIRAKH---VGFVFQTFNLIP 108
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV---LQDSARGIFLPPHrrrIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WLTALENVEIalaisGYPFHKRKRRSRELLESV---GLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLD 185
Cdd:COG4148 91 HLSVRGNLLY-----GRKRAPRAERRISFDEVVellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1491196576 186 SKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLdEVARLADHVVLLEQGR 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-230 |
2.00e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 140.18 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGR-LAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlDDAEASKIRaKHV 97
Cdd:PRK13637 8 LTHIYMEGTpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIR-KKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQ--TFNLIPwltalENVE--IA-----LAISGYPFHKRKRRSREL--LESVGLGDRlhhRPTELSGGEQQRVAIAR 166
Cdd:PRK13637 86 GLVFQypEYQLFE-----ETIEkdIAfgpinLGLSEEEIENRVKRAMNIvgLDYEDYKDK---SPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 167 ALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGK 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-230 |
2.69e-40 |
|
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: 137.41 E-value: 2.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILdKPTTGKVFFLGKdisKLDDAEASKIrakhv 97
Cdd:cd03269 6 VTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIrMILGII-LPDSGEVLFDGK---PLDIAARNRI----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMElVEELCDRVLLLNKGR 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-230 |
3.09e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.31 E-value: 3.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKDISKLDDAEaskIRaKHVGFVF 101
Cdd:COG1132 349 YPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNlLLRFYD-PTSGRILIDGVDIRDLTLES---LR-RQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 102 QTfnliPWL---TALENveIALAisgypfhkRKRRSRELLES----VGLGDRLHHRP-----------TELSGGEQQRVA 163
Cdd:COG1132 421 QD----TFLfsgTIREN--IRYG--------RPDATDEEVEEaakaAQAHEFIEALPdgydtvvgergVNLSGGQRQRIA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 164 IARALANNPDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-230 |
8.10e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 137.91 E-value: 8.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKG-RLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDDAEaskiR 93
Cdd:COG1101 4 LKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNaIAGSL-PPDSGSILIDGKDVTKLPEYK----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 AKHVGFVFQ-----TFnliPWLTALENveIALAIS-GYPFH-----KRKRRS--RELLESVGLG--DRLHHRPTELSGGE 158
Cdd:COG1101 79 AKYIGRVFQdpmmgTA---PSMTIEEN--LALAYRrGKRRGlrrglTKKRRElfRELLATLGLGleNRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 159 QQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEqALDYGNRLIMMHEGR 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
31-229 |
8.29e-40 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 137.84 E-value: 8.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGIL--DKPTTGKVFFLGKDISKlDDAEASKIRAK--HVGFVFQTFN 105
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSAGSHIELLGRTVQR-EGRLARDIRKSraNTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 LIPWLTALENVEIAlAISGYPFHK---------RKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:PRK09984 97 LVNRLSVLENVLIG-ALGSTPFWRtcfswftreQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEIT-KVADRIIYLHDG 229
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQG 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-230 |
2.25e-39 |
|
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: 133.71 E-value: 2.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEAskiRAK 95
Cdd:cd03216 3 LRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---RRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQtfnlipwltalenveialaisgypfhkrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANNPDVI 175
Cdd:cd03216 76 GIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLdEVFEIADRVTVLRDGR 159
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
32-230 |
4.76e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.27 E-value: 4.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeASKIRaKHVGFVFQT-FNLIPWL 110
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEIR-KKIGIIFQNpDNQFIGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGD 190
Cdd:PRK13632 100 TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 191 VIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGK 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-230 |
5.63e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 140.93 E-value: 5.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNI-MGILdKPTTGKVFFLGKDISKLDDAEAskiRA 94
Cdd:COG3845 8 LRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKIlYGLY-QPDSGEILIDGKPVRIRSPRDA---IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRK---RRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANN 171
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKaarARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLA-AEGKSIIFITHKLrEVMAIADRVTVLRRGK 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-185 |
1.07e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 133.38 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDKP--TTGKVFFLGKDISKLddaeasK 91
Cdd:COG4136 3 SLENLTITLGGRPL----LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTAL------P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 92 IRAKHVGFVFQTFNLIPWLTALENVEIALAiSGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANN 171
Cdd:COG4136 73 AEQRRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170
....*....|....
gi 1491196576 172 PDVILADEPTGNLD 185
Cdd:COG4136 152 PRALLLDEPFSKLD 165
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-230 |
1.34e-38 |
|
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: 132.67 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 18 SVTKIYGKGRLAVkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNI-MGILDKP-TTGKVFFLGKDISKlddaeaSKIRaK 95
Cdd:cd03213 12 TVKSSPSKSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNAlAGRRTGLgVSGEVLINGRPLDK------RSFR-K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGypfhkrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANNPDVI 175
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTH--NFEITKVADRIIYLHDGR 230
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHqpSSEIFELFDKLLLLSQGR 189
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
30-230 |
2.27e-38 |
|
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: 133.17 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILD--KPTTGKVFFLGKDISKlddaeasKIRAKHVGFVFQTFNL 106
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEggGTTSGQILFNGQPRKP-------DQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 IPWLTALENVEIAlAISGYPFHKRKRRSRELLESVGLGDrLHHRP------TELSGGEQQRVAIARALANNPDVILADEP 180
Cdd:cd03234 93 LPGLTVRETLTYT-AILRLPRKSSDAIRKKRVEDVLLRD-LALTRiggnlvKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 181 TGNLDSKSGDVIIKILKELSlEQNKTIIVVTHN--FEITKVADRIIYLHDGR 230
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLA-RRNRIVILTIHQprSDLFRLFDRILLLSSGE 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
37-230 |
2.29e-38 |
|
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: 132.62 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 37 SFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiraKHVGFVFQTFNLIPWLTALENV 116
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 117 EIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKIL 196
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1491196576 197 KELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGR 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
26-230 |
2.31e-38 |
|
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: 132.94 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 26 GRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLL-----NIMgildkPTTGKVFFLGK----DISKLDDAEASKIRAKH 96
Cdd:COG4778 20 GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLkciygNYL-----PDSGSILVRHDggwvDLAQASPREILALRRRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 VGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHH-RPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG4778 95 IGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREaVADRVVDVTPFS 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-230 |
3.06e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 134.83 E-value: 3.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGR-LAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISK---------- 83
Cdd:PRK13651 4 KVKNIVKIFNKKLpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekekv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 84 LDDAEASKIRA----------KHVGFVFQTFNLIPWLTALENVEIALAIS-GYPFHKRKRRSRELLESVGLG-DRLHHRP 151
Cdd:PRK13651 84 LEKLVIQKTRFkkikkikeirRRVGVVFQFAEYQLFEQTIEKDIIFGPVSmGVSKEEAKKRAAKYIELVGLDeSYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 152 TELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDnVLEWTKRTIFFKDGK 242
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
30-230 |
4.06e-38 |
|
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: 132.33 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskIRaKHVGFVFQTfnliPW 109
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LR-RNIGYVPQD----VT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 L---TALENveIALaisGYPFHKrkrrSRELLESV--------------GLGDRLHHRPTELSGGEQQRVAIARALANNP 172
Cdd:cd03245 89 LfygTLRDN--ITL---GAPLAD----DERILRAAelagvtdfvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSLEqnKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-229 |
5.68e-38 |
|
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: 138.40 E-value: 5.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILD--KPTTGKVF----------------FL 77
Cdd:TIGR03269 3 VKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpsKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 78 GK--------------DISKLDDAEASKIRaKHVGFVFQ-TFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVG 142
Cdd:TIGR03269 79 GEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 143 LGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVAD 221
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEvIEDLSD 237
|
....*...
gi 1491196576 222 RIIYLHDG 229
Cdd:TIGR03269 238 KAIWLENG 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-230 |
1.09e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 132.62 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIY-------GKGRLAVkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEA 89
Cdd:TIGR02769 6 RDVTHTYrtgglfgAKQRAPV--LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 90 SKIRaKHVGFVFQ----TFNliPWLTALEnveialaISGYPFH--------KRKRRSRELLESVGL-GDRLHHRPTELSG 156
Cdd:TIGR02769 84 RAFR-RDVQLVFQdspsAVN--PRMTVRQ-------IIGEPLRhltsldesEQKARIAELLDMVGLrSEDADKLPRQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 157 GEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRlVQSFCQRVAVMDKGQ 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-229 |
1.98e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 132.60 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKGR-LAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDI-SKLDDAEASKIRa 94
Cdd:PRK13646 6 DNVSYTYQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQtfnlIPWLTALE-NVEIALAIS----GYPFHKRKRRSRELLESVGLG-DRLHHRPTELSGGEQQRVAIARAL 168
Cdd:PRK13646 85 KRIGMVFQ----FPESQLFEdTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMnEVARYADEVIVMKEG 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
33-230 |
1.98e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 131.43 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVFFLGKDISKLDDAEASKIRA-----KHVGFVFqtfnl 106
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRRAvlpqhSSLSFPF----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 ipwlTALENVEIALaisgYPFHKRKRRSRELLESV-------GLGDRLHHrptELSGGEQQRVAIARALA------NNPD 173
Cdd:PRK13548 92 ----TVEEVVAMGR----APHGLSRAEDDALVAAAlaqvdlaHLAGRDYP---QLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAaRYADRIVLLHQGR 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
33-230 |
2.20e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 131.39 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVFFLGKDISKLDDAEASKIRA-----KHVGFVFqtfnl 106
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARRRAvlpqhSSLAFPF----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 ipwlTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALA-------NNPDVILADE 179
Cdd:COG4559 91 ----TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 180 PTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLNLAaQYADRILLLHQGR 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
32-230 |
4.78e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 131.36 E-value: 4.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISklDDAEASKIRAKhVGFVFQT-FNLIPWL 110
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLWDIRNK-AGMVFQNpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGD 190
Cdd:PRK13633 102 IVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 191 VIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGK 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-230 |
6.40e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.91 E-value: 6.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILDkPTTGKVFFLGKdisKLDDAEASKIRAKhVGFVFQT-FNLIPW 109
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLLL-PEAGTITVGGM---VLSEETVWDVRRQ-VGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 LTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSG 189
Cdd:PRK13635 97 ATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1491196576 190 DVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK13635 177 REVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGE 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-230 |
1.53e-36 |
|
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: 1.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGK-VFFLGKDISKLDDAEaskIRa 94
Cdd:COG1119 6 LRNVTVRRG-GK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWE---LR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFV--FQTFNLIPWLTALENVeialaISGY---------PFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVA 163
Cdd:COG1119 78 KRIGLVspALQLRFPRDETVLDVV-----LSGFfdsiglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 164 IARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGR 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
16-230 |
1.57e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.41 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKvffLGKDISKLDDAEaSKIRak 95
Cdd:PRK11247 15 LNAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE---LLAGTAPLAEAR-EDTR-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hvgFVFQTFNLIPWLTALENVeiALAISGypfhKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK11247 85 ---LMFQDARLLPWKKVIDNV--GLGLKG----QWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGK 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-230 |
2.58e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.84 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILDkPTTGKVFFLGKDISKLDdaeaskirA 94
Cdd:COG4152 4 LKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGILA-PDSGEVLWDGEPLDPED--------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVeIALA-ISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPD 173
Cdd:COG4152 71 RRIGYLPEERGLYPKMKVGEQL-VYLArLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMElVEELCDRIVIINKGR 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-230 |
1.17e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 126.95 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGIL-----DKPTTGKVFFLGKDISKLDDAEaskIRaKHVGFVFQTF 104
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE---LR-RRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 105 NLIPWLTALENVEIALAISGYPFHKRK--RRSRELLESVGL----GDRLHHRPTELSGGEQQRVAIARALANNPDVILAD 178
Cdd:PRK14247 92 NPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 179 EPTGNLDSKSGDVIIKILkeLSLEQNKTIIVVTH-NFEITKVADRIIYLHDGR 230
Cdd:PRK14247 172 EPTANLDPENTAKIESLF--LELKKDMTIVLVTHfPQQAARISDYVAFLYKGQ 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-229 |
2.17e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 126.79 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFlgkDISKLDDAEASKIRaKHVGFVFQT-FNLIPWL 110
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITDDNFEKLR-KHIGIVFQNpDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGD 190
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1491196576 191 VIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
33-230 |
2.83e-35 |
|
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: 123.48 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaSKIRAKHVGFVFQTFNLIPWlTA 112
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD----PNELGDHVGYLPQDDELFSG-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENVeialaisgypfhkrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVI 192
Cdd:cd03246 93 AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 1491196576 193 IKILKELSLeQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03246 136 NQAIAALKA-AGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
16-230 |
3.30e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 128.61 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKdisKLDDAEASKiraK 95
Cdd:PRK11000 6 LRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPAE---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 176 LADEPTGNLDS----KSGDVIIKILKELsleqNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:PRK11000 156 LLDEPLSNLDAalrvQMRIEISRLHKRL----GRTMIYVTHDqVEAMTLADKIVVLDAGR 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-229 |
5.63e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.90 E-value: 5.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAKHVGFVFQ-----TFN 105
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpehqLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 lipwltalENVEIALAIS----GYPFHKRKRRSRELLESVGLG-DRLHHRPTELSGGEQQRVAIARALANNPDVILADEP 180
Cdd:PRK13634 101 --------ETVEKDICFGpmnfGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491196576 181 TGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDG 229
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEdAARYADQIVVMHKG 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
26-229 |
5.87e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 125.33 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 26 GRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDaeasKIRAKHVGFVFQ--- 102
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY----KYRCKHIRMIFQdpn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 103 -TFNliPWLTALENVEIALAI-SGYPFHKRKRRSRELLESVGL-GDRLHHRPTELSGGEQQRVAIARALANNPDVILADE 179
Cdd:COG4167 98 tSLN--PRLNIGQILEEPLRLnTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 180 PTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDG 229
Cdd:COG4167 176 ALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKhISDKVLVMHQG 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-230 |
7.98e-35 |
|
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: 127.15 E-value: 7.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 25 KGRLAVKALDnVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKdisKLDDAEASKIRAKH---VGFVF 101
Cdd:TIGR02142 6 SKRLGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR---TLFDSRKGIFLPPEkrrIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 102 QTFNLIPWLTALENVEIALAISGYPfhKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPT 181
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPS--ERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491196576 182 GNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLqEVLRLADRVVVLEDGR 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-230 |
1.22e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 124.71 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTL-LNIMGILdKPTTGKVFFLGKDISklDDAEASKIRa 94
Cdd:PRK13644 4 LENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLL-RPQKGKVLVSGIDTG--DFSKLQGIR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTfnliPWLTAL-ENVEIALAISGY-----PFHKRKRRSRELLEsVGLGDRLHHRPTELSGGEQQRVAIARAL 168
Cdd:PRK13644 77 KLVGIVFQN----PETQFVgRTVEEDLAFGPEnlclpPIEIRKRVDRALAE-IGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGK 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-230 |
1.47e-34 |
|
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: 122.58 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDKpTTGKVFFLGKdisklddaeaskirakhVGFVFQTfnliPWL 110
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS-----------------IAYVSQE----PWI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 ---TALENVeialaISGYPFHkrKRRSRELLESVGL---------GDRlhhrpTE-------LSGGEQQRVAIARALANN 171
Cdd:cd03250 78 qngTIRENI-----LFGKPFD--EERYEKVIKACALepdleilpdGDL-----TEigekginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIK--ILKELSLeqNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
31-229 |
3.18e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 122.96 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLL---NIMGILDK--PTTGKVFFLGKDI--SKLDDAEaskIRaKHVGFVFQT 103
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPevTITGSIVYNGHNIysPRTDTVD---LR-KEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 FNLIPwLTALENVEIALAISGYpfhKRKRRSRELLESVGLG--------DRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK14239 95 PNPFP-MSIYENVVYGLRLKGI---KDKQVLDEAVEKSLKGasiwdevkDRLHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILkeLSLEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMqQASRISDRTGFFLDG 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-226 |
3.94e-34 |
|
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: 128.17 E-value: 3.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDiskLDDAEASKIRaKHVGFVFQTfnliPWL 110
