|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-219 |
2.18e-114 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 326.23 E-value: 2.18e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKErreraRELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIRENI 219
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-215 |
2.70e-106 |
|
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: 305.57 E-value: 2.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKErreraEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-217 |
2.21e-77 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 232.96 E-value: 2.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIsTLKEKDLTNYR 82
Cdd:COG1126 2 IEIENLHKSFG----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNpLNKEE-------LLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKN 155
Cdd:COG1126 77 R-KVGMVFQQFNLFPHLTVLENVTLAPIKVKK-MSKAEaeerameLLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHndaikDM------ADRVIYLHDGRIRE 217
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTH-----EMgfarevADRVVFMDGGRIVE 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-217 |
4.67e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 228.78 E-value: 4.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNID-----VGKylSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKN 155
Cdd:COG2884 79 RR-IGVVFQDFRLLPDRTVYENVAlplrvTGK--SRKEIRRrvREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDA-IKDMADRVIYLHDGRIRE 217
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLElVDRMPKRVLELEDGRLVR 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-215 |
1.30e-74 |
|
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: 226.01 E-value: 1.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:COG1127 6 IEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNI----DVGKYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:COG1127 82 R-RIGMLFQGGALFDSLTVFENVafplREHTDLSEAEIRElvLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-217 |
1.09e-72 |
|
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: 220.92 E-value: 1.09e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03258 82 R-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEieervLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEVVE 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-215 |
4.89e-72 |
|
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: 218.55 E-value: 4.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIsTLKEKDLTNYR 82
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVG----KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLApikvKGMSKAEAEEraLELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-215 |
7.45e-72 |
|
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: 217.77 E-value: 7.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYR 82
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-----GVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVGKYLSKNP-----LNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03259 72 RN-IGMVFQDYALFPHLTVAENIAFGLKLRGVPkaeirARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHdqEEALA-LADRIAVMNEGRI 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-217 |
1.37e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 221.49 E-value: 1.37e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVgkylsknPL-----NKE-------ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGR 150
Cdd:COG1135 82 RK-IGMIFQHFNLLSSRTVAENVAL-------PLeiagvPKAeirkrvaELLELVGLSDKADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 151 AIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmDVVRRICDRVAVLENGRIVE 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-215 |
4.65e-71 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 220.74 E-value: 4.65e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 2 FLSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNY 81
Cdd:COG3842 5 ALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 RRNhLGYVFQMYNLISHLNVEQNidVGKYLSKNPLNK-------EELLQTLGLK--EHRYkqPNQLSGGQQQRTSIGRAI 152
Cdd:COG3842 76 KRN-VGMVFQDYALFPHLTVAEN--VAFGLRMRGVPKaeirarvAELLELVGLEglADRY--PHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 153 IKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHndaikD------MADRVIYLHDGRI 215
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH-----DqeealaLADRIAVMNDGRI 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-220 |
2.18e-70 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 215.72 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLkekdltn 80
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 yrRNHLGYVFQMYNLISHLNVEQNIDVGkyLSKNPLNKEE-------LLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAII 153
Cdd:COG1116 79 --GPDRGVVFQEPALLPWLTVLDNVALG--LELRGVPKAErrerareLLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 154 KNPDLLLCDEPTGALDYHTsKDILQ-LIEDVNKKYGNTIIIVTHN--DAIKdMADRVIYL--HDGRIRENIK 220
Cdd:COG1116 155 NDPEVLLMDEPFGALDALT-RERLQdELLRLWQETGKTVLFVTHDvdEAVF-LADRVVVLsaRPGRIVEEID 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-215 |
6.57e-70 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 214.15 E-value: 6.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:COG3638 3 LELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVGKyLSKNPL--------NKEE------LLQTLGLKEHRYKQPNQLSGGQQQRTSI 148
Cdd:COG3638 80 R-RIGMIFQQFNLVPRLSVLTNVLAGR-LGRTSTwrsllglfPPEDreraleALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 149 GRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQvDLARRYADRIIGLRDGRV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-215 |
9.09e-70 |
|
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: 213.52 E-value: 9.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeyKTeVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:cd03261 1 IELRGLTKSFGG---RT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNidVGKYLSKNPLNKEEL--------LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIK 154
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFEN--VAFPLREHTRLSEEEireivlekLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 155 NPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-217 |
1.42e-69 |
|
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: 212.33 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkekdltnyR 82
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDVGkyLSKNPLNK-------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKN 155
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALG--LELQGVPKaeareraEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIKdMADRVIYL--HDGRIRE 217
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDidEAVF-LADRVVVLsaRPGRIVA 214
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-216 |
1.16e-68 |
|
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: 210.26 E-value: 1.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNKE------ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:TIGR02982 82 RR-IGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEarerarAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIR 216
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-217 |
1.26e-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: 210.44 E-value: 1.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtNYR 82
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQmyNLISHLN----VEQNI-------DVGKYLSKNPLNKEELLQTLGLKEHRYKQ-PNQLSGGQQQRTSIGR 150
Cdd:cd03257 81 RKEIQMVFQ--DPMSSLNprmtIGEQIaeplrihGKLSKKEARKEAVLLLLVGVGLPEEVLNRyPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 151 AIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVAVMYAGKIVE 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-217 |
4.61e-68 |
|
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: 208.83 E-value: 4.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDVgkylsknPL----------NKEELLQTLGLKE--HRYkqPNQLSGGQQQRTSIGR 150
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVML-------PLelagrrdaraRARALLERVGLGHrlDHY--PAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 151 AIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-215 |
9.52e-68 |
|
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: 208.58 E-value: 9.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLN-------KEE------LLQTLGLKEHRYKQPNQLSGGQQQRTSIG 149
Cdd:cd03256 78 R-QIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRslfglfpKEEkqralaALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 150 RAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQvDLAREYADRIVGLKDGRI 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-228 |
1.40e-67 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 219.21 E-value: 1.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDV-----GKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVpavyaGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDAIKDMADRVIYLHDGRIRENIKNTHKIPAK 228
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVA 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-215 |
1.28e-65 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 206.46 E-value: 1.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyr 82
Cdd:COG3839 4 LELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVG---KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG3839 75 RN-IAMVFQSYALYPHMTVYENIAFPlklRKVPKAEIDRrvREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHndaikD------MADRVIYLHDGRI 215
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH-----DqveamtLADRIAVMNDGRI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-217 |
1.59e-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: 1.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKT-EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNY 81
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 RRnHLGYVFQMYN--LISHLNVEQNI----DVGKYLSKNPLNK--EELLQTLGLKE---HRYkqPNQLSGGQQQRTSIGR 150
Cdd:COG1123 341 RR-RVQMVFQDPYssLNPRMTVGDIIaeplRLHGLLSRAERRErvAELLERVGLPPdlaDRY--PHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 151 AIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRIVE 485
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-215 |
1.68e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 199.90 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIstlkEKDLTNYR 82
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNID-VGKY--LSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG1131 73 R-RIGYVPQEPALYPDLTVRENLRfFARLygLPRKEAREriDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-225 |
2.76e-64 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 203.07 E-value: 2.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkekDLTN 80
Cdd:COG1118 1 MSIEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRRNhLGYVFQMYNLISHLNVEQNIDVGkyLSKNPLNK-------EELLQTLGLK--EHRYkqPNQLSGGQQQRTSIGRA 151
Cdd:COG1118 73 RERR-VGFVFQHYALFPHMTVAENIAFG--LRVRPPSKaeirarvEELLELVQLEglADRY--PSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 152 IIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIkDMADRVIYLHDGRIrENIKNTHKI 225
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqeEAL-ELADRVVVMNQGRI-EQVGTPDEV 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-214 |
1.02e-62 |
|
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: 193.56 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNyr 82
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIdvgkylsknplnkeellqTLGlkehrykqpnqLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENI------------------ALG-----------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIKdMADRVIYLHDGR 214