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP---LADADADSWR-DQIAWVPQH----PFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TA---LENveIALAISGYPFHKRKRRSR-----ELLESV--GLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEP 180
Cdd:TIGR02857 408 FAgtiAEN--IRLARPDASDAEIREALEragldEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEP 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1491196576 181 TGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYL 226
Cdd:TIGR02857 486 TAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
15-230 |
5.24e-34 |
|
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: 121.88 E-value: 5.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGrlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLddaEASKIRA 94
Cdd:cd03218 2 RAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL---PMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVrETLSITDRAYIIYEGK 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
16-230 |
6.17e-34 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 124.96 E-value: 6.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDnvsFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiraK 95
Cdd:PRK11650 6 LQAVRKSYDGKTQVIKGID---LDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 176 LADEPTGNLDSKsgdviIKI-----LKELSLEQNKTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:PRK11650 157 LFDEPLSNLDAK-----LRVqmrleIQRLHRRLKTTSLYVTHDqVEAMTLADRVVVMNGGV 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-230 |
6.71e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 122.87 E-value: 6.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKGRLAVKA-----LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASK 91
Cdd:PRK10419 7 SGLSHHYAHGGLSGKHqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 92 IRaKHVGFVFQ----TFN---LIPW--------LTALENVEialaisgypfhkRKRRSRELLESVGLGDR-LHHRPTELS 155
Cdd:PRK10419 87 FR-RDIQMVFQdsisAVNprkTVREiireplrhLLSLDKAE------------RLARASEMLRAVDLDDSvLDKRPPQLS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 156 GGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRlVERFCQRVMVMDNGQ 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-230 |
6.85e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 121.67 E-value: 6.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKgRLAVKaldNVSFTVKRGEflVV--MGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDDAEaskiR 93
Cdd:COG1137 7 ENLVKSYGK-RTVVK---DVSLEVNQGE--IVglLGPNGAGKTTTFYmIVGLV-KPDSGRIFLDGEDITHLPMHK----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 AKH-VGF------VFQTfnlipwLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIAR 166
Cdd:COG1137 76 ARLgIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 167 ALANNPDVILADEPTGNLDSKS-GDV--IIKILKElsleqnKTI-IVVT-HNF-EITKVADRIIYLHDGR 230
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAvADIqkIIRHLKE------RGIgVLITdHNVrETLGICDRAYIISEGK 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
32-230 |
9.68e-34 |
|
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: 121.09 E-value: 9.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLddaeASKIRAKH-VGFVFQTFNLIPW 109
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLL-PVKSGSIRLDGEDITKL----PPHERARAgIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 LTALENVEIALAisgypfhKRKRRSRELLESV-----GLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPT-GN 183
Cdd:TIGR03410 90 LTVEENLLTGLA-------ALPRRSRKIPDEIyelfpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTeGI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 184 LDSksgdvIIK----ILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:TIGR03410 163 QPS-----IIKdigrVIRRLRAEGGMAILLVEQYLDFAReLADRYYVMERGR 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
32-230 |
2.66e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.34 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTL-LNIMGILdKPTTGKVFFLGKDIsKLDDAEASKIRaKHVGFVFQTF-NLIPW 109
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGIL-KPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNPdDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 LTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSG 189
Cdd:PRK13639 94 PTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1491196576 190 DVIIKILKELSlEQNKTIIVVTHNFEITKV-ADRIIYLHDGR 230
Cdd:PRK13639 174 SQIMKLLYDLN-KEGITIIISTHDVDLVPVyADKVYVMSDGK 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-230 |
3.05e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 122.54 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKT-TLLNIMGILDKPttGKVF-----FLGKDISKLDDAEASKIRAKH 96
Cdd:PRK11022 13 FGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISEKERRNLVGAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 VGFVFQ--TFNLIPWLTALENVEIALAI-SGYPFHKRKRRSRELLESVGLGD---RLHHRPTELSGGEQQRVAIARALAN 170
Cdd:PRK11022 91 VAMIFQdpMTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQ 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
3.10e-33 |
|
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: 125.69 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 1 METLAESKQKDLVYILDSVTKI-------YGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNI-MGILDkPTTG 72
Cdd:TIGR03269 261 MEGVSEVEKECEVEVGEPIIKVrnvskryISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIiAGVLE-PTSG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 73 KVFF-LGKD-ISKLDDAEASKIRAK-HVGFVFQTFNLIPWLTALENVEIALAISgYPFHKRKRRSRELLESVGLGDR--- 146
Cdd:TIGR03269 340 EVNVrVGDEwVDMTKPGPDGRGRAKrYIGILHQEYDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEEkae 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 147 --LHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDS----KSGDVIIKILKELsleqNKTIIVVTHNFE-ITKV 219
Cdd:TIGR03269 419 eiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEM----EQTFIIVSHDMDfVLDV 494
|
250
....*....|.
gi 1491196576 220 ADRIIYLHDGR 230
Cdd:TIGR03269 495 CDRAALMRDGK 505
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
16-230 |
3.96e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 120.19 E-value: 3.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaSKIRAK 95
Cdd:COG4604 4 IKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP----SRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVeialAISGYPFHK-R-----KRRSRELLESVGLGDrLHHRP-TELSGGEQQRVAIARAL 168
Cdd:COG4604 76 RLAILRQENHINSRLTVRELV----AFGRFPYSKgRltaedREIIDEAIAYLDLED-LADRYlDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTH--NFEITkVADRIIYLHDGR 230
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHdiNFASC-YADHIVAMKDGR 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-230 |
1.34e-32 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 118.49 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISkldDAEASKIRaK 95
Cdd:cd03251 3 FKNVTFRYPGD--GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR---DYTLASLR-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQT---FNLipwlTALENVEIAlaisgypfhkRKRRSRELLESV---------------GLGDRLHHRPTELSGG 157
Cdd:cd03251 77 QIGLVSQDvflFND----TVAENIAYG----------RPGATREEVEEAaraanahefimelpeGYDTVIGERGVKLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 158 EQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTIENADRIVVLEDGK 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-229 |
1.43e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 119.00 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDK------PTTGKVFFLGKDISKLDdaeASKIRaKHVGFVFQTFNL 106
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQID---AIKLR-KEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 IPWLTALENVEIALAISGYpfhKRKRRSRELLES----VGLG----DRLHHRPTELSGGEQQRVAIARALANNPDVILAD 178
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGI---KEKREIKKIVEEclrkVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSLEQnkTIIVVTHN-FEITKVADRIIYLHDG 229
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNpQQVARVADYVAFLYNG 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-230 |
2.02e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.16 E-value: 2.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGR-LAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAKHV 97
Cdd:PRK13641 8 VDYIYSPGTpMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQtFNLIPWL--TALENVEIALAISGYPFHKRKRRSRELLESVGLGDRL-HHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:PRK13641 88 SLVFQ-FPEAQLFenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMdDVAEYADDVLVLEHGK 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
37-230 |
3.34e-32 |
|
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: 116.88 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 37 SFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiraKHVGFVFQTFNLIPWLTALENV 116
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 117 EIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKIL 196
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1491196576 197 KELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLsDARAIASQIAVVSQGK 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-230 |
4.04e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.30 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskIRAKhVGFVFQ-----TFN 105
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSK-VGLVFQdpddqVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 LIPWltalENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLD 185
Cdd:PRK13647 95 STVW----DDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1491196576 186 SKSGDVIIKILKELSlEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:PRK13647 171 PRGQETLMEILDRLH-NQGKTVIVATHDVDLAaEWADQVIVLKEGR 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
34-221 |
6.82e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 117.56 E-value: 6.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 34 DNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaKHVGFVFQTFNLIPWLTAL 113
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 114 ENVeialaisGYPFHKRKRRSREL--------LESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLD 185
Cdd:PRK11831 103 DNV-------AYPLREHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1491196576 186 SKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVAD 221
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVpEVLSIAD 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
32-230 |
6.90e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 119.94 E-value: 6.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiraKHVGFVFQTFNLIPWLT 111
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ------RPINMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGD- 190
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDr 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1491196576 191 ---VIIKILKELSLeqnkTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK11607 188 mqlEVVDILERVGV----TCVMVTHDQeEAMTMAGRIAIMNRGK 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-230 |
1.43e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 117.88 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVFFLGKDISKLDDAEASKIrakhvGFVF-QTFNLI 107
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEVRVLGYVPFKRRKEFARRI-----GVVFgQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLhHRPT-ELSGGEQQRVAIARALANNPDVILADEPTGNLDS 186
Cdd:COG4586 109 WDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELL-DTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1491196576 187 KSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDdIEALCDRVIVIDHGR 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-230 |
1.79e-31 |
|
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: 115.51 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVFFLGKDISKLDDAEASKIr 93
Cdd:cd03267 19 LIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILsGLL-QPTSGEVRVAGLVPWKRRKKFLRRI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 akhvGFVFQTFNLIPW-LTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNP 172
Cdd:cd03267 97 ----GVVFGQKTQLWWdLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMkDIEALARRVLVIDKGR 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
33-230 |
2.96e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.98 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKdisKLDDAEASKIRAKhVGFVFQT-FNLIPWLT 111
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIRHK-IGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDV 191
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 1491196576 192 IIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQ 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-230 |
3.21e-31 |
|
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: 113.30 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 24 GKGRLAVK------ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGiLDKPTTGKVFFLGKDISKLDDAEAskiRAKH 96
Cdd:cd03215 1 GEPVLEVRglsvkgAVRDVSFEVRAGEIVGIAGLVGNGQTELAEaLFG-LRPPASGEITLDGKPVTRRSPRDA---IRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 VGFV---FQTFNLIPWLTALENveIALAISgypfhkrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANNPD 173
Cdd:cd03215 77 IAYVpedRKREGLVLDLSVAEN--IALSSL------------------------------LSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELdELLGLCDRILVMYEGR 181
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
37-230 |
4.66e-31 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 114.29 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 37 SFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskiraKHVGFVFQTFNLIPWLTALENV 116
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 117 EIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKIL 196
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1491196576 197 KELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEdAARIAPRSLVVADGR 207
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
32-230 |
8.76e-31 |
|
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: 113.74 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskIRAKhVGFVFQTfNLIPWLT 111
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LRRQ-VGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENveIALAISGYPFHKRKRRSR---------ELLEsvGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTG 182
Cdd:cd03252 92 IRDN--IALADPGMSMERVIEAAKlagahdfisELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1491196576 183 NLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03252 168 ALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGR 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-230 |
9.55e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 115.83 E-value: 9.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 18 SVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlDDAEASKIRAKHV 97
Cdd:PRK11308 16 PVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQKLLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQtfN----LIPWLTALENVEIALAI-SGYPFHKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARALANN 171
Cdd:PRK11308 95 QIVFQ--NpygsLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLRPEHYDRyPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEhIADEVMVMYLGR 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
31-226 |
1.46e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 112.89 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLdDAEASKiraKHVGFVFQTfnliPWL 110
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL-KPEIYR---QQVSYCAQT----PTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 ---TALENVEialaisgYPFHKRKRRS-----RELLESVGLGDR-LHHRPTELSGGEQQRVAIARALANNPDVILADEPT 181
Cdd:PRK10247 93 fgdTVYDNLI-------FPWQIRNQQPdpaifLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1491196576 182 GNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYL 226
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-230 |
1.80e-30 |
|
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: 112.70 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKDISKLDDAEaskIRaKHVGFVF 101
Cdd:cd03254 12 YDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINlLMRFYD-PQKGQILIDGIDIRDISRKS---LR-SMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 102 QTfnliPWL---TALEN------------VEIALAISGypFHKRKRRSRELLESVglgdrLHHRPTELSGGEQQRVAIAR 166
Cdd:cd03254 84 QD----TFLfsgTIMENirlgrpnatdeeVIEAAKEAG--AHDFIMKLPNGYDTV-----LGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 167 ALANNPDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGK 214
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
30-229 |
2.57e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 114.62 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILD---KPTTGKVFFLGKDISKLDDAEASKIRAKHVGFVFQ--T 103
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 FNLIPWLTALENVEIALAISGYP------FHKRKRRSRELLESVGLGDrlhHR------PTELSGGEQQRVAIARALANN 171
Cdd:COG4170 100 SCLDPSAKIGDQLIEAIPSWTFKgkwwqrFKWRKKRAIELLHRVGIKD---HKdimnsyPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDG 229
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLEsISQWADTITVLYCG 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-230 |
2.86e-30 |
|
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: 112.32 E-value: 2.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeASKIRa 94
Cdd:cd03253 2 EFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQT---FNLipwlTALENV----------EIALAISGYPFHKRKRRSRELLESVgLGDRlhhrPTELSGGEQQR 161
Cdd:cd03253 75 RAIGVVPQDtvlFND----TIGYNIrygrpdatdeEVIEAAKAAQIHDKIMRFPDGYDTI-VGER----GLKLSGGEKQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 162 VAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVNADKIIVLKDGR 212
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
13-230 |
2.91e-30 |
|
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: 112.37 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 13 VYILDSVTKIYGKgRLAVKaldNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKI 92
Cdd:TIGR04406 1 TLVAENLIKSYKK-RKVVN---DVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 93 rakHVGFVFQTFNLIPWLTALENVEIALAISGYPFHK-RKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANN 171
Cdd:TIGR04406 77 ---GIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAeREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 172 PDVILADEPTGNLDSKS-GDV--IIKILKelslEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAvGDIkkIIKHLK----ERGIGVLITDHNVrETLDICDRAYIISDGK 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
34-230 |
7.43e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.34 E-value: 7.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 34 DNVSFTVKRGEFLVVMGPSGSGKT-TLLNIMGILDKP----TTGKVFFLGKDISKLDDAEASKIRAKHVGFVFQTfnliP 108
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQE----P 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 W--LTALENVEIALA--ISgypFHKRKRR--SR----ELLESVGL---GDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK15134 102 MvsLNPLHTLEKQLYevLS---LHRGMRReaARgeilNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGR 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-230 |
9.45e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.47 E-value: 9.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGIL-----DKPTTGKVFFLGKDISKlDDAEASKIRaKHVGFVFQTFNLI 107
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVR-REVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PWLTALENVEIALAISGYPFHKRK--RRSRELLESVGL----GDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPT 181
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491196576 182 GNLDSKSGDVIIKILKELSLEQnkTIIVVTHN-FEITKVADRIIYLHDGR 230
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSpAQAARVSDYVAFLYLGK 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-230 |
1.73e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTT---LLNIMGILDKPTTGKVFFLGkdiSKLDDAEASKIRAKhVGFVFQT-FNLI 107
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG---ITLTAKTVWDIREK-VGIVFQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSK 187
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1491196576 188 SGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGK 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-230 |
2.10e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.82 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgRLAVkalDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlddaEASKIRAK 95
Cdd:PRK13537 10 FRNVEKRYGD-KLVV---DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK13537 82 -VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMeEAERLCDRLCVIEEGR 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-229 |
2.81e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 114.50 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIrak 95
Cdd:PRK09700 8 MAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIA-------LAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARAL 168
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSLEqNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
30-230 |
3.84e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 111.74 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKT-TLLNIMGILDKP--TTGKVFFLGKDISKLDDAEASKIRAKHVGFVFQ--TF 104
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRAEQISMIFQdpMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 105 NLIPWLTALENVEIALAIsgypfHKRKRRSRELLESVGLGD---------RLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLML-----HKGMSKAEAFEESVRMLDavkmpearkRMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEItkVA---DRIIYLHDGR 230
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGV--VAgicDKVLVMYAGR 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-230 |
3.86e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.01 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFfLGKDISklddaeaskirak 95
Cdd:COG0488 1 LENLSKSFGGRPL----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-IPKGLR------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hVGFVFQTFNLIPWLTALENVEIAL-----------------------------------AISGYPFHkrkRRSRELLES 140
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLDGDaelraleaeleeleaklaepdedlerlaelqeefeALGGWEAE---ARAEEILSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 141 VGLGDRLHHRP-TELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSgdviIKILKELSLEQNKTIIVVTHN--FeIT 217
Cdd:COG0488 139 LGFPEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYPGTVLVVSHDryF-LD 213
|
250
....*....|...