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDldEAAR-LADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-217 |
1.41e-62 |
|
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: 195.41 E-value: 1.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyR 82
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISH--LNVEQNIDVGKYLSKNPLNKE---ELLQTLGL-KEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:COG1124 78 RRRVQMVFQDPYASLHprHTVDRILAEPLRIHGLPDREEriaELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDlAVVAHLCDRVAVMQNGRIVE 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-215 |
2.12e-62 |
|
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: 194.82 E-value: 2.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:TIGR02315 2 LEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLN----------KEELLQTL---GLKEHRYKQPNQLSGGQQQRTSIG 149
Cdd:TIGR02315 79 R-RIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRsllgrfseedKERALSALervGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 150 RAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQvDLAKKYADRIVGLKAGEI 224
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-210 |
2.46e-62 |
|
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: 193.60 E-value: 2.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRN 84
Cdd:TIGR03608 1 LKNISKKFGDKV----ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 HLGYVFQMYNLISHLNVEQNIDVG-KYLSKNPLNKEEL----LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLL 159
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGlKYKKLSKKEKREKkkeaLEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 160 LCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDAIKDMADRVIYL 210
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-215 |
1.12e-61 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 192.24 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:NF038007 2 LNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNI-------DVGKYLSKNPLNkeELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKN 155
Cdd:NF038007 82 RELIGYIFQSFNLIPHLSIFDNValplkyrGVAKKERIERVN--QVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-217 |
3.76e-61 |
|
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: 191.03 E-value: 3.76e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:TIGR02211 2 LKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEakeraYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-215 |
9.73e-61 |
|
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: 190.53 E-value: 9.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYR 82
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVG---KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03300 72 R-PVNTVFQNYALFPHLTVFENIAFGlrlKKLPKAEIKErvAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIKdMADRVIYLHDGRI 215
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqeEALT-MSDRIAVMNKGKI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-214 |
1.27e-58 |
|
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: 184.21 E-value: 1.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEDEykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrR 83
Cdd:cd03225 1 ELKNLSFSYPDGA--RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQmynlishlNVEQ---NIDVGKYLSKNPLNK-----------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIG 149
Cdd:cd03225 75 RKVGLVFQ--------NPDDqffGPTVEEEVAFGLENLglpeeeieervEEALELVGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 150 RAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-217 |
4.41e-58 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 186.93 E-value: 4.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRN 84
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 hLGYVFQMYNLISHLNVEQNID-----VGKylSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK11153 84 -IGMIFQHFNLLSSRTVFDNVAlplelAGT--PKAEIKArvTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRLVE 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-215 |
5.66e-58 |
|
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: 184.09 E-value: 5.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyR 82
Cdd:COG1120 2 LEAENLSVGYG----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK---------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAII 153
Cdd:COG1120 75 R-RIAYVPQEPPAPFGLTVRELVALGRYPHLGLFGRpsaedreavEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 154 KNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHdlNLAAR-YADRLVLLKDGRI 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-215 |
8.73e-58 |
|
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: 182.53 E-value: 8.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIstlKEKDLTNYR 82
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQmyN----LIShLNVEQNIDVGkylsknPLNK-----------EELLQTLGLKEHRYKQPNQLSGGQQQRTS 147
Cdd:COG1122 75 R-KVGLVFQ--NpddqLFA-PTVEEDVAFG------PENLglpreeirervEEALELVGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 148 IGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-215 |
1.37e-57 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 184.52 E-value: 1.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEDeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyRRN 84
Cdd:COG1125 4 FENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 hLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGL--KEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG1125 78 -IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERirarvDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHdiDEALK-LGDRIAVMREGRI 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-214 |
2.53e-57 |
|
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: 180.91 E-value: 2.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 19 TEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRnHLGYVFQMYNLISH 98
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR-RIGVVFQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 LNVEQNIDVGKYLSKNPLNK-----EELLQTLGLkEHRYKQ-PNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHT 172
Cdd:TIGR02673 94 RTVYENVALPLEVRGKKEREiqrrvGAALRQVGL-EHKADAfPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1466369044 173 SKDILQLIEDVNkKYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:TIGR02673 173 SERILDLLKRLN-KRGTTVIVATHDlSLVDRVAHRVIILDDGR 214
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-217 |
6.85e-56 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 178.84 E-value: 6.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKD----- 77
Cdd:COG4598 9 LEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 -----LTNYRRNhLGYVFQMYNLISHLNVEQNI-----DVGKylsknpLNKEE-------LLQTLGLKEHRYKQPNQLSG 140
Cdd:COG4598 85 adrrqLQRIRTR-LGMVFQSFNLWSHMTVLENVieapvHVLG------RPKAEaieraeaLLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 141 GQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDAI-KDMADRVIYLHDGRIRE 217
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFaRDVSSHVVFLHQGRIEE 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-215 |
9.09e-56 |
|
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: 177.21 E-value: 9.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 19 TEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRnHLGYVFQMYNLISH 98
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 LNVEQNIDVGKYLSKNP---LNKE--ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTS 173
Cdd:cd03292 93 RNVYENVAFALEVTGVPpreIRKRvpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1466369044 174 KDILQLIEDVNKKyGNTIIIVTHNDAI-KDMADRVIYLHDGRI 215
Cdd:cd03292 173 WEIMNLLKKINKA-GTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
9.52e-56 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 177.90 E-value: 9.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIS---TLKEKD 77
Cdd:COG4161 1 MSIQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRNhLGYVFQMYNLISHLNVEQNidvgkyLSKNP-----LNKEE-------LLQTLGLKEHRYKQPNQLSGGQQQR 145
Cdd:COG4161 77 IRLLRQK-VGMVFQQYNLWPHLTVMEN------LIEAPckvlgLSKEQarekamkLLARLRLTDKADRFPLHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 146 TSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEvEFARKVASQVVYMEKGRIIE 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-215 |
3.90e-55 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 176.10 E-value: 3.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKtevlkgIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYR 82
Cdd:COG3840 2 LRLDDLTYRYGDFPLR------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT-----ALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVGkyLSKN-PLNKEE------LLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKN 155
Cdd:COG3840 71 RP-VSMLFQENNLFPHLTVAQNIGLG--LRPGlKLTAEQraqveqALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIKdMADRVIYLHDGRI 215
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDpeDAAR-IADRVLLVADGRI 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-215 |
1.36e-54 |
|
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: 177.17 E-value: 1.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQP---DSGTITIQGKTISTLKEKDLT 79
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 NYRRNHLGYVFQ--MynliSHLN--------VEQNIDVGKYLSKNPLNKE--ELLQTLGLK--EHRYKQ-PNQLSGGQQQ 144
Cdd:COG0444 82 KIRGREIQMIFQdpM----TSLNpvmtvgdqIAEPLRIHGGLSKAEARERaiELLERVGLPdpERRLDRyPHELSGGMRQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 145 RTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVI--YLhdGRI 215
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlGVVAEIADRVAvmYA--GRI 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-217 |
1.37e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.89 E-value: 1.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkekdltnyR 82
Cdd:COG1121 7 IELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISH--LNVEQNIDVGKYLSKNPLNK---------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRA 151
Cdd:COG1121 74 RRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRpsradreavDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 152 IIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDlGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-215 |
1.55e-54 |
|
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: 174.80 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEyktEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkEKDLTNYR 82
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR---EQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQ--PNQLSGGQQQRTSIGRAIIKN 155
Cdd:cd03295 75 RK-IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKireraDELLALVGLDPAEFADryPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHdiDEAFR-LADRIAIMKNGEI 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-215 |
4.58e-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: 4.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnyR 82
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-----V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDvgkylsknplnkeellqtlglkehrykqpnqLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENLK-------------------------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-215 |
5.79e-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: 176.77 E-value: 5.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 2 FLSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltny 81