gi 1491196576 218 KVADRIIYLHDGR 230
Cdd:COG0488 214 RVATRILELDRGK 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
32-226 |
5.35e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.70 E-value: 5.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVfflgkdisklddaeaSKIRAKHVGFVFQTFNLiPW- 109
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKvLAGVL-RPTSGTV---------------RRAGGARVAYVPQRSEV-PDs 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 --LTALENVEIALAISGYPFHKRKRRSR----ELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGN 183
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRRLTRDDRaavdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1491196576 184 LDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITKVADRIIYL 226
Cdd:NF040873 150 LDAESRERIIALLAEEH-ARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-230 |
7.65e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.10 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGR-LAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKV----FFLGKDISKLDdaEA 89
Cdd:PRK13645 8 ILDNVSYTYAKKTpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIK--EV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 90 SKIRaKHVGFVFQ--TFNLIPwltalENVEIALAISGYPFHKRK----RRSRELLESVGLGDRLHHR-PTELSGGEQQRV 162
Cdd:PRK13645 86 KRLR-KEIGLVFQfpEYQLFQ-----ETIEKDIAFGPVNLGENKqeayKKVPELLKLVQLPEDYVKRsPFELSGGQKRRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 163 AIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGK 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-230 |
7.73e-29 |
|
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: 113.69 E-value: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 25 KGRLAVKA------------LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVFFLGKDISKLDDAEask 91
Cdd:COG4618 328 KGRLSVENltvvppgskrpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREE--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 92 iRAKHVGFVFQTFNLIPWlTALEN------------VEIA-LA-----IS----GYpfhkrkrrsrellESVgLGDRLHH 149
Cdd:COG4618 404 -LGRHIGYLPQDVELFDG-TIAENiarfgdadpekvVAAAkLAgvhemILrlpdGY-------------DTR-IGEGGAR 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 150 rpteLSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:COG4618 468 ----LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
.
gi 1491196576 230 R 230
Cdd:COG4618 543 R 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
32-213 |
7.79e-29 |
|
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: 113.22 E-value: 7.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKDISKLDDAEASKIrakhVGFVFQTFNLIPwL 110
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLAtLAGLLD-PLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFD-T 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TALENVEIAlaisgypfhkRKRRS----RELLESVGLGDRLHHRP-----------TELSGGEQQRVAIARALANNPDVI 175
Cdd:TIGR02868 424 TVRENLRLA----------RPDATdeelWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILkeLSLEQNKTIIVVTHN 213
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
30-230 |
1.05e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 110.33 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKV----FFLGKDISKLDDAEAS---KIR-----AKHV 97
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPyskKIKnfkelRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQTFNLIPWLTALENV----EIALAISGYPFHKRkrrSRELLESVGLGDR-LHHRPTELSGGEQQRVAIARALANNP 172
Cdd:PRK13631 119 SMVFQFPEYQLFKDTIEKDimfgPVALGVKKSEAKKL---AKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKElSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEhVLEVADEVIVMDKGK 253
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
30-230 |
1.50e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 107.62 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAeaskirakhVGFVfqtfnliPW 109
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG---------GGFN-------PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 LTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSG 189
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1491196576 190 DVIIKILKELsLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03220 179 EKCQRRLREL-LKQGKTVILVSHDPSsIKRLCDRALVLEKGK 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-230 |
2.74e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.06 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTT---GKVFFLGKDIsklddaEASKIRAKhVGFVFQTFNLIPW 109
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI------DAKEMRAI-SAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 LTALEnveiALAISG-------YPFHKRKRRSRELLESVGLGDRLH------HRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:TIGR00955 114 LTVRE----HLMFQAhlrmprrVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTH--NFEITKVADRIIYLHDGR 230
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHqpSSELFELFDKIILMAEGR 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
17-230 |
3.07e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 107.70 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAKH 96
Cdd:PRK11701 10 RGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 V-----GFVFQtfN----LIPWLTALENV-EIALAISGYPFHKRKRRSRELLESVGLG-DRLHHRPTELSGGEQQRVAIA 165
Cdd:PRK11701 86 LlrtewGFVHQ--HprdgLRMQVSAGGNIgERLMAVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 166 RALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKV-ADRIIYLHDGR 230
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGR 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-230 |
3.43e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 109.03 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 29 AVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGiLDKPTTGKVFFLGKDISKLDDAEASKIRaKHVGFVFQT--FN 105
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 LIPWLTALENVEIALAISgYPFHKR---KRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARALANNPDVILADEPT 181
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTY-HPKLSRqevKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491196576 182 GNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKhISDRVLVMYLGH 239
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-221 |
4.22e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.56 E-value: 4.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 7 SKQKDLVYILDSVTKIYGKgRLAVKaldNVSFTVKRGEFLVVMGPSGSGKTTLL---NIMG--ILDKPTTGKVFFLGKDI 81
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGS-FLAVK---NVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNdlIPGFRVEGKVTFHGKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 82 SKlDDAEASKIRaKHVGFVFQTFNLIPwLTALENVEIALAISGYP-----FHKRKRRSRELLESVGlgDRLHHRPTELSG 156
Cdd:PRK14243 80 YA-PDVDPVEVR-RRIGMVFQKPNPFP-KSIYDNIAYGARINGYKgdmdeLVERSLRQAALWDEVK--DKLKQSGLSLSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 157 GEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKElsLEQNKTIIVVTHNF-EITKVAD 221
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE--LKEQYTIIIVTHNMqQAARVSD 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
30-230 |
5.29e-28 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 108.74 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILD---KPTTGKVFFLGKDISKLDDAEASKIRAKHVGFVFQTfn 105
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKaICGVTKdnwRVTADRMRFDDIDLLRLSPRERRKLVGHNVSMIFQE-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 liPW--LTALENVEIAL--AISGYP--------FHKRKRRSRELLESVGLGDR---LHHRPTELSGGEQQRVAIARALAN 170
Cdd:PRK15093 98 --PQscLDPSERVGRQLmqNIPGWTykgrwwqrFGWRKRRAIELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmLSQWADKINVLYCGQ 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
30-230 |
5.52e-28 |
|
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: 106.47 E-value: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeASKIRaKHVGFVFQTfnliPW 109
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLR-SQIGLVSQE----PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 L---TALENveIALAisgypfhkRKRRSRELLESV-----------GLGDRLH----HRPTELSGGEQQRVAIARALANN 171
Cdd:cd03249 88 LfdgTIAEN--IRYG--------KPDATDEEVEEAakkanihdfimSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
30-230 |
5.90e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.20 E-value: 5.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILdKPTTGKVFFLGKDISKlddAEASKIRaKHVGFVFQTFNLIP 108
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFrHFNGIL-KPTSGSVLIRGEPITK---ENIREVR-KFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WLTALENvEIALAIS--GYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDS 186
Cdd:PRK13652 92 FSPTVEQ-DIAFGPInlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1491196576 187 KSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGR 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-230 |
6.09e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.55 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAKhvgfvfqtfnlIPW 109
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS-----------VPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 LTALE---NVEIALAISGYPFHKR--------KRRSRELLESVGLgDRLHHRP-TELSGGEQQRVAIARALANNPDVILA 177
Cdd:PRK09536 85 DTSLSfefDVRQVVEMGRTPHRSRfdtwtetdRAAVERAMERTGV-AQFADRPvTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLaARYCDELVLLADGR 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
33-230 |
6.57e-28 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 106.46 E-value: 6.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdkPTTGKVFFLGKDISKLDDAEASKIRA------KHVGF--VFQT 103
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHRAylsqqqSPPFAmpVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 FNL-IPWLTALENVEIALAisgypfhkrkrrsrELLESVGLGDRLHHRPTELSGGEQQRVAIARAL-----ANNPD--VI 175
Cdd:COG4138 90 LALhQPAGASSEAVEQLLA--------------QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTlRHADRVWLLKQGK 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
16-230 |
9.91e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.99 E-value: 9.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkGRLAVkalDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISklddAEASKIRAK 95
Cdd:PRK13536 44 LAGVSKSYG-DKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP----ARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hVGFVFQTFNLIPWLTALENveiaLAISGYPFHKRKRRSRE----LLESVGLGDRLHHRPTELSGGEQQRVAIARALANN 171
Cdd:PRK13536 116 -IGVVPQFDNLDLEFTVREN----LLVFGRYFGMSTREIEAvipsLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMeEAERLCDRLCVLEAGR 249
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
33-230 |
1.50e-27 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 105.53 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILD-KPTTGKVFFLGKDISKLDDAEaskiRAKH-VGFVFQ------- 102
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHPKyEVTSGSILLDGEDILELSPDE----RARAgIFLAFQypveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 103 --TFNLIpwLTALENVEIAlAISGYPFHKrkrRSRELLESVGLGDRLHHRP--TELSGGEQQRVAIARALANNPDVILAD 178
Cdd:COG0396 92 vsVSNFL--RTALNARRGE-ELSAREFLK---LLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNFEITK--VADRIIYLHDGR 230
Cdd:COG0396 166 ETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHYQRILDyiKPDFVHVLVDGR 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-230 |
2.08e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.16 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaskira 94
Cdd:COG1134 24 LKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 khVGFVFQtfnliPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLhHRP--TeLSGGEQQRVAIARALANNP 172
Cdd:COG1134 95 --LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFI-DQPvkT-YSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 173 DVILADEPTGnldskSGDVI-----IKILKELsLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:COG1134 166 DILLVDEVLA-----VGDAAfqkkcLARIREL-RESGRTVIFVSHSMGaVRRLCDRAIWLEKGR 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-230 |
4.14e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 108.46 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 24 GKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEAskIRAKhVGFVFQT 103
Cdd:PRK11288 11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA--LAAG-VAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 FNLIPWLTALENVEI-ALAISGYPFHKR--KRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEP 180
Cdd:PRK11288 88 LHLVPEMTVAENLYLgQLPHKGGIVNRRllNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 181 TGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELR-AEGRVILYVSHRMeEIFALCDAITVFKDGR 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
31-230 |
4.18e-27 |
|
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: 102.39 E-value: 4.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDDAeaskiRAKHVGFVFQTFNLIpw 109
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDL-KPQQGEITLDGVPVSDLEKA-----LSSLISVLNQRPYLF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 ltalenveialaisgypfhkrkrrSRELLESVGlgdrlhhrpTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSG 189
Cdd:cd03247 88 ------------------------DTTLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1491196576 190 DVIIKILkeLSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03247 135 RQLLSLI--FEVLKDKTLIWITHHLTGIEHMDKILFLENGK 173
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-230 |
9.38e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.06 E-value: 9.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGR-LAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRA 94
Cdd:PRK13649 5 LQNVSYTYQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQtF--NLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARALANN 171
Cdd:PRK13649 85 KKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAME 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK13649 164 PKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMdDVANYADFVYVLEKGK 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
19-230 |
1.31e-26 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 103.37 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGrlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKD-----ISKLDDAEASKIR 93
Cdd:TIGR02323 9 LSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 AKHVGFVFQTF--NLIPWLTALENV-EIALAISGYPFHKRKRRSRELLESVGLG-DRLHHRPTELSGGEQQRVAIARALA 169
Cdd:TIGR02323 85 RTEWGFVHQNPrdGLRMRVSAGANIgERLMAIGARHYGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIARNLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 170 NNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDGR 230
Cdd:TIGR02323 165 TRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGR 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
32-230 |
1.90e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILdKPTTGKVFFLGKDIskldDAEASKIRA--KHVGFVFQT-FNLI 107
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFqNLNGIL-KPSSGRILFDGKPI----DYSRKGLMKlrESVGMVFQDpDNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PWLTALENVEIALAISGYPFHKRKRRSRELLESVGLgDRLHHRPTE-LSGGEQQRVAIARALANNPDVILADEPTGNLDS 186
Cdd:PRK13636 96 FSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1491196576 187 KSGDVIIKILKELSLEQNKTIIVVTHNFEITKV-ADRIIYLHDGR 230
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGR 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-230 |
3.90e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGiLDKPTTGKVFFLGKDISKLDDAEAskIRAkhvGFVF-----QTF 104
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARaLFG-ADPADSGEIRLDGKPVRIRSPRDA--IRA---GIAYvpedrKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 105 NLIPWLTALENVEIAlAISGYPFHKRKRRSRELLESVGLGDRLHHRP-------TELSGGEQQRVAIARALANNPDVILA 177
Cdd:COG1129 340 GLVLDLSIRENITLA-SLDRLSRGGLLDRRRERALAEEYIKRLRIKTpspeqpvGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 178 DEPTGNLD--SKSGdvIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG1129 419 DEPTRGIDvgAKAE--IYRLIRELA-AEGKAVIVISSELpELLGLSDRILVMREGR 471
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-230 |
5.03e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.63 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLddaeASKIRAKHVGFVFQ 102
Cdd:PRK11231 12 YGTKRI----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML----SSRQLARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 103 TfNLIP-WLTALENVEIA----LAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:PRK11231 84 H-HLTPeGITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLnQASRYCDHLVVLANGH 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-218 |
1.17e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.40 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGK-TTLLNIMGILdkPTTGKVFFLGKDISKLDDAEASKIRaKHVGFVFQTFN--LIP 108
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKsTTGLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNssLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WLTALENVEIALAISgYPF---HKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARALANNPDVILADEPTGNL 184
Cdd:PRK15134 378 RLNVLQIIEEGLRVH-QPTlsaAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190
....*....|....*....|....*....|....
gi 1491196576 185 DSKSGDVIIKILKELSLEQNKTIIVVTHNFEITK 218
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVR 490
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-227 |
1.32e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.88 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTL---LNIMGILDKPT--TGKVFFLGKDISKlDDAEASKIRaKHVGFVFQTFN 105
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEVrvEGRVEFFNQNIYE-RRVNLNRLR-RQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 LIPwLTALENVEIALAISGYpfhKRKRRSRELLESV--------GLGDRLHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIVGW---RPKLEIDDIVESAlkdadlwdEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLH 227
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLhQVSRLSDFTAFFK 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-230 |
1.55e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.86 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 14 YILD--SVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILDKPT-TGKVFFLGKDIsklddaEA 89
Cdd:PRK13549 4 YLLEmkNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsGVYPHGTyEGEIIFEGEEL------QA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 90 SKIR---AKHVGFVFQTFNLIPWLTALENV----EIALA-ISGYPfhKRKRRSRELLESVGLGDRLHHRPTELSGGEQQR 161
Cdd:PRK13549 74 SNIRdteRAGIAIIHQELALVKELSVLENIflgnEITPGgIMDYD--AMYLRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 162 VAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLnEVKAISDTICVIRDGR 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-230 |
2.22e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.57 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISkldDAEASKIRAK 95
Cdd:PRK11614 8 FDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENveiaLAISGYpFHKRKRRSRELLESVGLGDRLHHRPTE----LSGGEQQRVAIARALANN 171
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEEN----LAMGGF-FAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLR-EQGMTIFLVEQNAnQALKLADRGYVLENGH 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
30-230 |
2.48e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.18 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGiLDKPTTGKVFFLGKDISKLDdaeASKIRAKHVGFV---FQTFN 105
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEaLAG-LRPPASGSIRLDGEDITGLS---PRERRRLGVAYIpedRLGRG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 LIPWLTALENVeIALAISGYPFHKR--------KRRSRELLE--SVGLGDrLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG3845 347 LVPDMSVAENL-ILGRYRRPPFSRGgfldrkaiRAFAEELIEefDVRTPG-PDTPARSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELR-DAGAAVLLISEDLdEILALSDRIAVMYEGR 479
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-230 |
3.96e-25 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 102.56 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILDKPT-TGKVFFLG-----KDISkldDAEASKIRAKHvgfvfQ 102
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsGVYPHGSyEGEILFDGevcrfKDIR---DSEALGIVIIH-----Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 103 TFNLIPWLTALENV----EIAL--AISgypFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:NF040905 86 ELALIPYLSIAENIflgnERAKrgVID---WNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLnEIRRVADSITVLRDGR 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
32-212 |
4.57e-25 |
|
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: 97.81 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDaeaskIRAKHVGFVFQTFNLIPWLT 111
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-----EPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYpfhkRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDsKSGDV 191
Cdd:TIGR01189 90 ALENLHFWAAIHGG----AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAGVA 164
|
170 180
....*....|....*....|.
gi 1491196576 192 IIKILKELSLEQNKTIIVVTH 212
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
16-230 |
5.30e-25 |
|
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: 95.98 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVfflgkdisklddaeaskirak 95
Cdd:cd03221 3 LENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hvgfvfqtfnlipwlTALENVEIalaisGYpFHKrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANNPDVI 175
Cdd:cd03221 58 ---------------TWGSTVKI-----GY-FEQ------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELsleqNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEY----PGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
33-230 |
5.31e-25 |
|
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: 102.43 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaSKIRAKHVGFVFQTFNLIPWLTA 112
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD----RETFGKHIGYLPQDVELFPGTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 L------ENVE----IALA-ISGypfhkrkrrSRELLESV--GLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADE 179
Cdd:TIGR01842 410 EniarfgENADpekiIEAAkLAG---------VHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 180 PTGNLDSKSGDVIIKILKELSLeQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGCVDKILVLQDGR 530
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-212 |
5.57e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 97.57 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 34 DNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASkirakhvgfvfqtfNLI------ 107
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ--------------DLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 ---PWLTALENVEIALAISGYPfhkRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIAR-ALANNPDVILaDEPTGN 183
Cdd:PRK13538 84 gikTELTALENLRFYQRLHGPG---DDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL-DEPFTA 159
|
170 180
....*....|....*....|....*....
gi 1491196576 184 LDSKSGDVIIKILkELSLEQNKTIIVVTH 212
Cdd:PRK13538 160 IDKQGVARLEALL-AQHAEQGGMVILTTH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-230 |
8.16e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 8.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 11 DLVYILDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFfLGKDIsklddaea 89
Cdd:COG0488 313 KKVLELEGLSKSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKlLAGEL-EPDSGTVK-LGETV-------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 90 skirakHVGFVFQTF-NLIPWLTALENVEialaiSGYPfHKRKRRSRELLESVGL-GDRLHHRPTELSGGEQQRVAIARA 167
Cdd:COG0488 379 ------KIGYFDQHQeELDPDKTVLDELR-----DGAP-GGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 168 LANNPDVILADEPTGNLDSKSgdviIKILKELSLEQNKTIIVVTHN--FeITKVADRIIYLHDGR 230
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDryF-LDRVATRILEFEDGG 506
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-230 |
1.67e-24 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 97.31 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 36 VSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdkPTTGKVFFLGKDISKLDDAEASKIRA-----KHVGF---VFQTFNL 106
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHRAylsqqQTPPFampVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 -IPWLTALENVEIALaisgypfhkrkrrsRELLESVGLGDRLHHRPTELSGGEQQRVAIARAL-----ANNPD--VILAD 178
Cdd:PRK03695 93 hQPDKTRTEAVASAL--------------NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTlRHADRVWLLKQGK 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-230 |
2.01e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 97.86 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTG-----KVFFLGKDISKLDDAEASKIRakhVGFVFQTFNLI 107
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRR---VGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PwLTALENVeialaISGYPFHKRKRR------SRELLESVGL----GDRLHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:PRK14271 114 P-MSIMDNV-----LAGVRAHKLVPRkefrgvAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKelSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIR--SLADRLTVIIVTHNLaQAARISDRAALFFDGR 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-213 |
2.06e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.10 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIrAKHVGFvfqtfnLIPWLTA 112
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY-LGHRNA------MKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENVEIALAISGypfhKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSgdvi 192
Cdd:PRK13539 91 AENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA---- 162
|
170 180
....*....|....*....|....
gi 1491196576 193 IKILKEL---SLEQNKTIIVVTHN 213
Cdd:PRK13539 163 VALFAELiraHLAQGGIVIAATHI 186
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
33-230 |
2.11e-24 |
|
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: 96.06 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILD-KPTTGKVFFLGKDISKLDDAEaskiRAKH-VGFVFQtfnlipw 109
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEE----RARLgIFLAFQ------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 ltalenveialaisgYPFHKRKRRSRELLESVGLGdrlhhrpteLSGGEQQRVAIARALANNPDVILADEPTGNLDSKSG 189
Cdd:cd03217 85 ---------------YPPEIPGVKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1491196576 190 DVIIKILKELsLEQNKTIIVVTHNFEITK--VADRIIYLHDGR 230
Cdd:cd03217 141 RLVAEVINKL-REEGKSVLIITHYQRLLDyiKPDRVHVLYDGR 182
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
30-230 |
3.43e-24 |
|
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: 100.56 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDIS--KLDDaeaskIRAkHVGFVFQTFNLI 107
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdyTLAS-----LRR-QVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PwLTALENVEIAlAISGYPfhkrKRRSRELLESVGLGDRLHHRP-----------TELSGGEQQRVAIARALANNPDVIL 176
Cdd:TIGR02203 419 N-DTIANNIAYG-RTEQAD----RAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKElsLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALER--LMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-224 |
5.06e-24 |
|
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: 96.32 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 18 SVTKIYGKGRLAVKALDnvsftVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISklddAEASKIRAKHV 97
Cdd:cd03237 5 TMKKTLGEFTLEVEGGS-----ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS----YKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQTFNlipwltalenvEIALAISGYPFHKRkrrsrELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:cd03237 76 GTVRDLLS-----------SITKDFYTHPYFKT-----EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRII 224
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIiMIDYLADRLI 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-230 |
5.87e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 96.21 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 26 GRLAVkalDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDaeaSKIRAKHVGFVFQTFN 105
Cdd:PRK11300 17 GLLAV---NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG---HQIARMGVVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 LIPWLTALENVEIA-------------LAISGYPFHKRK--RRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALAN 170
Cdd:PRK11300 91 LFREMTVIENLLVAqhqqlktglfsglLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKlVMGISDRIYVVNQGT 231
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-230 |
1.66e-23 |
|
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: 94.46 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 27 RLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDaeasKIRAKHVGFVFQTfnl 106
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH----KYLHSKVSLVGQE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 iPWLTA---LENveIALAISGYPFHKRKRRSR--------ELLESvGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:cd03248 97 -PVLFArslQDN--IAYGLQSCSFECVKEAAQkahahsfiSELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWP--ERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-229 |
2.36e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.77 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILDKpTTGKVFFLGKDISkLDDAEASKirAKHVGFVFQTFNLIP 108
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLtGIYTR-DAGSILYLGKEVT-FNGPKSSQ--EAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WLTALENV----EIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNL 184
Cdd:PRK10762 93 QLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1491196576 185 DSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK10762 173 TDTETESLFRVIRELK-SQGRGIVYISHRLkEIFEICDDVTVFRDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-230 |
2.42e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.00 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 27 RLAVKALDNVSFTVKRGEFLVVMGPSGSGKT-TLLNIMGILDKpTTGKV----FFLGK------DISKLDDAEASKIRAK 95
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVqcdkMLLRRrsrqviELSEQSAAQMRHVRGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQ--TFNLIPWLTALEnvEIALAI---SGYPFHKRKRRSRELLESVGLGDR---LHHRPTELSGGEQQRVAIARA 167
Cdd:PRK10261 105 DMAMIFQepMTSLNPVFTVGE--QIAESIrlhQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 168 LANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGE 246
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
33-229 |
3.08e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.57 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGI-------LDKPTTGKVFFLgkdisklddAEASKIrakhvgfvfqtf 104
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRaIAGLwpygsgrIARPAGARVLFL---------PQRPYL------------ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 105 nliPWLTALEnveiALAisgYPFHKRK---RRSRELLESVGLG---DRLH---HRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:COG4178 438 ---PLGTLRE----ALL---YPATAEAfsdAELREALEAVGLGhlaERLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKElSLEqNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLRE-ELP-GTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
34-230 |
3.17e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.38 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 34 DNVSFTVKRGEFLVVMGPSGSGKT-TLLNIMGILD---KPTTGKVFFLGKDISklddaeASKIRAKHVGFVFQT----FN 105
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVA------PCALRGRKIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 106 liPWLTALENVEIALAISGYPfhKRKRRSRELLESVGLGDR---LHHRPTELSGGEQQRVAIARALANNPDVILADEPTG 182
Cdd:PRK10418 94 --PLHTMHTHARETCLALGKP--ADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1491196576 183 NLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGR 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-230 |
3.30e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.61 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdkPTTGKVFFLGKDISKLDDAEASKirakHVGFVFQTFNLiPWLT 111
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELDPESWRK----HLSWVGQNPQL-PHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENV----------EIALAIsgypfhkRKRRSRELLESVGLGdrLHHRPTE----LSGGEQQRVAIARALANNPDVILA 177
Cdd:PRK11174 439 LRDNVllgnpdasdeQLQQAL-------ENAWVSEFLPLLPQG--LDTPIGDqaagLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-230 |
3.95e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.50 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskIRaK 95
Cdd:TIGR01193 476 INDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT---LR-Q 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQ---TF------NLIpwLTALENVEIALAISGYPFHKRKRRSRELleSVGLGDRLHHRPTELSGGEQQRVAIAR 166
Cdd:TIGR01193 549 FINYLPQepyIFsgsileNLL--LGAKENVSQDEIWAACEIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 167 ALANNPDVILADEPTGNLDSKSGDviiKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEK---KIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGK 685
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-230 |
6.75e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAeasKIRaKHVGFVFQTFNLI---- 107
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA---SLR-RNIAVVFQDAGLFnrsi 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 --------PWLTALENVEIALAISGYPFHKRKrrsrelleSVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADE 179
Cdd:PRK13657 426 ednirvgrPDATDEEMRAAAERAQAHDFIERK--------PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 180 PTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRNADRILVFDNGR 546
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
48-230 |
1.34e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.17 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 48 VMGPSGSGKTTLLNIMGILDKPTTGKVFfLGKDIskLDDAEaSKI----RAKHVGFVFQTFNLIPWLTALENVEIALAis 123
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIV-LNGRV--LFDAE-KGIclppEKRRIGYVFQDARLFPHYKVRGNLRYGMA-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 124 gypfHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQ 203
Cdd:PRK11144 103 ----KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180
....*....|....*....|....*...