Cdd:TIGR03265 4 YLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 RRNHlGYVFQMYNLISHLNVEQNIDVGkyLSKNPLNKE-------ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIK 154
Cdd:TIGR03265 75 KRDY-GIVFQSYALFPNLTVADNIAYG--LKNRGMGRAevaervaELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 155 NPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDqEEALSMADRIVVMNHGVI 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
2.10e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.77 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLkekDLTNYR 82
Cdd:COG4619 1 LELEGLSFRVGG----KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQmynlISHL---NVEQNIDVGKYLSKNPLNKE---ELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKN 155
Cdd:COG4619 74 R-QVAYVPQ----EPALwggTVRDNLPFPFQLRERKFDREralELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDA-IKDMADRVIYLHDGRI 215
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-217 |
4.22e-53 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 170.73 E-value: 4.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDV-----GKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELpallrGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-223 |
4.73e-53 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 170.97 E-value: 4.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI---STLKEKD 77
Cdd:PRK11124 1 MSIQLNGINCFYGA----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRNhLGYVFQMYNLISHLNVEQN-----IDVGKyLSKNPLNKE--ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGR 150
Cdd:PRK11124 77 IRELRRN-VGMVFQQYNLWPHLTVQQNlieapCRVLG-LSKDQALARaeKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 151 AIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIRENIKNTH 223
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEvEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-217 |
7.78e-53 |
|
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: 169.36 E-value: 7.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyr 82
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03301 72 RD-IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEidervREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHnDAIKDM--ADRVIYLHDGRIRE 217
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTH-DQVEAMtmADRIAVMNDGQIQQ 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-217 |
8.46e-53 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 177.79 E-value: 8.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPD---SGTITIQGKTISTLKEKDlt 79
Cdd:COG1123 5 LEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 nyRRNHLGYVFQ--MYNLIShLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAI 152
Cdd:COG1123 81 --RGRRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEararvLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 153 IKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIVE 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-215 |
1.02e-52 |
|
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: 169.93 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdltnYR 82
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP-----HE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYV--FQMYNLISHLNVEQNIDVG-------KYLSKNPLNKE--------ELLQTLGLKEHRYKQPNQLSGGQQQR 145
Cdd:cd03219 72 IARLGIGrtFQIPRLFPELTVLENVMVAaqartgsGLLLARARREEreareraeELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 146 TSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-225 |
1.50e-52 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 169.28 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGI-----DQPDSGTITIQGKTISTLKEkD 77
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDV-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRNhLGYVFQMYNLIsHLNVEQNIDVGKYLSKNPLNK------EELLQTLGLKE--HRYKQPNQLSGGQQQRTSIG 149
Cdd:cd03260 76 VLELRRR-VGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEeldervEEALRKAALWDevKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 150 RAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYgnTIIIVTHNDA-IKDMADRVIYLHDGRIREnIKNTHKI 225
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQqAARVADRTAFLLNGRLVE-FGPTEQI 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-215 |
1.67e-51 |
|
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: 167.82 E-value: 1.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGED-----------EYKTEVLKG---------IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGT 62
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgKSKEEILKKtgqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 63 ITIQGKTISTLKEKDLTNYRRNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQ 137
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEreeraAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 138 LSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHdlDEALR-LGDRIAIMKDGRL 239
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-216 |
2.26e-51 |
|
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: 170.28 E-value: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI-STLKEKDLTNYRRnHLGYVFQMYNLISHLNVEQ 103
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPPHRR-RIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 104 NIDVGKYLSKNPLNK---EELLQTLGLkEH---RYkqPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDIL 177
Cdd:COG4148 97 NLLYGRKRAPRAERRisfDEVVELLGI-GHlldRR--PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1466369044 178 QLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSlDEVARLADHVVLLEQGRVV 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-215 |
2.72e-51 |
|
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: 164.53 E-value: 2.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyRR 83
Cdd:cd03214 1 EVENLSVGYG----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQMynlishlnveqnidvgkylsknplnkeelLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDE 163
Cdd:cd03214 73 RKIAYVPQA-----------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 164 PTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHdlNLAAR-YADRVILLKDGRI 176
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-215 |
1.04e-50 |
|
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: 165.60 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdltnYR 82
Cdd:COG0411 5 LEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-----HR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYV--FQMYNLISHLNVEQNIDVG----------KYLSKNPLNK----------EELLQTLGLKEHRYKQPNQLSG 140
Cdd:COG0411 76 IARLGIArtFQNPRLFPELTVLENVLVAaharlgrgllAALLRLPRARreereareraEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 141 GQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVVLDFGRV 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-215 |
1.21e-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: 164.82 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEyktevLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnyR 82
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVG--KYLSKNPLNKEELLQT---LGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03299 71 RD-ISYVPQNYALFPHMTVYKNIAYGlkKRKVDKKEIERKVLEIaemLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-216 |
2.39e-50 |
|
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: 163.23 E-value: 2.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEkGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI-STLKEKDLTNYRRnHLGYVFQMYNLISHLNVEQ 103
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPPQQR-KIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 104 NIDVG-KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLI 180
Cdd:cd03297 95 NLAFGlKRKRNREDRIsvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1466369044 181 EDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRLQ 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-215 |
2.72e-50 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 167.82 E-value: 2.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYR 82
Cdd:PRK09452 15 VELRGISKSFDG----KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPlNKE------ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:PRK09452 86 R-HVNTVFQSYALFPHMTVFENVAFGLRMQKTP-AAEitprvmEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIKdMADRVIYLHDGRI 215
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqeEALT-MSDRIVVMRDGRI 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-230 |
3.35e-50 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 164.15 E-value: 3.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFgedeYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLK----EKDLTN 80
Cdd:PRK11264 6 VKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRRNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNKE------ELLQTLGL--KEHRYkqPNQLSGGQQQRTSIGRAI 152
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEatararELLAKVGLagKETSY--PRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 153 IKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDAI-KDMADRVIYLHDGRIREniknthKIPAKDL 230
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFaRDVADRAIFMDQGRIVE------QGPAKAL 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-214 |
3.53e-50 |
|
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: 161.40 E-value: 3.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLkkSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyr 82
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQmynlISHL---NVEQNIdvgkylsknplnkeellqtlglkehrykqpnqLSGGQQQRTSIGRAIIKNPDLL 159
Cdd:cd03228 75 RKNIAYVPQ----DPFLfsgTIRENI--------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 160 LCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGR 214
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-218 |
3.55e-50 |
|
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: 163.88 E-value: 3.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnyR 82
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDV-----GKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYfaelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIREN 218
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHImQEVEALCDRVVILHKGKVVAQ 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-215 |
6.73e-50 |
|
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: 162.89 E-value: 6.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltn 80
Cdd:cd03296 1 MSIEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 yrRNhLGYVFQMYNLISHLNVEQNIDVG---KYLSKNPLNKE------ELLQTLGLK--EHRYkqPNQLSGGQQQRTSIG 149
Cdd:cd03296 74 --RN-VGFVFQHYALFRHMTVFDNVAFGlrvKPRSERPPEAEirakvhELLKLVQLDwlADRY--PAQLSGGQRQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 150 RAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIkDMADRVIYLHDGRI 215
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqeEAL-EVADRVVVMNKGRI 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-218 |
3.75e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 161.03 E-value: 3.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 6 KDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyR--R 83
Cdd:PRK09493 5 KNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE----RliR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQMYNLISHLNVEQNIDVG----KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGplrvRGASKEEAEKqaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDAI-KDMADRVIYLHDGRIREN 218
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFaEKVASRLIFIDKGRIAED 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-216 |
9.15e-49 |
|
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: 159.52 E-value: 9.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdltnYR 82
Cdd:cd03224 1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-----HE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLG--YVFQMYNLISHLNVEQNIDVGKYLSKNPLNKEELLQTLG----LKEhRYKQP-NQLSGGQQQRTSIGRAIIKN 155
Cdd:cd03224 72 RARAGigYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYElfprLKE-RRKQLaGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNaRFALEIADRAYVLERGRVV 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-219 |
1.60e-48 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 159.21 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNID----VGKylsKNPLNKE----ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIK 154
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAmpllIGK---KKPAEINsralEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 155 NPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIRENI 219
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-217 |
1.63e-48 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 169.24 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLkkSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLkekDLTNYR 82
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHlNVEQNIDVGkylskNP-LNKEEL---LQTLGLKEHRYKQPN-----------QLSGGQQQRTS 147
Cdd:COG2274 549 R-QIGVVLQDVFLFSG-TIRENITLG-----DPdATDEEIieaARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 148 IGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-214 |
1.17e-47 |
|
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: 154.32 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrR 83
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQmynlishlnveqnidvgkylsknplnkeellqtlglkehrykqpnqLSGGQQQRTSIGRAIIKNPDLLLCDE 163
Cdd:cd00267 73 RRIGYVPQ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 164 PTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDpELAELAADRVIVLKDGK 157
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
3-215 |
1.54e-47 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 159.86 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKsfgedEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLK-EKdltny 81
Cdd:NF040840 2 IRIENLSK-----DWKEFKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPpEK----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 rRNhLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:NF040840 72 -RG-IAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEierkvKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIKdMADRVIYLHDGRI 215
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfeEALS-LADRVGIMLNGRL 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-216 |
4.96e-47 |
|
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: 154.97 E-value: 4.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnyR 82
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDV-----GKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFyarlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSmDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-215 |
8.42e-47 |
|
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: 154.19 E-value: 8.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 26 DFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyrrNHLGYVFQMYNLISHLNVEQNI 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 106 DVGKY--LSKNPLNKEEL---LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLI 180
Cdd:cd03298 92 GLGLSpgLKLTAEDRQAIevaLARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1466369044 181 EDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03298 172 LDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRI 207
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-217 |
8.60e-47 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 155.41 E-value: 8.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkekdlTNYR 82
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG------PGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnhlGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG4525 78 R---GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAErraraEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNdaIKD---MADRVIYL--HDGRIRE 217
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS--VEEalfLATRLVVMspGPGRIVE 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-214 |
1.01e-46 |
|
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: 153.79 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIstlkEKDLTN 80
Cdd:COG4133 1 MMLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRRnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNKE---ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG4133 73 YRR-RLAYLGHADGLKPELTVRENLRFWAALYGLRADREaidEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHnDAIKDMADRVIYLHDGR 214
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTH-QPLELAAARVLDLGDFK 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-210 |
1.03e-46 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 153.84 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekdltnYRR 83
Cdd:cd03235 1 EVEDLTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE---------KER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQmynlisHLNVEQN--IDV------GKYLSKNPLNK---------EELLQTLGLKEHRYKQPNQLSGGQQQRT 146
Cdd:cd03235 68 KRIGYVPQ------RRSIDRDfpISVrdvvlmGLYGHKGLFRRlskadkakvDEALERVGLSELADRQIGELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 147 SIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYL 210
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
1.04e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 155.24 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGE---DEykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdlt 79
Cdd:COG1101 2 LELKNLSKTFNPgtvNE--KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 nYRR-NHLGYVFQ--MYNLISHLNVEQNIDV----GKYLSKNP-LNKE------ELLQTLGLK-EHRYKQP-NQLSGGQQ 143
Cdd:COG1101 76 -YKRaKYIGRVFQdpMMGTAPSMTIEENLALayrrGKRRGLRRgLTKKrrelfrELLATLGLGlENRLDTKvGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 144 QRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIkDMADRVIYLHDGRIRENIKN 221
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNmeQAL-DYGNRLIMMHEGRIILDVSG 233
|
...
gi 1466369044 222 THK 224
Cdd:COG1101 234 EEK 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-217 |
1.50e-46 |
|
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: 161.39 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKS-TLLNIIGGIDQPD---SGTITIQGKTISTLKEKDL 78
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 79 TNYRRNHLGYVFQ--MYNLISHLNVEQNID----VGKYLSKNPLNKE--ELLQTLGLK--EHRYKQ-PNQLSGGQQQRTS 147
Cdd:COG4172 87 RRIRGNRIAMIFQepMTSLNPLHTIGKQIAevlrLHRGLSGAAARARalELLERVGIPdpERRLDAyPHQLSGGQRQRVM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 148 IGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAI-KDMADRVIYLHDGRIRE 217
Cdd:COG4172 167 IAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVvRRFADRVAVMRQGEIVE 237
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-215 |
1.87e-45 |
|
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: 152.61 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRnHLGYVFQM--YN 94
Cdd:TIGR04521 16 FEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK-KVGLVFQFpeHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LIShLNVEQNIDVGkylsknPLN----KEE-------LLQTLGLKEHRYKQ-PNQLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:TIGR04521 95 LFE-ETVYKDIAFG------PKNlglsEEEaeervkeALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKI 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-216 |
2.98e-45 |
|
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: 154.11 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI-STLKEKDLTNYRRNhLGYVFQMYNLISHLNVEQ 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRR-IGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 104 NIDVGKYLSKNPL---NKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLI 180
Cdd:TIGR02142 95 NLRYGMKRARPSErriSFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1466369044 181 EDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRVA 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-215 |
2.25e-44 |
|
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: 151.11 E-value: 2.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 37 LLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYRRnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPl 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLR-HINMVFQSYALFPHMTVEENVAFGLKMRKVP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 117 NKE------ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNT 190
Cdd:TIGR01187 74 RAEikprvlEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180
....*....|....*....|....*..
gi 1466369044 191 IIIVTHN--DAIKdMADRVIYLHDGRI 215
Cdd:TIGR01187 154 FVFVTHDqeEAMT-MSDRIAIMRKGKI 179
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-217 |
2.66e-44 |
|
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: 156.08 E-value: 2.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLkkSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyr 82
Cdd:COG4987 334 LELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMynliSHL---NVEQNIDVGkylskNP-LNKEELLQTL---GLKEHRYKQPN-----------QLSGGQQQ 144
Cdd:COG4987 408 RRRIAVVPQR----PHLfdtTLRENLRLA-----RPdATDEELWAALervGLGDWLAALPDgldtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 145 RTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-217 |
3.02e-44 |
|
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: 155.69 E-value: 3.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEyktEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyr 82
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMynliSHL---NVEQNIDVGkylskNP-LNKEELLQTL---GLKEHRYKQPN-----------QLSGGQQQ 144
Cdd:COG4988 410 RRQIAWVPQN----PYLfagTIRENLRLG-----RPdASDEELEAALeaaGLDEFVAALPDgldtplgeggrGLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 145 RTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-215 |
3.75e-44 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 151.39 E-value: 3.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltn 80
Cdd:PRK10851 1 MSIEIANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 yrrNHLGYVFQMYNLISHLNVEQNIDVG-------KYLSKNPLNKE--ELLQTLGLkEH---RYkqPNQLSGGQQQRTSI 148
Cdd:PRK10851 74 ---RKVGFVFQHYALFRHMTVFDNIAFGltvlprrERPNAAAIKAKvtQLLEMVQL-AHladRY--PAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 149 GRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNI 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-165 |
5.69e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 144.71 E-value: 5.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYNLISHLNV 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 102 EQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRY----KQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:pfam00005 77 RENLRLGLLLKGLSKREkdaraEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-215 |
1.03e-43 |
|
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: 145.05 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLkkSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLkekDLTNYR 82
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHlNVEQNIdvgkylsknplnkeellqtlglkehrykqpnqLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:cd03246 76 D-HVGYLPQDDELFSG-SIAENI--------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-217 |