gi 1491196576 204 NKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK11144 179 NIPILYVSHSLdEILRLADRVVVLEQGK 206
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-229 |
1.47e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 28 LAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRAKHVGFVFQ-TFNL 106
Cdd:PRK13643 17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 IPWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARALANNPDVILADEPTGNLD 185
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1491196576 186 SKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK13643 177 PKARIEMMQLFESIH-QSGQTVVLVTHLMdDVADYADYVYLLEKG 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-230 |
8.07e-22 |
|
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: 93.35 E-value: 8.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILDKPT-TGKVFFLGKDI--SKLDDAEASK 91
Cdd:TIGR02633 4 MKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsGVYPHGTwDGEIYWSGSPLkaSNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 92 IRAKHvgfvfQTFNLIPWLTALENV----EIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPT-ELSGGEQQRVAIAR 166
Cdd:TIGR02633 80 IVIIH-----QELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 167 ALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLnEVKAVCDTICVIRDGQ 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-230 |
9.04e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.35 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEaskIRAkHVGFVFQ---TFNLi 107
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQ-AISVVSQrvhLFSA- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 pwlTALENVEIALAisgypfHKRKRRSRELLESVGLGDRLHH------------RPteLSGGEQQRVAIARALANNPDVI 175
Cdd:PRK11160 429 ---TLRDNLLLAAP------NASDEALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHN-FEITKVaDRIIYLHDGR 230
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHA--QNKTVLMITHRlTGLEQF-DRICVMDNGQ 550
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-229 |
1.10e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.54 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISklddAEASKIRAKHVGFVFQT-FNLIP 108
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT----AENVWNLRRKIGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKS 188
Cdd:PRK13642 96 GATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1491196576 189 GDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAG 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-230 |
1.38e-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: 92.96 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLddAEASkIRAkHVGFVFQTfnlipwlTA 112
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV--TQAS-LRA-AIGIVPQD-------TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENVEIALAIsGYPfhkRKRRSRELLESVGLGDRLHH---------------RPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:COG5265 443 LFNDTIAYNI-AYG---RPDASEEEVEAAARAAQIHDfieslpdgydtrvgeRGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEiTKV-ADRIIYLHDGR 230
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVA--RGRTTLVIAHRLS-TIVdADEILVLEAGR 569
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
30-230 |
1.47e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.00 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIRaKHVGFVFQT--FNLI 107
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PWLTALENVEIALAISGY-PFHKRKRRSRELLESVGLGDRLHHR-PTELSGGEQQRVAIARALANNPDVILADEPTGNLD 185
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1491196576 186 SKSGDVIIKILKELSLEQNKTIIVVTHNFEIT-KVADRIIYLHDGR 230
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMAVVeRISHRVAVMYLGQ 541
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-230 |
2.08e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.15 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKiraKHVGFVFQT---FNLI 107
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVK---KGMAYITESrrdNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PWLTALENVEIA--LAISGYP-----FHKRKRR-----SRELLE----SVglgdrlHHRPTELSGGEQQRVAIARALANN 171
Cdd:PRK09700 354 PNFSIAQNMAISrsLKDGGYKgamglFHEVDEQrtaenQRELLAlkchSV------NQNITELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 172 PDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELpEIITVCDRIAVFCEGR 486
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-230 |
3.00e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.28 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKGRLAvkalDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLddaeASKIRAKH 96
Cdd:PRK10253 11 EQLTLGYGKYTVA----ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY----ASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 97 VGFVFQTFNLIPWLTALENVeialAISGYPFH---KRKRRSRE-----LLESVGLGDRLHHRPTELSGGEQQRVAIARAL 168
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELV----ARGRYPHQplfTRWRKEDEeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLnQACRYASHLIALREGK 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-230 |
3.20e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.11 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGE---FLvvmGPSGSGKTTLLNIM-GILDkPTTGKVFFLGKDIskldDAEASKIRaKHVGFVFQTFNLI 107
Cdd:NF033858 281 AVDHVSFRIRRGEifgFL---GSNGCGKSTTMKMLtGLLP-ASEGEAWLFGQPV----DAGDIATR-RRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PWLTALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSK 187
Cdd:NF033858 352 GELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1491196576 188 SGDVIIKILKELSLEQNKTIIVVTHnF--EitkvA---DRIIYLHDGR 230
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTH-FmnE----AercDRISLMHAGR 474
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-230 |
1.26e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.54 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVK-------------RGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaSKIRAKHVG 98
Cdd:PRK10575 13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS----SKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQTFNLIPWLTALENVeialAISGYPFH--------KRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALAN 170
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELV----AIGRYPWHgalgrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGE 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-229 |
1.35e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.54 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 1 METLAESKQKdlvyildSVTKIYGKG---RLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFL 77
Cdd:PRK15112 1 VETLLEVRNL-------SKTFRYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 78 GKDISKLDDAeaskIRAKHVGFVFQ--TFNLIPWLTALENVEIALAI-SGYPFHKRKRRSRELLESVGL-GDRLHHRPTE 153
Cdd:PRK15112 74 DHPLHFGDYS----YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 154 LSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITK-VADRIIYLHDG 229
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKhISDQVLVMHQG 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-222 |
2.17e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYgKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTT-LLNIMGILDKpTTGKVFFLGKDISKLDDAEASKir 93
Cdd:PRK10895 5 TAKNLAKAY-KGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGIVPR-DAGNIIIDDEDISLLPLHARAR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 aKHVGFVFQTFNLIPWLTALENVEIALAI-SGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNP 172
Cdd:PRK10895 78 -RGIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADR 222
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVrETLAVCER 206
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-230 |
2.47e-20 |
|
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: 85.39 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGRLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDKP--TTGKVFFLGKDIsklddAEASKIRAK 95
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKaLANRTEGNvsVEGDIHYNGIPY-----KEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANNPDVI 175
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVRG-----------------------ISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTH--NFEITKVADRIIYLHDGR 230
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGR 197
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
30-229 |
2.87e-20 |
|
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: 85.46 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILDKpTTGKVFFLGKDISKLDDAEASKIRAKHVGFVFQTfnliP 108
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQK----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WL---TALENVeialaISGYPFHKRkrRSRELLESVGL---------GDR--LHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:cd03290 89 WLlnaTVEENI-----TFGSPFNKQ--RYKAVTDACSLqpdidllpfGDQteIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIK--ILKELSlEQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQegILKFLQ-DDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-230 |
4.97e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 27 RLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaSKIRAKHVGFVFQ---- 102
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD----HHYLHRQVALVGQepvl 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 103 -----TFNLIPWLTALENVEIALA---------ISGYPfhkrkrrsrellesVGLGDRLHHRPTELSGGEQQRVAIARAL 168
Cdd:TIGR00958 567 fsgsvRENIAYGLTDTPDEEIMAAakaanahdfIMEFP--------------NGYDTEVGEKGSQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGdviiKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGS 690
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-230 |
5.98e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 20 TKIYGKGRLAVKALD-----NVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASkira 94
Cdd:PRK15439 261 QQAAGAPVLTVEDLTgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRL---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 kHVGFVF-----QTFNL-----IPWltaleNVeIALAISGYPFHKRKRRSRELLESV--GLGDRLHHRPTE---LSGGEQ 159
Cdd:PRK15439 337 -ARGLVYlpedrQSSGLyldapLAW-----NV-CALTHNRRGFWIKPARENAVLERYrrALNIKFNHAEQAartLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 160 QRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLeEIEQMADRVLVMHQGE 480
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-228 |
6.82e-20 |
|
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: 83.36 E-value: 6.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM--------GILDKPTTGKVFFLGkdisklddaeaskirakhvgfvfQTf 104
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgsGRIGMPEGEDLLFLP-----------------------QR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 105 nliPWLTA--LENVEIalaisgYPFHKrkrrsrellesvglgdrlhhrptELSGGEQQRVAIARALANNPDVILADEPTG 182
Cdd:cd03223 73 ---PYLPLgtLREQLI------YPWDD-----------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1491196576 183 NLDSKSGDVIIKILKELSLeqnkTIIVVTHNFEITKVADRIIYLHD 228
Cdd:cd03223 121 ALDEESEDRLYQLLKELGI----TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
32-230 |
9.61e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISkldDAEASKIRaKHVGFVFQTFNLIpwlt 111
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR---DYTLASLR-NQVALVSQNVHLF---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 aleNVEIALAISgypFHKRKRRSRELLESV---------------GLGDRLHHRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:PRK11176 430 ---NDTIANNIA---YARTEQYSREQIEEAarmayamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKElsLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDE--LQKNRTSLVIAHRLSTIEKADEILVVEDGE 555
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-230 |
9.82e-20 |
|
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: 87.76 E-value: 9.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAeaskIRaKHVGFVFQTFNLIPWLT 111
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA----VR-QSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDV 191
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 192 IIKILkeLSLEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMdEADLLGDRIAIISQGR 1137
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
33-229 |
2.07e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.47 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMG-ILDKPTTGKVFFLGKDISklddaeaskirakhvgfvfQTFNLIPWL 110
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGaLKGTPVAGCVDVPDNQFG-------------------REASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TALENVEIALaisgypfhkrkrrsrELLESVGLGDR--LHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKS 188
Cdd:COG2401 107 GRKGDFKDAV---------------ELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1491196576 189 GDVIIKILKELSLEQNKTIIVVTHNFEITKV--ADRIIYLHDG 229
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVATHHYDVIDDlqPDLLIFVGYG 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-212 |
3.34e-19 |
|
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: 85.76 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 13 VYILDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFfLGKDISklddaeaski 92
Cdd:TIGR03719 4 IYTMNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-PQPGIK---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 93 rakhVGFVFQTFNLIPWLTALENVEIALA-----------IS---GYP------FHKRKRRSRELLESVGLGD------- 145
Cdd:TIGR03719 70 ----VGYLPQEPQLDPTKTVRENVEEGVAeikdaldrfneISakyAEPdadfdkLAAEQAELQEIIDAADAWDldsqlei 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 146 -----RLhhrP------TELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSleqnKTIIVVTH 212
Cdd:TIGR03719 146 amdalRC---PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP----GTVVAVTH 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
33-212 |
1.01e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.00 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIR-AKHVGFVFQTfnlipwLT 111
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLyLGHAPGIKTT------LS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIAlaisgYPFHKRKrRSRELLESVGLGDrLHHRPT-ELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGD 190
Cdd:cd03231 90 VLENLRFW-----HADHSDE-QVEEALARVGLNG-FEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|..
gi 1491196576 191 VIIKILKElSLEQNKTIIVVTH 212
Cdd:cd03231 163 RFAEAMAG-HCARGGMVVLTTH 183
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-214 |
1.06e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.62 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRlavKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKlddaeasKIR 93
Cdd:PRK15056 8 VVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKaLMGFV-RLASGKISILGQPTRQ-------ALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 AKHVGFVFQTFNL---IPWLtalenVEIALAISGY--------PFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRV 162
Cdd:PRK15056 77 KNLVAYVPQSEEVdwsFPVL-----VEDVVMMGRYghmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 163 AIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF 214
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR-DEGKTMLVSTHNL 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-230 |
7.53e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDKPTTGKVFFLGK--DISKLDDAEASKI------RAKHvgfv 100
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKpvKIRNPQQAIAQGIamvpedRKRD---- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 101 fqtfNLIPWLTALENVEIAlAISGYPFHKRKRRSREL---LESVglgDRLHHRP-------TELSGGEQQRVAIARALAN 170
Cdd:PRK13549 351 ----GIVPVMGVGKNITLA-ALDRFTGGSRIDDAAELktiLESI---QRLKVKTaspelaiARLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 171 NPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELpEVLGLSDRVLVMHEGK 482
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-230 |
1.05e-17 |
|
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: 81.41 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDKPTTGKVFFLGK--DISKLDDAEASKI------RAKHvgfv 100
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKpvDIRNPAQAIRAGIamvpedRKRH---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 101 fqtfNLIPWLTALENVEIAlAISGYPFHKRKRRSRELlESVGLG-DRLHHRP-------TELSGGEQQRVAIARALANNP 172
Cdd:TIGR02633 349 ----GIVPILGVGKNITLS-VLKSFCFKMRIDAAAEL-QIIGSAiQRLKVKTaspflpiGRLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-230 |
1.66e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.93 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 30 VKALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDKpTTGKVFFLGKDISKLDDAEASKiraKHVGFVFQTFNLIP 108
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKcLFGIYQK-DSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WLTALENveiaLAISGYPFH-------KRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPT 181
Cdd:PRK10982 87 QRSVMDN----MWLGRYPTKgmfvdqdKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491196576 182 GNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLK-ERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-230 |
3.31e-17 |
|
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: 77.53 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKDISKLDdaeASKIRaKHVGFVFQT------- 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVE-LSSGSILIDGVDISKIG---LHDLR-SRISIIPQDpvlfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 --FNLIP---------WLtALENVEIALAISGYPFhkrkrrsrellesvGLGDRLHHRPTELSGGEQQRVAIARALANNP 172
Cdd:cd03244 94 irSNLDPfgeysdeelWQ-ALERVGLKEFVESLPG--------------GLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKE-LSleqNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREaFK---DCTVLTIAHRLDTIIDSDRILVLDKGR 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-224 |
3.70e-17 |
|
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: 79.83 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 17 DSVTKIYGKGRLAVKAldnvsFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFlGKDIS-KlddaeASKIRAK 95
Cdd:COG1245 345 PDLTKSYGGFSLEVEG-----GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKISyK-----PQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQtfnlipwltALENVeIALAISGYPFHKrkrrsrELLESVGLgDRLHHRP-TELSGGEQQRVAIARALANNPDV 174
Cdd:COG1245 414 YDGTVEE---------FLRSA-NTDDFGSSYYKT------EIIKPLGL-EKLLDKNvKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRII 224
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYlIDYISDRLM 527
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-212 |
3.76e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.78 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 13 VYILDSVTKIYGKGRlavKALDNVSFT----VKRGeflvVMGPSGSGKTTLLNIMGILDKPTTGKVfFLGKDISklddae 88
Cdd:PRK11819 6 IYTMNRVSKVVPPKK---QILKDISLSffpgAKIG----VLGLNGAGKSTLLRIMAGVDKEFEGEA-RPAPGIK------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 89 askirakhVGFVFQTFNLIPWLTALENVEIALAisgypfHKRKRRSR----------------ELLESVG-LGDRLHHR- 150
Cdd:PRK11819 72 --------VGYLPQEPQLDPEKTVRENVEEGVA------EVKAALDRfneiyaayaepdadfdALAAEQGeLQEIIDAAd 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 151 -----------------P------TELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSleqnKTI 207
Cdd:PRK11819 138 awdldsqleiamdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYP----GTV 213
|
....*
gi 1491196576 208 IVVTH 212
Cdd:PRK11819 214 VAVTH 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
33-229 |
5.22e-17 |
|
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: 79.95 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDkPTTGKVFFLGKdisklddaeaskirakhVGFVFQTfnliPWL- 110
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELE-PSEGKIKHSGR-----------------ISFSPQT----SWIm 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 --TALENVEIALAISGYpfhkrkrRSRELLESVGLGDRLHHRPTE-----------LSGGEQQRVAIARALANNPDVILA 177
Cdd:TIGR01271 500 pgTIKDNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 178 DEPTGNLDSKSGDVIIK--ILKELSleqNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEscLCKLMS---NKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
10-229 |
1.29e-16 |
|
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: 74.97 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 10 KDLVYILDSVTkiyGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGilDKPTTGKVfflGKDISkLDDAEA 89
Cdd:cd03232 7 KNLNYTVPVKG---GKRQL----LNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVI---TGEIL-INGRPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 90 SKIRAKHVGFVFQTFNLIPWLTALENVEIALAISGypfhkrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALA 169
Cdd:cd03232 74 DKNFQRSTGYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 170 NNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTH--NFEITKVADRIIYLHDG 229
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLA-DSGQAILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-229 |
1.40e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 18 SVTKIYGkgrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIrakHV 97
Cdd:PRK15439 16 SISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---GI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 98 GFVFQTFNLIPWLTALENVEIALAISgypfHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:PRK15439 89 YLVPQEPLLFPNLSVKENILFGLPKR----QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLpEIRQLADRISVMRDG 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-230 |
2.35e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 24 GKGRLAVKAL-----DNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILDKpTTGKVFFLGKDISKLDDAEA-------- 89
Cdd:PRK10762 254 GEVRLKVDNLsgpgvNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPQDGlangivyi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 90 SKIRaKHVGFVFQtfnlipwLTALENVEI-ALAIsgypFHKRKRRSRELLESVGLGD--RLHHRPT--------ELSGGE 158
Cdd:PRK10762 333 SEDR-KRDGLVLG-------MSVKENMSLtALRY----FSRAGGSLKHADEQQAVSDfiRLFNIKTpsmeqaigLLSGGN 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 159 QQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK10762 401 QQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-224 |
2.72e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.54 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 18 SVTKIYGKGRLAVKAldnvsFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVFFlGKDIS-KlddaeASKIRAK 95
Cdd:PRK13409 345 DLTKKLGDFSLEVEG-----GEIYEGEVIGIVGPNGIGKTTFAKLLaGVL-KPDEGEVDP-ELKISyK-----PQYIKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTfnlipwltaLENVEIALAISGYpfhkrkrrSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVI 175
Cdd:PRK13409 413 YDGTVEDL---------LRSITDDLGSSYY--------KSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491196576 176 LADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFE-ITKVADRII 224
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYmIDYISDRLM 525
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
33-229 |
3.29e-16 |
|
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: 75.66 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILDkPTTGKVFFLGKdisklddaeaskirakhVGFVFQTFNLIPWlT 111
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELE-PSEGKIKHSGR-----------------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYpfhkrkrRSRELLESVGLGDRLHHRPTE-----------LSGGEQQRVAIARALANNPDVILADEP 180
Cdd:cd03291 114 IKENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 181 TGNLDSKSGDVIIK--ILKelsLEQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:cd03291 187 FGYLDVFTEKEIFEscVCK---LMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-230 |
3.75e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMG--ILDKPTTGKVFflgkdiskLDDAEASKIRAKHVGFVFQTFNLIPWL 110
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAgrIQGNNFTGTIL--------ANNRKPTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TALENVeIALAISGYPFHKRKRRSRELLESV----GL--------GDRLHHrptELSGGEQQRVAIARALANNPDVILAD 178
Cdd:PLN03211 156 TVRETL-VFCSLLRLPKSLTKQEKILVAESViselGLtkcentiiGNSFIR---GISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTH--NFEITKVADRIIYLHDGR 230
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHqpSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-230 |
3.85e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAvkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFLGKDISKLDDaeaSKIRa 94
Cdd:PRK10790 343 IDNVSFAYRDDNLV---LQNINLSVPSRGFVALVGHTGSGKSTLASlLMGYY-PLTEGEIRLDGRPLSSLSH---SVLR- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KHVGFVFQTfnliPWLTA---LENVEIALAISgypfhkrKRRSRELLESV-------GLGDRLHHRPTE----LSGGEQQ 160
Cdd:PRK10790 415 QGVAMVQQD----PVVLAdtfLANVTLGRDIS-------EEQVWQALETVqlaelarSLPDGLYTPLGEqgnnLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 161 RVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKElsLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA--VREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-185 |
5.78e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.73 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 27 RLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeaskiRAKHVGFVFQTFNL 106
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 107 IPWLTALENVEIALAISGYpfhKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLD 185
Cdd:PRK13543 94 KADLSTLENLHFLCGLHGR---RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-213 |
7.60e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVfflgkdisklddAEASKIRak 95
Cdd:PRK09544 7 LENVSVSFGQRRV----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 hVGFVFQTFNLIPWLtalenveiALAISGYPFHKRKRRSREL---LESVGLGDRLHHRPTELSGGEQQRVAIARALANNP 172
Cdd:PRK09544 69 -IGYVPQKLYLDTTL--------PLTVNRFLRLRPGTKKEDIlpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHN 213
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-230 |
1.83e-15 |
|
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: 75.37 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILDKpTTGKVFFLGKdisklddaeaskirakhVGFVFQTfnliPWL- 110
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-----------------VAYVPQQ----AWIq 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 --TALENVeialaISGYPFHKRkrRSRELLESVGL---------GDR--LHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:TIGR00957 712 ndSLRENI-----LFGKALNEK--YYQQVLEACALlpdleilpsGDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 178 DEPTGNLDSKSGDVII-KILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-230 |
7.76e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 23 YGKGRLAVKALDN------VSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEAskIRA-- 94
Cdd:PRK11288 253 LGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDA--IRAgi 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 -------KHVGFVfqtfnlipwltALENVEIALAISGYPFHKR------KRRSREL----LESVGLGDRLHHRPT-ELSG 156
Cdd:PRK11288 331 mlcpedrKAEGII-----------PVHSVADNINISARRHHLRagclinNRWEAENadrfIRSLNIKTPSREQLImNLSG 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 157 GEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLpEVLGVADRIVVMREGR 473
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-230 |
2.21e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.93 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGRLAVKALDnvsFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISklddaeASKIRA- 94
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT------AEQPEDy 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 -KHVGFVFQTFNLIPWLTALENVEIALAIsgypfhkrkrrSRELLESVGLGDRLHHRP-----TELSGGEQQRVAIARAL 168
Cdd:PRK10522 396 rKLFSAVFTDFHLFDQLLGPEGKPANPAL-----------VEKWLERLKMAHKLELEDgrisnLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-230 |
2.67e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 70.23 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGkvfflgkDISKLDDAEASKIRAkhvgfvfqtfNLIPWLT 111
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-------KVDRNGEVSVIAISA----------GLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDV 191
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 192 IIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:PRK13546 182 CLDKIYEFK-EQNKTIFFVSHNLgQVRQFCTKIAWIEGGK 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-229 |
3.94e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.31 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMgildkpttgkvffLGkDISKLDDAEASkIRAKhVGFVFQtfnlIPWL-- 110
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAM-------------LG-ELPPRSDASVV-IRGT-VAYVPQ----VSWIfn 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 -TALENVeialaISGYPF----HKRKRRSREL---LESVGLGD--RLHHRPTELSGGEQQRVAIARALANNPDVILADEP 180
Cdd:PLN03130 693 aTVRDNI-----LFGSPFdperYERAIDVTALqhdLDLLPGGDltEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1491196576 181 TGNLDSKSG-DVIIKILK-ELsleQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:PLN03130 768 LSALDAHVGrQVFDKCIKdEL---RGKTRVLVTNQLHFLSQVDRIILVHEG 815
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
31-230 |
4.44e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 68.59 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDdaeASKIRAKhvgfvfqtFNLIPWL 110
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSS--------LTIIPQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TALENVEIALAISgyPF-HKRKRRSRELLESVGLGDrlhhrptELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSG 189
Cdd:cd03369 91 PTLFSGTIRSNLD--PFdEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1491196576 190 DVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03369 162 ALIQKTIREEF--TNSTILTIAHRLRTIIDYDKILVMDAGE 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-212 |
8.82e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 8.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKldDAEASKiraKHVGFVFQTFNLIPWLTA 112
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--DLCTYQ---KQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENVEIALAISGYPFHkrkrrSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVI 192
Cdd:PRK13540 92 RENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|
gi 1491196576 193 IKILKElSLEQNKTIIVVTH 212
Cdd:PRK13540 167 ITKIQE-HRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
48-230 |
1.48e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.11 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 48 VMGPSGSGKTTL-LNIMGILdKPTTGKVFFLGKdisKLDDAEASKIRAKH-VGFVFQTFNLIPWLTALENvEIALAIS-- 123
Cdd:PRK13638 32 LVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGK---PLDYSKRGLLALRQqVATVFQDPEQQIFYTDIDS-DIAFSLRnl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 124 GYPFHKRKRRSRELLESVGlGDRLHHRPTE-LSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELsLE 202
Cdd:PRK13638 107 GVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRI-VA 184
|
170 180
....*....|....*....|....*....
gi 1491196576 203 QNKTIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK13638 185 QGNHVIISSHDIDlIYEISDAVYVLRQGQ 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
39-212 |
1.75e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 39 TVKRGEFLVVMGPSGSGKTTLLNIM-GIL--------DKPTTGKV--FFLGKDI----SKLDDaeaSKIRAKHVgfvFQT 103
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsGELipnlgdyeEEPSWDEVlkRFRGTELqnyfKKLYN---GEIKVVHK---PQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 FNLIPWLT------ALENVEialaisgypfhKRKRRsRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILA 177
Cdd:PRK13409 169 VDLIPKVFkgkvreLLKKVD-----------ERGKL-DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTH 212
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELA--EGKYVLVVEH 269
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
154-228 |
2.81e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 2.81e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 154 LSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHD 228
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
16-181 |
3.71e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKgrlaVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISkldDAEASKIRAK 95
Cdd:NF033858 4 LEGVSHRYGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFVFQTF--NLIPWLTALENVEialaisgypFH---------KRKRRSRELLESVGLgDRLHHRPT-ELSGGEQQRVA 163
Cdd:NF033858 77 RIAYMPQGLgkNLYPTLSVFENLD---------FFgrlfgqdaaERRRRIDELLRATGL-APFADRPAgKLSGGMKQKLG 146
|
170
....*....|....*...
gi 1491196576 164 IARALANNPDVILADEPT 181
Cdd:NF033858 147 LCCALIHDPDLLILDEPT 164
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-228 |
3.87e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 27 RLAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFlgKDISKLDDAEASKIRAKhVGFVFQ---- 102
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSK-IGVVSQdpll 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 103 ----TFNLIPW----LTALENVEIALAISGYPFHKRKRR--------------------SRELLE--------------- 139
Cdd:PTZ00265 472 fsnsIKNNIKYslysLKDLEALSNYYNEDGNDSQENKNKrnscrakcagdlndmsnttdSNELIEmrknyqtikdsevvd 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 140 ---SVGLGDRLHHRP-----------TELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNK 205
Cdd:PTZ00265 552 vskKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
250 260
....*....|....*....|...
gi 1491196576 206 TIIVVTHNFEITKVADRIIYLHD 228
Cdd:PTZ00265 632 ITIIIAHRLSTIRYANTIFVLSN 654
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
20-224 |
4.47e-13 |
|
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: 65.29 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 20 TKIYGKGRLAVKALDnvsftVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKvfflgkdisklddaeaskirakhvgf 99
Cdd:cd03222 7 VKRYGVFFLLVELGV-----VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN-------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 100 vfqtfnlipwlTALENVEIAlaisgypfhkrkrrsrellesvglgdrlhHRP--TELSGGEQQRVAIARALANNPDVILA 177
Cdd:cd03222 56 -----------DEWDGITPV-----------------------------YKPqyIDLSGGELQRVAIAAALLRNATFYLF 95
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF-EITKVADRII 224
Cdd:cd03222 96 DEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLaVLDYLSDRIH 143
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-230 |
9.81e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMgildkpttgkvfflgkdISKLDDAEASKIRAKHVGFVFQTfnliPWL-- 110
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSL-----------------LSQFEISEGRVWAERSIAYVPQQ----AWImn 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 -TALENVEIALAISGYPFHKRKRRSRelLE------SVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGN 183
Cdd:PTZ00243 735 aTVRGNILFFDEEDAARLADAVRVSQ--LEadlaqlGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1491196576 184 LDSKSGDVIIK--ILKELSleqNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PTZ00243 813 LDAHVGERVVEecFLGALA---GKTRVLATHQVHVVPRADYVVALGDGR 858
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
33-224 |
1.28e-12 |
|
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: 64.97 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLL---------------------NIMGILDKPTTGKVFFLGKDISkLDDAEASK 91
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIA-IDQKTTSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 92 IRAKHVGFVFQTFNLIPWLTALENVeialaisgypfhkrKRRSRELLEsVGLGD-RLHHRPTELSGGEQQRVAIARALAN 170
Cdd:cd03270 90 NPRSTVGTVTEIYDYLRLLFARVGI--------------RERLGFLVD-VGLGYlTLSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 171 NPDVIL--ADEPTGNLDSKSGDVIIKILKELSLEQNkTIIVVTHNFEITKVADRII 224
Cdd:cd03270 155 GLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVI 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-230 |
1.29e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 66.66 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLD-DAEASKIrakhvGFVFQTfnliPWL 110
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRL-----AVVSQT----PFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 ---TALENveIALAisgypfhkRKRRSRELLESVGLGDRLH---------------HRPTELSGGEQQRVAIARALANNP 172
Cdd:PRK10789 401 fsdTVANN--IALG--------RPDATQQEIEHVARLASVHddilrlpqgydtevgERGVMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 173 DVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWG--EGRTVIISAHRLSALTEASEILVMQHGH 526
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-229 |
1.89e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMG---ILD--------------------KPTTGKVF-FLGKDISKLddae 88
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDdgriiyeqdlivarlqqdppRNVEGTVYdFVAEGIEEQ---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 89 ASKIRAKHvgfvfQTFNLIPW------LTALENVEIALAIS-GYPFHKRkrrSRELLESVGLGDrlHHRPTELSGGEQQR 161
Cdd:PRK11147 95 AEYLKRYH-----DISHLVETdpseknLNELAKLQEQLDHHnLWQLENR---INEVLAQLGLDP--DAALSSLSGGWLRK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 162 VAIARALANNPDVILADEPTGNLDSKSgdviIKILKELSLEQNKTIIVVTHN--FeITKVADRIIYLHDG 229
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDrsF-IRNMATRIVDLDRG 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-229 |
3.39e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGilDKPTTGkVFFLGKDIS---KLDDAEASKIrakhvGFVFQTFNLIPW 109
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTG-VITGGDRLVngrPLDSSFQRSI-----GYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 110 LTALEnveiALAISGY---PFH---KRKRRSRE----LLESVGLGDRLHHRPTE-LSGGEQQRVAIARALANNPDVIL-A 177
Cdd:TIGR00956 851 STVRE----SLRFSAYlrqPKSvskSEKMEYVEevikLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 178 DEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITKVA--DRIIYLHDG 229
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
33-230 |
4.64e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILDKP-------TTGKVFFLGKDISKLDDAEASKIRA-----KHVGF 99
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAvlpqaAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 100 VFQTfnlipwltalenVEIALaISGYPFHKR----KRRSREL----LESVGLGDRLHHRPTELSGGEQQRVAIARALAN- 170
Cdd:PRK13547 97 AFSA------------REIVL-LGRYPHARRagalTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 171 --------NPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEI-TKVADRIIYLHDGR 230
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRIAMLADGA 232
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
28-224 |
4.74e-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: 62.34 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 28 LAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNimgildkpTTGKVFFLGKDISKLDDAEASKIRakhvgFVFQTFNLI 107
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGLYASGKARLISFLPKFSRNKLI-----FIDQLQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 pwltalenveialaisgypfhkrkrrsrelleSVGLGDRLHHRPTE-LSGGEQQRVAIARALANNPD--VILADEPTGNL 184
Cdd:cd03238 73 --------------------------------DVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 185 DSKSGDVIIKILKELsLEQNKTIIVVTHNFEITKVADRII 224
Cdd:cd03238 121 HQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWII 159
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
32-229 |
4.88e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.91 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVfflgkDISklddAEASKIrAKHVGFVFQtfnlipwLT 111
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIK----GSAALI-AISSGLNGQ-------LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIALAISGYPFHKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDV 191
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1491196576 192 IIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDG 229
Cdd:PRK13545 182 CLDKMNEFK-EQGKTIFFISHSLsQVKSFCTKALWLHYG 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-212 |
5.03e-12 |
|
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: 64.81 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 39 TVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKV-----------FFLGKDI----SKLDDAEaskIRAKHVGfvfQ 102
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILsGEL-KPNLGDYdeepswdevlkRFRGTELqdyfKKLANGE---IKVAHKP---Q 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 103 TFNLIPWL------TALENVEialaisgypfhkRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVIL 176
Cdd:COG1245 168 YVDLIPKVfkgtvrELLEKVD------------ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 1491196576 177 ADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTH 212
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELA-EEGKYVLVVEH 270
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-230 |
3.38e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLnimgildKPTTGKV--FFLGKD----ISKLDDAEASKIRAKHVGFVFQTFNL 106
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLL-------KTIASNTdgFHIGVEgvitYDGITPEEIKKHYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 IPWLTALENVEIALAISGyPFHKRKRRSRE---------LLESVGLGdrlHHRPTE--------LSGGEQQRVAIARALA 169
Cdd:TIGR00956 150 FPHLTVGETLDFAARCKT-PQNRPDGVSREeyakhiadvYMATYGLS---HTRNTKvgndfvrgVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 170 NNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNF--EITKVADRIIYLHDGR 230
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsqDAYELFDKVIVLYEGY 288
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-215 |
3.48e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 16 LDSVTKIYGKGrlAVKALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDI-SKLDDAEASkira 94
Cdd:TIGR01257 1940 LNELTKVYSGT--SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQN---- 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 khVGFVFQTFNLIPWLTALENVEIALAISGYPFHKRKRRSRELLESVGL---GDRLhhrPTELSGGEQQRVAIARALANN 171
Cdd:TIGR01257 2014 --MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLslyADRL---AGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1491196576 172 PDVILADEPTGNLDSKSG----DVIIKILKElsleqNKTIIVVTHNFE 215
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARrmlwNTIVSIIRE-----GRAVVLTSHSME 2131
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-185 |
4.62e-11 |
|
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: 61.87 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 11 DLVYILDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVfFLGKDIsklddaeas 90
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLL----IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-EIGETV--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 91 kirakHVGFVFQTF-NLIPWLTALEnveialAISGYPFH----KRKRRSRELLESVGL-GDRLHHRPTELSGGEQQRVAI 164
Cdd:TIGR03719 386 -----KLAYVDQSRdALDPNKTVWE------EISGGLDIiklgKREIPSRAYVGRFNFkGSDQQKKVGQLSGGERNRVHL 454
|
170 180
....*....|....*....|.