3.19e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 153.01 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVF 90
Cdd:COG1132 346 SFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 QMYNLIsHLNVEQNIDVGkylsKNPLNKEEL---LQTLGLKE------HRYKQP-----NQLSGGQQQRTSIGRAIIKNP 156
Cdd:COG1132 421 QDTFLF-SGTIRENIRYG----RPDATDEEVeeaAKAAQAHEfiealpDGYDTVvgergVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDmADRVIYLHDGRIRE 217
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRlSTIRN-ADRILVLDDGRIVE 554
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-216 |
4.88e-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: 4.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdltn 80
Cdd:COG0410 2 PMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRRNHLG--YVFQMYNLISHLNVEQNIDVGKYLSKNPLNKEELLQTLG-----LKEHRyKQP-NQLSGGQQQRTSIGRAI 152
Cdd:COG0410 73 HRIARLGigYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYelfprLKERR-RQRaGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 153 IKNPDLLLCDEPTGALdyhtS----KDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:COG0410 152 MSRPKLLLLDEPSLGL----AplivEEIFEIIRRLNRE-GVTILLVEQNaRFALEIADRAYVLERGRIV 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-217 |
7.15e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 147.19 E-value: 7.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSF----GEDEYKTEVLK---GIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKE 75
Cdd:COG4608 8 LEVRDLKKHFpvrgGLFGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 76 KDLTNYRRnHLGYVFQmyNLISHLN--------VEQNIDVGKYLSKNPLNK--EELLQTLGLK-EHRYKQPNQLSGGQQQ 144
Cdd:COG4608 88 RELRPLRR-RMQMVFQ--DPYASLNprmtvgdiIAEPLRIHGLASKAERRErvAELLELVGLRpEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 145 RTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDA-IKDMADRVI--YLhdGRIRE 217
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSvVRHISDRVAvmYL--GKIVE 238
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-215 |
1.02e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 147.68 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyr 82
Cdd:PRK11650 4 LKLQAVRKSYDG---KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDVG---KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK11650 76 RD-IAMVFQNYALYPHMSVRENMAYGlkiRGMPKAEIEErvAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 158 LLLCDEPTGALDyhtSKDILQL---IEDVNKKYGNTIIIVTHnDAIKDM--ADRVIYLHDGRI 215
Cdd:PRK11650 155 VFLFDEPLSNLD---AKLRVQMrleIQRLHRRLKTTSLYVTH-DQVEAMtlADRVVVMNGGVA 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-215 |
1.14e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 150.55 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekdLTN 80
Cdd:COG1129 3 PLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR------FRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YR---RNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPL------NKE--ELLQTLGLKEHrykqPNQ----LSGGQQQR 145
Cdd:COG1129 73 PRdaqAAGIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwramRRRarELLARLGLDID----PDTpvgdLSVAQQQL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 146 TSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRlDEVFEIADRVTVLRDGRL 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-216 |
2.85e-42 |
|
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: 144.11 E-value: 2.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGktISTLKEKDLTNYR 82
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQ------------------MYNL-ISHLNVEQNIDvgkylsknplnkeELLQTLGLKEHRYKQPNQLSGGQQ 143
Cdd:TIGR04520 77 K-KVGMVFQnpdnqfvgatveddvafgLENLgVPREEMRKRVD-------------EALKLVGMEDFRDREPHLLSGGQK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 144 QRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIkdMADRVIYLHDGRIR 216
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHdmEEAV--LADRVIVMNKGKIV 215
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-217 |
4.31e-42 |
|
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: 143.20 E-value: 4.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGtITIQGKTIstLKEKDLTNYR 82
Cdd:TIGR00972 2 IEIENLNLFYGEKE----ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPG-VRIEGKVL--FDGQDIYDKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 ------RNHLGYVFQMYNLIShLNVEQNIDVG----KYLSKNPLNK--EELLQTLGL----KEHRYKQPNQLSGGQQQRT 146
Cdd:TIGR00972 75 idvvelRRRVGMVFQKPNPFP-MSIYDNIAYGprlhGIKDKKELDEivEESLKKAALwdevKDRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 147 SIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYgnTIIIVTHN--DAIKdMADRVIYLHDGRIRE 217
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNmqQAAR-ISDRTAFFYDGELVE 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-219 |
1.58e-41 |
|
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: 140.43 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnyr 82
Cdd:cd03268 1 LKTNDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDV-GKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLC 161
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLlARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 162 DEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHNDA-IKDMADRVIYLHDGRIRENI 219
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-217 |
2.79e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 141.26 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKD----- 77
Cdd:PRK10619 6 LNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 ----LTNYRRNHLGYVFQMYNLISHLNVEQNIDVGKY----LSKNPLNKEEL--LQTLGLKEH-RYKQPNQLSGGQQQRT 146
Cdd:PRK10619 82 adknQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIqvlgLSKQEARERAVkyLAKVGIDERaQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 147 SIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEmGFARHVSSHVIFLHQGKIEE 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-215 |
2.89e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 140.49 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 26 DFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkekdlTNYRRNHLGYVFQMYNLISHLNVEQNI 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT------TPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 106 DVGKY--LSKNPLNKEEL---LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLI 180
Cdd:PRK10771 93 GLGLNpgLKLNAAQREKLhaiARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1466369044 181 EDVNKKYGNTIIIVTHN--DAIKdMADRVIYLHDGRI 215
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSleDAAR-IAPRSLVVADGRI 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-217 |
4.83e-41 |
|
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: 146.75 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSF---------GEDEYKteVLKGIDFEIEKGEICVLLGPSGSGKSTL-LNIIGGIDQpdSGTITIQGKTIST 72
Cdd:COG4172 276 LEARDLKVWFpikrglfrrTVGHVK--AVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIPS--EGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 73 LKEKDLTNYRRnHLGYVFQ--MYNLISHLNVEQNIDVGKYLSKNPLNKEE-------LLQTLGLKE---HRYkqPNQLSG 140
Cdd:COG4172 352 LSRRALRPLRR-RMQVVFQdpFGSLSPRMTVGQIIAEGLRVHGPGLSAAErrarvaeALEEVGLDPaarHRY--PHEFSG 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 141 GQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlAVVRALAHRVMVMKDGKVVE 506
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-216 |
5.12e-41 |
|
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: 139.34 E-value: 5.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKekdltnyr 82
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVeqnIDVGKYLSK-NPLNKEE-------LLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIK 154
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKV---IDQLVYLAQlKGLKKEEarrrideWLERLELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 155 NPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-214 |
2.08e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 142.28 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSF-GEdeyktEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNY 81
Cdd:PRK11607 20 LEIRNLTKSFdGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 RRNhLGYVFQMYNLISHLNVEQNIDVG---KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:PRK11607 90 QRP-INMMFQSYALFPHMTVEQNIAFGlkqDKLPKAEIASrvNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 157 DLLLCDEPTGALDYHTsKDILQL-IEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:PRK11607 169 KLLLLDEPMGALDKKL-RDRMQLeVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGK 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-215 |
3.60e-40 |
|
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: 135.25 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyR 82
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFqmynlishlnveqnidvgkylsknplnkeellqtlglkehrykqpnQLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:cd03216 74 RAGIAMVY----------------------------------------------QLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-216 |
6.72e-40 |
|
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: 136.73 E-value: 6.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkeKDLTNYRRN 84
Cdd:cd03265 3 VENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 hLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLL 159
Cdd:cd03265 75 -IGIVFQDLSVDDELTGWENLYIHARLYGVPGAErreriDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 160 LCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRII 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
16-215 |
2.76e-39 |
|
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: 134.99 E-value: 2.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 16 EYKTEVLKgIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdltnYRRNhLGYVFQMYNL 95
Cdd:TIGR01277 9 EYEHLPME-FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP-----YQRP-VSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 96 ISHLNVEQNIDVGKY--LSKNPLNKEELL---QTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDY 170
Cdd:TIGR01277 82 FAHLTVRQNIGLGLHpgLKLNAEQQEKVVdaaQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1466369044 171 HTSKDILQLIEDVNKKYGNTIIIVTHN--DAIKdMADRVIYLHDGRI 215
Cdd:TIGR01277 162 LLREEMLALVKQLCSERQRTLLMVTHHlsDARA-IASQIAVVSQGKI 207
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-217 |
4.26e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.55 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGI--DQPD---SGTITIQGKTISTlKEKD 77
Cdd:COG1117 12 IEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYD-PDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRnHLGYVFQMYNLISHlNVEQNIDVG----KYLSKNPLNK--EELLQTLGLKE---HRYKQP-NQLSGGQQQRTS 147
Cdd:COG1117 87 VVELRR-RVGMVFQKPNPFPK-SIYDNVAYGlrlhGIKSKSELDEivEESLRKAALWDevkDRLKKSaLGLSGGQQQRLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 148 IGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYgnTIIIVTHNdaikdM------ADRVIYLHDGRIRE 217
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHN-----MqqaarvSDYTAFFYLGELVE 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-215 |
4.46e-39 |
|
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: 133.92 E-value: 4.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEdeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIstlKEKDltnyRR 83
Cdd:cd03226 1 RIENISFSYKK---GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKE----RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQ--MYNLISHlNVEQNIDVG-KYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLL 160