gi 1491196576 165 ARALANNPDVILADEPTGNLD 185
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLD 475
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
33-212 |
9.74e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNImgILDKP----TTGKVFFLGKDISKLDDAEASkirakHVGfVFQTFNL-- 106
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPaykiLEGDILFKGESILDLEPEERA-----HLG-IFLAFQYpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 107 -IPWLTALENVEIALaisgypfhKRKRRSREL---------------LESVGLGDRLHHRPTE--LSGGEQQRVAIARAL 168
Cdd:CHL00131 95 eIPGVSNADFLRLAY--------NSKRKFQGLpeldplefleiinekLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1491196576 169 ANNPDVILADEPTGNLDsksgdviIKILKELS------LEQNKTIIVVTH 212
Cdd:CHL00131 167 LLDSELAILDETDSGLD-------IDALKIIAeginklMTSENSIILITH 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-212 |
1.21e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM-GILdKPTTGKVfflgKDISKLDDAEASKIRAkhvgfvfqtfNLIPWLT 111
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMlGQL-QADSGRI----HCGTKLEVAYFDQHRA----------ELDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENV-----EIalAISGypfhkrkrRSRELLESvgLGDRLHH-----RPTE-LSGGEQQRVAIARALANNPDVILADEP 180
Cdd:PRK11147 400 VMDNLaegkqEV--MVNG--------RPRHVLGY--LQDFLFHpkramTPVKaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
170 180 190
....*....|....*....|....*....|..
gi 1491196576 181 TGNLDSKSgdviIKILKELSLEQNKTIIVVTH 212
Cdd:PRK11147 468 TNDLDVET----LELLEELLDSYQGTVLLVSH 495
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-216 |
2.25e-10 |
|
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: 58.92 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRLAVKALDnvsfTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKV-----------FFLGKDI-- 81
Cdd:cd03236 2 LEDEPVHRYGPNSFKLHRLP----VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELqn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 82 --SKLDDAEASKIRAKhvgfvfQTFNLIPWL---TALENVEIAlaisgypfHKRKRRSrELLESVGLGDRLHHRPTELSG 156
Cdd:cd03236 78 yfTKLLEGDVKVIVKP------QYVDLIPKAvkgKVGELLKKK--------DERGKLD-ELVDQLELRHVLDRNIDQLSG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 157 GEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEI 216
Cdd:cd03236 143 GELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELA-EDDNYVLVVEHDLAV 201
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-227 |
2.92e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 37 SFTVKRGEFLVVMGPSGSGKTTLLNIMG---ILDKPTTGKVF-----FLGKDISKLD-----DAEASKIRAKHVGFVFQT 103
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaIDGIPKNCQILhveqeVVGDDTTALQcvlntDIERTQLLEEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 FNL-IPWLTALENVEIALAISGYPFHKR-----KR-----------RSRELLESVGLGDRLHHRPTE-LSGGEQQRVAIA 165
Cdd:PLN03073 277 RELeFETETGKGKGANKDGVDKDAVSQRleeiyKRlelidaytaeaRAASILAGLSFTPEMQVKATKtFSGGWRMRIALA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491196576 166 RALANNPDVILADEPTGNLDSKSgdviIKILKELSLEQNKTIIVVTH--NFEITKVADrIIYLH 227
Cdd:PLN03073 357 RALFIEPDLLLLDEPTNHLDLHA----VLWLETYLLKWPKTFIVVSHarEFLNTVVTD-ILHLH 415
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
33-226 |
4.01e-10 |
|
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: 58.39 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN----------IMGILDKPTTGKVFFLGKDISKLDDAEASKI----R---AK 95
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarrLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPIgrtpRsnpAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 96 HVGFvfqtFNLIPWL------------TALE------------NVEIALAISGYPFHKRKRRSRELLESVGLGD-RLHHR 150
Cdd:cd03271 91 YTGV----FDEIRELfcevckgkrynrETLEvrykgksiadvlDMTVEEALEFFENIPKIARKLQTLCDVGLGYiKLGQP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491196576 151 PTELSGGEQQRVAIARAL---ANNPDVILADEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTHNFEITKVADRIIYL 226
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHNLDVIKCADWIIDL 244
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-226 |
4.76e-10 |
|
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: 59.26 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 132 RRSRELLESVGLGD-RLHHRPTELSGGEQQRVAIARAL---ANNPDVILADEPTGNLDSksgDVIIKILKELS--LEQNK 205
Cdd:TIGR00630 807 SRKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHF---DDIKKLLEVLQrlVDKGN 883
|
90 100
....*....|....*....|.
gi 1491196576 206 TIIVVTHNFEITKVADRIIYL 226
Cdd:TIGR00630 884 TVVVIEHNLDVIKTADYIIDL 904
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-224 |
5.94e-10 |
|
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: 56.21 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 21 KIYGKGRLAVKALDNVSFTvkRGEFLVVMGPSGSGKTTLLNIMGildkpttgkvFFLGKDISKLDDAEASKIRakhvGFV 100
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDAIG----------LALGGAQSATRRRSGVKAG----CIV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 101 fqtfnlipwltALENVEIALAISGypfhkrkrrsrellesvglgdrlhhrpteLSGGEQQRVAIARALANN-----PDVI 175
Cdd:cd03227 65 -----------AAVSAELIFTRLQ-----------------------------LSGGEKELSALALILALAslkprPLYI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1491196576 176 LaDEPTGNLDSKSGDVIIKILKELSLEQNkTIIVVTHNFEITKVADRII 224
Cdd:cd03227 105 L-DEIDRGLDPRDGQALAEAILEHLVKGA-QVIVITHLPELAELADKLI 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
31-230 |
9.67e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLlnIMGILDKP----TTGKVFFLGK--DISKLDDAEASKI------RaKHVG 98
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMSVFGRSygrnISGTVFKDGKevDVSTVSDAIDAGLayvtedR-KGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FvfqtfNLIP------WLTAL----------ENVEIALAiSGYpfhkRKR---RSRELLESVGlgdrlhhrptELSGGEQ 159
Cdd:NF040905 351 L-----NLIDdikrniTLANLgkvsrrgvidENEEIKVA-EEY----RKKmniKTPSVFQKVG----------NLSGGNQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 160 QRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNF-EITKVADRIIYLHDGR 230
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELpELLGMCDRIYVMNEGR 481
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
133-212 |
1.82e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 133 RSRELLESVGLGDRLHHRP-TELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSgdviIKILKELSLEQNKTIIVVT 211
Cdd:PRK15064 134 RAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIIS 209
|
.
gi 1491196576 212 H 212
Cdd:PRK15064 210 H 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-230 |
3.58e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 15 ILDSVTKIYGKGRLavkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGILdKPTTGKVFFlgkdisklddAEASKIr 93
Cdd:PRK15064 321 EVENLTKGFDNGPL----FKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGEL-EPDSGTVKW----------SENANI- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 94 akhvGFVFQ--------TFNLIPWltalenveialaISGYpfhkRKRRSRELLESVGLG------DRLHHRPTELSGGEQ 159
Cdd:PRK15064 385 ----GYYAQdhaydfenDLTLFDW------------MSQW----RQEGDDEQAVRGTLGrllfsqDDIKKSVKVLSGGEK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 160 QRVAIARALANNPDVILADEPTGNLDSKSgdviIKILkELSLEQNK-TIIVVTHNFE-ITKVADRIIYLHDGR 230
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMES----IESL-NMALEKYEgTLIFVSHDREfVSSLATRIIEITPDG 512
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-229 |
3.60e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMgildkpttgkvfflgkdISKLDDAEASKIRAK-HVGFVFQtfnlIPWL- 110
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-----------------LGELSHAETSSVVIRgSVAYVPQ----VSWIf 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 --TALENVeialaISGYPFHKRK----------RRSRELLESVGLGDrLHHRPTELSGGEQQRVAIARALANNPDVILAD 178
Cdd:PLN03232 692 naTVRENI-----LFGSDFESERywraidvtalQHDLDLLPGRDLTE-IGERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 179 EPTGNLDSKSGDVIIK--ILKELsleQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:PLN03232 766 DPLSALDAHVAHQVFDscMKDEL---KGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
154-224 |
4.53e-09 |
|
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: 54.54 E-value: 4.53e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491196576 154 LSGGEQQ------RVAIARALANNPDVILADEPTGNLDSKSGD-VIIKILKELSLEQNKTIIVVTHNFEITKVADRII 224
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-230 |
5.05e-09 |
|
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: 53.53 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 42 RGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDisklddaeaskirakhvgfvfqtfnlipwltalenveiala 121
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 122 isgypfhkrkrRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKI-----L 196
Cdd:smart00382 40 -----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 197 KELSLEQNKTIIVVTHNFEITK------VADRIIYLHDGR 230
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGpallrrRFDRRIVLLLIL 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-185 |
8.43e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGilDKPT--TGKVFFLGK---------DISKlddaeaskirakHVGFV 100
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSlITG--DHPQgySNDLTLFGRrrgsgetiwDIKK------------HIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 101 FQTFNLIPWL-TALENVeialAISGYpF----------HKRKRRSRELLESVGLGDRLHHRP-TELSGGEQQRVAIARAL 168
Cdd:PRK10938 342 SSSLHLDYRVsTSVRNV----ILSGF-FdsigiyqavsDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRAL 416
|
170
....*....|....*..
gi 1491196576 169 ANNPDVILADEPTGNLD 185
Cdd:PRK10938 417 VKHPTLLILDEPLQGLD 433
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-230 |
1.29e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISK--LDDAEA--SKIRAKHVGFVFQT-FNLI 107
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTDLRRvlSIIPQSPVLFSGTVrFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 P---------WlTALENVEIALAISGYPFhkrkrrsrellesvGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILAD 178
Cdd:PLN03232 1332 PfsehndadlW-EALERAHIKDVIDRNPF--------------GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEF--KSCTMLVIAHRLNTIIDCDKILVLSSGQ 1446
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
36-230 |
2.29e-08 |
|
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: 54.03 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 36 VSFTVKRGE--FLVvmGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlDDAEA--SKIRAkhvgfVFQTFNLIPWLT 111
Cdd:COG4615 351 IDLTIRRGElvFIV--GGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA-DNREAyrQLFSA-----VFSDFHLFDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 112 ALENVEIAlaisgypfhkrkRRSRELLESVGLGDRLHHR-----PTELSGGEQQRVAIARALANNPDVILADE------P 180
Cdd:COG4615 423 GLDGEADP------------ARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 181 -------TgnldsksgdviiKILKELSlEQNKTIIVVTHN---FEitkVADRIIYLHDGR 230
Cdd:COG4615 491 efrrvfyT------------ELLPELK-ARGKTVIAISHDdryFD---LADRVLKMDYGK 534
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-224 |
3.01e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 53.88 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 132 RRSRELLESVGLGD-RLHHRPTELSGGEQQRVAIARALA---NNPDVILADEPTgnldskSG----DV--IIKILKELsL 201
Cdd:COG0178 804 ARKLQTLQDVGLGYiKLGQPATTLSGGEAQRVKLASELSkrsTGKTLYILDEPT------TGlhfhDIrkLLEVLHRL-V 876
|
90 100
....*....|....*....|...
gi 1491196576 202 EQNKTIIVVTHNFEITKVADRII 224
Cdd:COG0178 877 DKGNTVVVIEHNLDVIKTADWII 899
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-230 |
3.64e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 35 NVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFflgkdisklddaEASKIRAKhvgfVFQTFNLIPW-LTAL 113
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF------------RSAKVRMA----VFSQHHVDGLdLSSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 114 ENVEIALAISGYPfhkrKRRSRELLESVGLGDRLHHRPT-ELSGGEQQRVAIARALANNPDVILADEPTGNLDSksgDVI 192
Cdd:PLN03073 591 PLLYMMRCFPGVP----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL---DAV 663
|
170 180 190
....*....|....*....|....*....|....*...
gi 1491196576 193 IKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PLN03073 664 EALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
32-230 |
4.40e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 32 ALDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILDKpTTGKVFFLGKDISKLDDAEASKirakhVGFVFQT------- 103
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVeTLFGIREK-SAGTITLHGKKINNHNANEAIN-----HGFALVTeerrstg 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 --FNL-IPWLTALENVEIALAISGYPFHKR-KRRSRELLESVGLGDRLHHRPT-ELSGGEQQRVAIARALANNPDVILAD 178
Cdd:PRK10982 337 iyAYLdIGFNSLISNIRNYKNKVGLLDNSRmKSDTQWVIDSMRVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1491196576 179 EPTGNLDSKSGDVIIKILKELSLEQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-226 |
4.77e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 150 RP-TELSGGEQQRVAIARALAN---NPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITKVADRIIY 225
Cdd:PRK00635 805 RPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLT-HQGHTVVIIEHNMHVVKVADYVLE 883
|
.