Cdd:cd03226 71 KSIGYVMQdvDYQLFTD-SVREELLLGlKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDyEFLAKVCDRVLLLANGAI 204
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-214 |
5.49e-39 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 134.48 E-value: 5.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSF---GEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITI----QGKTISTLKE 75
Cdd:COG4778 5 LEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 76 KDLTNYRRNHLGYVFQMYNLI---SHLNV------EQNIDVGKYLSKnplnKEELLQTLGLKEHRYK-QPNQLSGGQQQR 145
Cdd:COG4778 85 REILALRRRTIGYVSQFLRVIprvSALDVvaepllERGVDREEARAR----ARELLARLNLPERLWDlPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 146 TSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHNDAIKD-MADRVIYLHDGR 214
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREaVADRVVDVTPFS 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-213 |
1.02e-38 |
|
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: 133.75 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTnyrrnhlgyVFQMYNLISHLNV 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQNI-----DVGKYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSK 174
Cdd:TIGR01184 72 RENIalavdRVLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1466369044 175 DILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDG 213
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-215 |
1.37e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 134.42 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdltNYR 82
Cdd:PRK11247 13 LLLNAVSKRYGE----RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE----DTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnhlgYVFQMYNLISHLNVEQNIDVGkyLSKN-PLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLC 161
Cdd:PRK11247 85 -----LMFQDARLLPWKKVIDNVGLG--LKGQwRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 162 DEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHdvSEAVA-MADRVLLIEEGKI 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-221 |
3.07e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 132.31 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRnHLGYVFQMYNLISHL 99
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 NVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSK 174
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDirrrvSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1466369044 175 DILQLIEDVNkKYGNTIIIVTHNDA-IKDMADRVIYLHDGRIRENIKN 221
Cdd:PRK10908 175 GILRLFEEFN-RVGVTVLMATHDIGlISRRSYRMLTLSDGHLHGGVGG 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-216 |
4.16e-38 |
|
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: 131.55 E-value: 4.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGeICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkeKDLTNYR 82
Cdd:cd03264 1 LQLENLTKRYG----KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03264 72 R-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEvkarvDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-216 |
5.84e-38 |
|
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: 131.72 E-value: 5.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGktISTLKEKdlTNYR 82
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEP--AEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHLNVEQNIDV--GKY-LSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03266 78 RR-LGFVSDSTGLYDRLTARENLEYfaGLYgLKGDELTArlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImQEVERLCDRVVVLHRGRVV 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-215 |
1.19e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 134.77 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYRR 83
Cdd:PRK11000 5 TLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NhLGYVFQMYNLISHLNVEQNIDVGKYLS---KNPLNKE-----ELLQTLGLKEhryKQPNQLSGGQQQRTSIGRAIIKN 155
Cdd:PRK11000 76 G-VGMVFQSYALYPHLSVAENMSFGLKLAgakKEEINQRvnqvaEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHnDAIKDM--ADRVIYLHDGRI 215
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH-DQVEAMtlADKIVVLDAGRV 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-215 |
2.29e-37 |
|
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: 130.34 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKekdlTNYR 82
Cdd:TIGR03410 1 LEVSNLNVYYGQ----SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP----PHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 -RNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK--EELLQTLG-LKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDL 158
Cdd:TIGR03410 73 aRAGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKipDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 159 LLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYlDFARELADRYYVMERGRV 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-215 |
4.53e-37 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 130.20 E-value: 4.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 19 TEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSG-TITIQGKT-----ISTLkekdltnyrRNHLGYV--F 90
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedVWEL---------RKRIGLVspA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 QMYNLISHLNVEqniDV---GKY----LSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDL 158
Cdd:COG1119 87 LQLRFPRDETVL---DVvlsGFFdsigLYREPTDEqreraRELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 159 LLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHvEEIPPGITHVLLLKDGRV 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-215 |
1.03e-36 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 128.81 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkekdLTNYR 82
Cdd:cd03218 1 LRAENLSKRYG----KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-----LPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLG--YVFQMYNLISHLNVEQNIDV---GKYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKN 155
Cdd:cd03218 72 RARLGigYLPQEASIFRKLTVEENILAvleIRGLSKKEREEklEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNvRETLSITDRAYIIYEGKV 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
1.18e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 129.81 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKeKDLTNYR 82
Cdd:PRK13639 2 LETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-KSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQmyNLISHL---NVEQNIDVGKY---LSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIK 154
Cdd:PRK13639 78 KT-VGIVFQ--NPDDQLfapTVEEDVAFGPLnlgLSKEEVEKrvKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 155 NPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKI 215
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-230 |
1.66e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 131.38 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 2 FLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGK--TISTLKEKDLT 79
Cdd:PRK11432 6 FVVLKNITKRFG----SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvTHRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 nyrrnhlgYVFQMYNLISHLNVEQNIDVGkyLSKNPLNKEELLQ---------TLGLKEHRYKqpNQLSGGQQQRTSIGR 150
Cdd:PRK11432 82 --------MVFQSYALFPHMSLGENVGYG--LKMLGVPKEERKQrvkealelvDLAGFEDRYV--DQISGGQQQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 151 AIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHND----AIKDMadrVIYLHDGRIREniknthKIP 226
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQseafAVSDT---VIVMNKGKIMQ------IGS 220
|
....
gi 1466369044 227 AKDL 230
Cdd:PRK11432 221 PQEL 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-217 |
2.03e-36 |
|
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: 128.12 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIstlKEKDLTNYRRnHLGYVFQ-------- 91
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLRR-AIGVVPQdtvlfndt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 92 -MYNlISHLNV----EQNIDVGKYLSKNP--LNKEELLQTL----GLKehrykqpnqLSGGQQQRTSIGRAIIKNPDLLL 160
Cdd:cd03253 91 iGYN-IRYGRPdatdEEVIEAAKAAQIHDkiMRFPDGYDTIvgerGLK---------LSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDmADRVIYLHDGRIRE 217
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRlSTIVN-ADKIIVLKDGRIVE 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-215 |
3.58e-36 |
|
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: 126.94 E-value: 3.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVF 90
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 QMYNLISHlNVEQNIDVGKYLSKNplnkEELLQTL---GLKEHRYKQPN-----------QLSGGQQQRTSIGRAIIKNP 156
Cdd:cd03245 85 QDVTLFYG-TLRDNITLGAPLADD----ERILRAAelaGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 157 DLLLCDEPTGALDYHTSKdilQLIEDVNK-KYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:cd03245 160 PILLLDEPTSAMDMNSEE---RLKERLRQlLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-217 |
3.63e-36 |
|
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: 127.35 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLkkSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyr 82
Cdd:cd03251 1 VEFKNV--TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHlNVEQNIDVGKyLSKNPLNKEELLQTLGLKEHRYKQPN-----------QLSGGQQQRTSIGRA 151
Cdd:cd03251 75 RRQIGLVSQDVFLFND-TVAENIAYGR-PGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 152 IIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDmADRVIYLHDGRIRE 217
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRlSTIEN-ADRIVVLEDGKIVE 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
3.77e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 127.45 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGktistlkeKDLTN 80
Cdd:COG1137 2 MTLEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG--------EDITH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 ---YRRNHLG--Y------VFQmynlisHLNVEQNID-VgkyLSKNPLNK-------EELLQTLGLkEHRYKQP-NQLSG 140
Cdd:COG1137 70 lpmHKRARLGigYlpqeasIFR------KLTVEDNILaV---LELRKLSKkereerlEELLEEFGI-THLRKSKaYSLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 141 GQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNvRETLGICDRAYIISEGKV 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-215 |
8.67e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 127.44 E-value: 8.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGI---DQPDSGTITIQGKTISTLKE--KD 77
Cdd:PRK09984 5 IRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNyRRNHLGYVFQMYNLISHLNVEQNIDVGKYLSK----------NPLNKEELLQTL---GLKEHRYKQPNQLSGGQQQ 144
Cdd:PRK09984 81 IRK-SRANTGYIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswfTREQKQRALQALtrvGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 145 RTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHV 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-225 |
1.06e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.11 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKS------FGEDEYKTeVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEK 76
Cdd:PRK10419 4 LNVSGLSHHyahgglSGKHQHQT-VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 77 DLTNYRRNhLGYVFQmyNLISHLNVEQniDVGKYLSKnPLNK-------------EELLQTLGLK-EHRYKQPNQLSGGQ 142
Cdd:PRK10419 83 QRKAFRRD-IQMVFQ--DSISAVNPRK--TVREIIRE-PLRHllsldkaerlaraSEMLRAVDLDdSVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 143 QQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRENIKN 221
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDlRLVERFCQRVMVMDNGQIVETQPV 236
|
....