gi 1491196576 226 L 226
Cdd:PRK00635 884 L 884
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-230 |
1.13e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKLDDAEASKIrakhVGFVFQT--------- 103
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV----LGIIPQApvlfsgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 104 FNLIP---------WlTALENVEIALAIsgypfhkrkRRSrelleSVGLGDRLHHRPTELSGGEQQRVAIARALANNPDV 174
Cdd:PLN03130 1331 FNLDPfnehndadlW-ESLERAHLKDVI---------RRN-----SLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 175 ILADEPTGNLDSKSGDVIIKILKElslE-QNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIRE---EfKSCTMLIIAHRLNTIIDCDRILVLDAGR 1449
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
33-212 |
2.53e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILD--KPTTGKVFFLGKDISKLDDAEASkirAKHVGFVFQTFNLIPWL 110
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 -------TALENVeialaisgypfhkRKRRSRELLESVGLGD------RLHHRPTEL---------SGGEQQRVAIARAL 168
Cdd:PRK09580 94 snqfflqTALNAV-------------RSYRGQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKKRNDILQMA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1491196576 169 ANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTH 212
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLR-DGKRSFIIVTH 203
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
132-224 |
3.98e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.46 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 132 RRSRELLESVGLGD-RLHHRPTELSGGEQQRVAIARALANNPD----VILaDEPTGNLDSKsgDV--IIKILKELsLEQN 204
Cdd:PRK00349 808 ARKLQTLVDVGLGYiKLGQPATTLSGGEAQRVKLAKELSKRSTgktlYIL-DEPTTGLHFE--DIrkLLEVLHRL-VDKG 883
|
90 100
....*....|....*....|
gi 1491196576 205 KTIIVVTHNFEITKVADRII 224
Cdd:PRK00349 884 NTVVVIEHNLDVIKTADWII 903
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-185 |
4.04e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 11 DLVYILDSVTKIYGkGRLAVkalDNVSFTVKRGEFLVVMGPSGSGKTTLLN-IMGiLDKPTTGKVfFLGKDIsklddaea 89
Cdd:PRK11819 322 DKVIEAENLSKSFG-DRLLI---DDLSFSLPPGGIVGIIGPNGAGKSTLFKmITG-QEQPDSGTI-KIGETV-------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 90 skirakHVGFVFQTF-NLIPWLTALENV-----EIALAisgypfhKRKRRSRELLESVGL--GDRlHHRPTELSGGEQQR 161
Cdd:PRK11819 388 ------KLAYVDQSRdALDPNKTVWEEIsggldIIKVG-------NREIPSRAYVGRFNFkgGDQ-QKKVGVLSGGERNR 453
|
170 180
....*....|....*....|....
gi 1491196576 162 VAIARALANNPDVILADEPTGNLD 185
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-216 |
4.89e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.23 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLlniMGILDKPTTGKvfFLGKDISKLDDAEASKIRAKHVGFVFQTFNLIPWLTA 112
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTL---MDVLAGRKTGG--YIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENVeIALAISGYPFHKRKRRSR-------ELLESVGLGDRLHHRP--TELSGGEQQRVAIARALANNPDVILADEPTGN 183
Cdd:PLN03140 971 RESL-IYSAFLRLPKEVSKEEKMmfvdevmELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190
....*....|....*....|....*....|...
gi 1491196576 184 LDSKSGDVIIKILKElSLEQNKTIIVVTHNFEI 216
Cdd:PLN03140 1050 LDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSI 1081
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-224 |
7.41e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 7.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491196576 154 LSGGEQQRVAIARALANNPDVI--LADEPTGNLDSKSGDVIIKILKELSlEQNKTIIVVTHNFEITKVADRII 224
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLR-DQGNTVLLVEHDEQMISLADRII 548
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-215 |
1.13e-06 |
|
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: 49.14 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 19 VTKIYGKGRLAVkaLDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILdKPTTGKVfflgkdisKLDdaeaskirakhvG 98
Cdd:TIGR01271 1223 LTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEI--------QID------------G 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 99 FVFQTFNLIPWLTALENVEIALAISGYPFHKR----KRRSRELL----ESVGLGDRLHHRPTEL-----------SGGEQ 159
Cdd:TIGR01271 1280 VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNldpyEQWSDEEIwkvaEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHK 1359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1491196576 160 QRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFE 215
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF--SNCTVILSEHRVE 1413
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-192 |
1.57e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 31 KALDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISKlddaeaskIRAKHVGFVFQTFNLIPWL 110
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN--------IAKPYCTYIGHNLGLKLEM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 TALENVEialaisgypFHKRKRRSRELLESV----GLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDS 186
Cdd:PRK13541 86 TVFENLK---------FWSEIYNSAETLYAAihyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
....*.
gi 1491196576 187 KSGDVI 192
Cdd:PRK13541 157 ENRDLL 162
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
33-230 |
2.95e-06 |
|
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: 47.16 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGildkpttgKVFFLGKDISkLDdaeaskirakhvGFVFQTFNLIPWLTA 112
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL--------RLLNTEGDIQ-ID------------GVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENVEIALAISGYPFHKR-----KRRSRELL---ESVGLGDRLHHRPTEL-----------SGGEQQRVAIARALANNPD 173
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNldpygKWSDEEIWkvaEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 174 VILADEPTGNLDSKSGDVIIKILKELSleQNKTIIVVTHNFEITKVADRIIYLHDGR 230
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAF--ADCTVILSEHRIEAMLECQRFLVIEENK 213
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
37-212 |
4.14e-06 |
|
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: 47.05 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 37 SFTVKRGEFLVVMGPSGSGKTTLLNIMG--------ILDKPTTGKVFFLGKDisklddaeaskirakhvgfvfqtfnliP 108
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQR---------------------------P 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 109 WLT--ALENVEIalaisgYP-----FHKRKRRSREL---LESVGLGDRLHHR---------PTELSGGEQQRVAIARALA 169
Cdd:TIGR00954 525 YMTlgTLRDQII------YPdssedMKRRGLSDKDLeqiLDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1491196576 170 NNPDVILADEPTGNLdskSGDVIIKILkELSLEQNKTIIVVTH 212
Cdd:TIGR00954 599 HKPQFAILDECTSAV---SVDVEGYMY-RLCREFGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
128-228 |
5.65e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 128 HKRKRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSlEQNKTI 207
Cdd:PRK10938 110 VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITL 188
|
90 100
....*....|....*....|..
gi 1491196576 208 IVVTHNF-EITKVADRIIYLHD 228
Cdd:PRK10938 189 VLVLNRFdEIPDFVQFAGVLAD 210
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-212 |
8.20e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 128 HKRKRRSRELLESVGLGDRLHHRPTE-LSGGEQQRVAIARALA----------NNPDVILADEPTGNLDSKSGDVIIKIL 196
Cdd:TIGR00618 924 HVNARKYQGLALLVADAYTGSVRPSAtLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGIL 1003
|
90
....*....|....*.
gi 1491196576 197 KELSlEQNKTIIVVTH 212
Cdd:TIGR00618 1004 DAIR-EGSKMIGIISH 1018
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-226 |
1.03e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIM--------GILDKPTTGKVFFLGKDISKLD----------DAEASKIRA 94
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadgGSYTFPGNWQLAWVNQETPALPqpaleyvidgDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 95 KhvgfvFQTFNLIPWLTALENVEIAL-AISGYPFhkrKRRSRELLESVGLG-DRLHHRPTELSGGEQQRVAIARALANNP 172
Cdd:PRK10636 97 Q-----LHDANERNDGHAIATIHGKLdAIDAWTI---RSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1491196576 173 DVILADEPTGNLDSksgDVIIKILKELSlEQNKTIIVVTHNFE-ITKVADRIIYL 226
Cdd:PRK10636 169 DLLLLDEPTNHLDL---DAVIWLEKWLK-SYQGTLILISHDRDfLDPIVDKIIHI 219
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-229 |
2.77e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 136 ELLESVGLGD-RLHHRPTELSGGEQQRVAIARALANN-PDVI-LADEPTGNLDSKSGDVIIKILKELsLEQNKTIIVVTH 212
Cdd:PRK00635 1369 TFIDKVGLSYiTLGQEQDTLSDGEHYRLHLAKKISSNlTDIIyLLEDPLSGLHPQDAPTLLQLIKEL-VTNNNTVIATDR 1447
|
90
....*....|....*..
gi 1491196576 213 NFEITKVADRIIYLHDG 229
Cdd:PRK00635 1448 SGSLAEHADHLIHLGPG 1464
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-229 |
3.05e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLL-NIMGILDKpTTGKVFFLGKDISKLDDAEA----SKIRAKHV---GFVFQtf 104
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLlTFMRMVEV-CGGEIRVNGREIGAYGLRELrrqfSMIPQDPVlfdGTVRQ-- 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 105 NLIPWLTAL-ENVEIALAISGYpfhkrkrRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARA-LANNPDVILADEPTG 182
Cdd:PTZ00243 1403 NVDPFLEASsAEVWAALELVGL-------RERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAlLKKGSGFILMDEATA 1475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1491196576 183 NLDSKSGDVIIKILkeLSLEQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:PTZ00243 1476 NIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
36-212 |
4.24e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 36 VSFT-VKRGEFLVVMGPSGSGKTTLLNIMgildkptT----GKVFFLGKDISKLDDAEASKIRAKhVGFVFQTFNlipwl 110
Cdd:cd03279 20 IDFTgLDNNGLFLICGPTGAGKSTILDAI-------TyalyGKTPRYGRQENLRSVFAPGEDTAE-VSFTFQLGG----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 111 tALENVEIALAISgypfHKRKRRSRELLEsvGLGDRLHHRPTE-LSGGEQQRVAIARALA----------NNPDVILADE 179
Cdd:cd03279 87 -KKYRVERSRGLD----YDQFTRIVLLPQ--GEFDRFLARPVStLSGGETFLASLSLALAlsevlqnrggARLEALFIDE 159
|
170 180 190
....*....|....*....|....*....|...
gi 1491196576 180 PTGNLDSKSGDVIIKILKELSlEQNKTIIVVTH 212
Cdd:cd03279 160 GFGTLDPEALEAVATALELIR-TENRMVGVISH 191
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
151-221 |
4.65e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 151 PTELSGGEQQ------RVAIARALANN-------PDVILaDEPTGNLDSksGDV-----IIKILKELSLEQnktIIVVTH 212
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDS--GHVsqlvdLVESMRRLGVEQ---IVVVSH 852
|
....*....
gi 1491196576 213 NFEITKVAD 221
Cdd:PRK02224 853 DDELVGAAD 861
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-224 |
7.25e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 133 RSR-ELLESVGLGD-RLHHRPTELSGGEQQRVAIARALANNPDVIL--ADEPTGNLDSKSGDVIIKILKELSlEQNKTII 208
Cdd:TIGR00630 466 RERlGFLIDVGLDYlSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLR-DLGNTLI 544
|
90
....*....|....*.
gi 1491196576 209 VVTHNFEITKVADRII 224
Cdd:TIGR00630 545 VVEHDEDTIRAADYVI 560
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
131-230 |
1.77e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 131 KRRSRELLESVGLGDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNKTIIVV 210
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT 201
|
90 100
....*....|....*....|
gi 1491196576 211 THNFEITKVADRIIYLHDGR 230
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRGR 221
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-224 |
2.64e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 133 RSR-ELLESVGLG----DRLhhRPTeLSGGEQQRVAIARALANN-PDV--ILaDEPTGNLDSKSGDVIIKILKELSLEQN 204
Cdd:COG0178 463 RSRlGFLVDVGLDyltlDRS--AGT-LSGGEAQRIRLATQIGSGlVGVlyVL-DEPSIGLHQRDNDRLIETLKRLRDLGN 538
|
90 100
....*....|....*....|
gi 1491196576 205 kTIIVVTHNFEITKVADRII 224
Cdd:COG0178 539 -TVIVVEHDEDTIRAADYII 557
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
154-221 |
4.05e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 4.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 154 LSGGEQQ------RVAIARALANNPDVILADEPTGNLDSKSGDVIIKILkELSLEQNKTI---IVVTHNFEITKVAD 221
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDII-EYSLKDSSDIpqvIMISHHRELLSVAD 877
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
135-230 |
5.20e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 135 RELLESVGL-GDRLHHRPTELSGGEQQRVAIARALANNPDVILADEPTGNLDSKsgdvIIKILKELSLEQNKTIIVVTHN 213
Cdd:PRK10636 411 RDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD----MRQALTEALIDFEGALVVVSHD 486
|
90
....*....|....*...
gi 1491196576 214 FEITKVADRIIYL-HDGR 230
Cdd:PRK10636 487 RHLLRSTTDDLYLvHDGK 504
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-229 |
1.67e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 39.54 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTLLNIMGILDKPTTGKVFFLGKDISK--LDDAEASKIRAKHVGFVFQ---TFNLI 107
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKigLHDLRFKITIIPQDPVLFSgslRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 108 PWLT-ALENVEIALAISgypfHKRKRRSrellesvGLGDRLHHRPTE----LSGGEQQRVAIARALANNPDVILADEPTG 182
Cdd:TIGR00957 1382 PFSQySDEEVWWALELA----HLKTFVS-------ALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1491196576 183 NLDSKSGDVIIKILKelSLEQNKTIIVVTHNFEITKVADRIIYLHDG 229
Cdd:TIGR00957 1451 AVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKG 1495
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
161-213 |
3.37e-03 |
|
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: 38.49 E-value: 3.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1491196576 161 RVAIARALANNPDVILADEPTGNLDSKS----GDVIIKILKELSLEQNKTIIVVTHN 213
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHD 1269
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
145-228 |
4.29e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.82 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 145 DRLHHRPTELSGG--EQ----QRVAIARALANNPDVILADEPTGNLDSKSGDVIIKILKELSLEQNktIIVVTHNFEI-- 216
Cdd:COG4717 550 DGRTRPVEELSRGtrEQlylaLRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQ--VIYFTCHEELve 627
|
90
....*....|....
gi 1491196576 217 --TKVADRIIYLHD 228
Cdd:COG4717 628 lfQEEGAHVIELES 641
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
47-214 |
7.11e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.53 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 47 VVMGPSGSGKTTLLN-IMGILdkptTGKVFFLGKDISKLDDAEASKIRakhVGFVFQT-------------FNLIPWLTA 112
Cdd:COG0419 27 LIVGPNGAGKSTILEaIRYAL----YGKARSRSKLRSDLINVGSEEAS---VELEFEHggkryrierrqgeFAEFLEAKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491196576 113 LENVEIALAISGYPFHKR------------KRRSRELLESVGLGDRLHHRPTE------LSGGEQQRVAIARALannpDV 174
Cdd:COG0419 100 SERKEALKRLLGLEIYEElkerlkeleealESALEELAELQKLKQEILAQLSGldpietLSGGERLRLALADLL----SL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1491196576 175 ILaDepTGNLDSKSGDVIIKILKELSleqnktiiVVTHNF 214
Cdd:COG0419 176 IL-D--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
33-59 |
9.02e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 36.93 E-value: 9.02e-03
10 20
....*....|....*....|....*..
gi 1491196576 33 LDNVSFTVKRGEFLVVMGPSGSGKTTL 59
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| |