gi 1466369044 222 THKI 225
Cdd:PRK10419 237 GDKL 240
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-225 |
1.34e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 127.47 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIsTLKEKDLTNYRRNhLGYVFQM--YN 94
Cdd:PRK13637 18 FEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKK-VGLVFQYpeYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LISHlNVEQNIDVGKY---LSKNPLNKE--ELLQTLGLKEHRYK--QPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:PRK13637 96 LFEE-TIEKDIAFGPInlgLSEEEIENRvkRAMNIVGLDYEDYKdkSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 168 LDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI------RENIKNTHKI 225
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKCelqgtpREVFKEVETL 239
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-215 |
6.41e-35 |
|
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: 124.37 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 10 KSFGEDEYKT-EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNY-----RR 83
Cdd:cd03267 24 KSLFKRKYREvEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIgvvfgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGY---VFQMYNLISHLnveQNIDVGKYLSknplNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLL 160
Cdd:cd03267 104 TQLWWdlpVIDSFYLLAAI---YDLPPARFKK----RLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRL 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-224 |
7.30e-35 |
|
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: 124.19 E-value: 7.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYNLIShL 99
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 NVEQNIDVGKylskNPLNKEELLQTLGLKE-HRY--KQPN-----------QLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:cd03249 92 TIAENIRYGK----PDATDEEVEEAAKKANiHDFimSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 166 GALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDmADRVIYLHDGRIREniKNTHK 224
Cdd:cd03249 168 SALDAESEKLVQEALDRAMK--GRTTIVIAHRlSTIRN-ADLIAVLQNGQVVE--QGTHD 222
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-215 |
1.14e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 130.37 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyRRNhLGYVF 90
Cdd:TIGR03375 470 SFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL---RRN-IGYVP 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 QMYNLIsHLNVEQNIDVGkylskNPL-NKEELLQTL---GLKEHRYKQPN-----------QLSGGQQQRTSIGRAIIKN 155
Cdd:TIGR03375 546 QDPRLF-YGTLRDNIALG-----APYaDDEEILRAAelaGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRD 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:TIGR03375 620 PPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-217 |
4.27e-34 |
|
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: 121.95 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVF 90
Cdd:cd03254 9 NFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 QMYNLISHlNVEQNIDVGkylskNPLNKEE----LLQTLGLKEHRYKQPN-----------QLSGGQQQRTSIGRAIIKN 155
Cdd:cd03254 84 QDTFLFSG-TIMENIRLG-----RPNATDEevieAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-224 |
4.82e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 123.68 E-value: 4.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKekdltnyr 82
Cdd:COG4152 2 LELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYvfqM------YnlishlnveQNIDVG---------KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQR 145
Cdd:COG4152 70 RRRIGY---LpeerglY---------PKMKVGeqlvylarlKGLSKAEAKRraDEWLERLGLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 146 TSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIR-----ENI 219
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQmELVEELCDRIVIINKGRKVlsgsvDEI 216
|
....*
gi 1466369044 220 KNTHK 224
Cdd:COG4152 217 RRQFG 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-197 |
6.54e-34 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 122.12 E-value: 6.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyrrnhlGYVFQMYNLISHLN 100
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKD 175
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQrleiaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 1466369044 176 ILQLIEDVNKKYGNTIIIVTHN 197
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-215 |
1.13e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 121.34 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTnyrr 83
Cdd:COG4604 3 EIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQMYNLISHLNVEQNIDVGKY-LSKNPLNKE------ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:COG4604 75 KRLAILRQENHINSRLTVRELVAFGRFpYSKGRLTAEdreiidEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHdiNFASC-YADHIVAMKDGRV 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-215 |
3.29e-33 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 118.42 E-value: 3.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGED--EYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGG--IDQPDSGTITIQGKTIstlkekDL 78
Cdd:cd03213 4 LSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL------DK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 79 TNYRRnHLGYVFQMYNLISHLNVEQNIDVgkylsknplnkeellqTLGLKehrykqpnQLSGGQQQRTSIGRAIIKNPDL 158
Cdd:cd03213 78 RSFRK-IIGYVPQDDILHPTLTVRETLMF----------------AAKLR--------GLSGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 159 LLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTH--NDAIKDMADRVIYLHDGRI 215
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHqpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-217 |
3.37e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 120.02 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQ--PD---SGTITIQGKTISTLkekD 77
Cdd:PRK14247 4 IEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKM---D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRnHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNKEEL-------LQTLGLKEH---RYKQP-NQLSGGQQQRT 146
Cdd:PRK14247 77 VIELRR-RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELqervrwaLEKAQLWDEvkdRLDAPaGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 147 SIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYgnTIIIVTHNDA-IKDMADRVIYLHDGRIRE 217
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQqAARISDYVAFLYKGQIVE 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-210 |
1.21e-32 |
|
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: 123.55 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 18 KTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYNLIS 97
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HlNVEQNIDVGKYLSKNPLNKE--------ELLQTLGLKEHRY--KQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:TIGR02857 410 G-TIAENIRLARPDASDAEIREaleragldEFVAALPQGLDTPigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1466369044 168 LDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYL 210
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-216 |
1.46e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 120.75 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 34 ICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEK-DLTNYRRnHLGYVFQMYNLISHLNVEQNIDVGkYLS 112
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLPPEKR-RIGYVFQDARLFPHYKVRGNLRYG-MAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 113 KNPLNKEELLQTLGLkEH---RYkqPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGN 189
Cdd:PRK11144 104 SMVAQFDKIVALLGI-EPlldRY--PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINI 180
|
170 180
....*....|....*....|....*...
gi 1466369044 190 TIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:PRK11144 181 PILYVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-217 |
1.59e-32 |
|
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: 116.26 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdltnyr 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnhlgyvfQMYNLISHLNveqnidvgkylSKNPLNKEELLQTLGLkehrykqpnQLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:cd03247 72 --------ALSSLISVLN-----------QRPYLFDTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-217 |
2.53e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 123.01 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLkkSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyr 82
Cdd:PRK11160 339 LTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHlNVEQNIdvgkYLSKNPLNKEELLQTL---GLKEH---------------RykqpnQLSGGQQQ 144
Cdd:PRK11160 413 RQAISVVSQRVHLFSA-TLRDNL----LLAAPNASDEALIEVLqqvGLEKLleddkglnawlgeggR-----QLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 145 RTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDMaDRVIYLHDGRIRE 217
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRlTGLEQF-DRICVMDNGQIIE 553
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-218 |
3.76e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 122.76 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVF 90
Cdd:PRK13657 341 SFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 QMYNLISHlNVEQNIDVGKYLSKNplnkEELL--------------QTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:PRK13657 416 QDAGLFNR-SIEDNIRVGRPDATD----EEMRaaaeraqahdfierKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIREN 218
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVES 550
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-212 |
6.25e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 115.66 E-value: 6.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPD---SGTITIQGKTISTLkekdltNYRRNHLGYVFQMYNLISH 98
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL------PAEQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 LNVEQNI------DVGKYLSKNPLnkEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHT 172
Cdd:COG4136 91 LSVGENLafalppTIGRAQRRARV--EQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1466369044 173 SKDILQLIEDVNKKYGNTIIIVTH--NDAIKdmADRVIYLHD 212
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTHdeEDAPA--AGRVLDLGN 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-217 |
1.00e-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: 116.05 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLkekDLTNYRRnHLGYVFQMyNLISHL 99
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRR-QVGVVLQE-NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 NVEQNIDVGK-------------------YLSKNPLNKEELLQTLGLKehrykqpnqLSGGQQQRTSIGRAIIKNPDLLL 160
Cdd:cd03252 91 SIRDNIALADpgmsmervieaaklagahdFISELPEGYDTIVGEQGAG---------LSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-216 |
1.27e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.55 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEDEykteVLKGIDFEIEKGE-ICvLLGPSGSGKSTLLNIIGGIDQPDSGTITIQ-GKTISTLK-EKDLTNY 81
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDrIG-LVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLPqEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 R---------RNHLGYVFQMYNLISHLNVEQNIDVGKYLSKnpLNK-------------EELLQTLGLKEHRYKQP-NQL 138
Cdd:COG0488 76 LtvldtvldgDAELRALEAELEELEAKLAEPDEDLERLAEL--QEEfealggweaearaEEILSGLGFPEEDLDRPvSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 139 SGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTskdILQLiEDVNKKYGNTIIIVTHN----DAIkdmADRVIYLHDGR 214
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWL-EEFLKNYPGTVLVVSHDryflDRV---ATRILELDRGK 226
|
..
gi 1466369044 215 IR 216
Cdd:COG0488 227 LT 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-215 |
1.35e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.73 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 6 KDLKKSFGEDEYKTE--VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGktISTLKEKDLTNYRr 83
Cdd:PRK13633 8 KNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQMY-NLISHLNVEQNIDVG-KYLSKNPLN----KEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK13633 85 NKAGMVFQNPdNQIVATIVEEDVAFGpENLGIPPEEirerVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdmADRVIYLHDGRI 215
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHymEEAVE--ADRIIVMDSGKV 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-215 |
2.14e-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: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyRRNHLGYV---FQMYNLIS 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HLNVEQNIdvgkylsknplnkeellqTLglkehrykqPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDIL 177
Cdd:cd03215 92 DLSVAENI------------------AL---------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1466369044 178 QLIEDVNKKyGNTIIIV-THNDAIKDMADRVIYLHDGRI 215
Cdd:cd03215 145 RLIRELADA-GKAVLLIsSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-215 |
2.54e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 2.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEDEykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkeKDLTNYRR 83
Cdd:PRK13632 9 KVENVSFSYPNSE--NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS----KENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQMY-NLISHLNVEQNIDVG---KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK13632 83 KKIGIIFQNPdNQFIGATVEDDIAFGlenKKVPPKKMKDiiDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN--DAIKdmADRVIYLHDGRI 215
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDmdEAIL--ADKVIVFSEGKL 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-217 |
4.75e-31 |
|
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: 113.78 E-value: 4.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEDEYKT-EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtISTLKEkdltnyr 82
Cdd:cd03220 19 SLKKLGILGRKGEVGEfWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLG------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnhLGYVFQMynlisHLNVEQNI------------DVGKYLsknplnkEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGR 150
Cdd:cd03220 91 ---LGGGFNP-----ELTGRENIylngrllglsrkEIDEKI-------DEIIEFSELGDFIDLPVKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 151 AIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDpSSIKRLCDRALVLEKGKIRF 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-217 |
5.26e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.01 E-value: 5.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIqGKTIstlkekdltnyr 82
Cdd:COG0488 316 LELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnHLGYVFQMYnliSHLNVEQN-IDVGKYLSKNpLNKEELLQTLGL----KEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG0488 379 --KIGYFDQHQ---EELDPDKTvLDELRDGAPG-GTEQEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 158 LLLCDEPTGALDYHTskdiLQLIEDVNKKYGNTIIIVTHN----DAIkdmADRVIYLHDGRIRE 217
Cdd:COG0488 453 VLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDryflDRV---ATRILEFEDGGVRE 509
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-217 |
6.51e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.02 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEDEYKT-EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtISTLKEkdltnyr 82
Cdd:COG1134 23 SLKELLLRRRRTRREEfWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSALLE------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnhLGYVFQMynlisHLNVEQNID-VGKYLSknpLNKEELLQTL-------GLKEHRYkQP-NQLSGGQQQRTSIGRAII 153
Cdd:COG1134 95 ---LGAGFHP-----ELTGRENIYlNGRLLG---LSRKEIDEKFdeivefaELGDFID-QPvKTYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 154 KNPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSmGAVRRLCDRAIWLEKGRLVM 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-215 |
7.00e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.12 E-value: 7.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIS-TLKEKDLTNYRRnHLGYVFQM--YNLISH 98
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRK-KVGIVFQFpeHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 lNVEQNIDVGkylsknPLN-----------KEELLQTLGLKEH-RYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:PRK13634 102 -TVEKDICFG------PMNfgvseedakqkAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1466369044 167 ALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTV 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-215 |
8.80e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.45 E-value: 8.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEDeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRN 84
Cdd:PRK13647 7 VEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV----RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 HLGYVFQ-MYNLISHLNVEQNIDVGKY---LSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDL 158
Cdd:PRK13647 80 KVGLVFQdPDDQVFSSTVWDDVAFGPVnmgLDKDEVERrvEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 159 LLCDEPTGALDyHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK13647 160 IVLDEPMAYLD-PRGQETLMEILDRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGRV 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-210 |
1.13e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.94 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtistlkekdltnyRRnhLGYVFQMYNLISHL- 99
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-------------AR--VAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 -NVEQNIDVGKYLSKNPLNK---------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALD 169
Cdd:NF040873 72 lTVRDLVAMGRWARRGLWRRltrddraavDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1466369044 170 YHTSKDILQLIEDVNKKyGNTIIIVTHNDAIKDMADRVIYL 210
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-215 |
1.29e-30 |
|
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: 112.75 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPD---SGTITIQGKTIStlkeKDLT 79
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK----PDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 nyrRNHLGYVFQMYNLISHLNVEQNIdvgKYLSKNPL-------NKEELLQTLGLKE-------HRYKQpnQLSGGQQQR 145
Cdd:cd03234 80 ---QKCVAYVRQDDILLPGLTVRETL---TYTAILRLprkssdaIRKKRVEDVLLRDlaltrigGNLVK--GISGGERRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 146 TSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVT-HN--DAIKDMADRVIYLHDGRI 215
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR--RNRIVILTiHQprSDLFRLFDRILLLSSGEI 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-215 |
3.17e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 114.03 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 16 EYKT-EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkeKDLTNYRRNhLGYVF-QMY 93
Cdd:COG4586 31 EYREvEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF----KRRKEFARR-IGVVFgQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 94 NLISHLNVEQNIDVGK--Y-LSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGAL 168
Cdd:COG4586 106 QLWWDLPAIDSFRLLKaiYrIPDAEYKKrlDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1466369044 169 DYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDmDDIEALCDRVIVIDHGRI 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-215 |
5.55e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.59 E-value: 5.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYN-LISH 98
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV----RKFVGLVFQNPDdQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 LNVEQNIDVGkylsknPLNK-----------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:PRK13652 94 PTVEQDIAFG------PINLgldeetvahrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1466369044 168 LDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRI 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-213 |
4.92e-29 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 113.73 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 2 FLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTny 81
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 rRNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLN------------KEELLQTLGLKEHRYKQPNQLSGGQQQRTSIG 149
Cdd:PRK09700 79 -QLGIGIIYQELSVIDELTVLENLYIGRHLTKKVCGvniidwremrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 150 RAIIKNPDLLLCDEPTGALdyhTSKDILQLIEDVN--KKYGNTIIIVTHNDA-IKDMADRVIYLHDG 213
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNqlRKEGTAIVYISHKLAeIRRICDRYTVMKDG 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-215 |
5.20e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.43 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKT--EVLKGIDFE------------------IEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGT 62
Cdd:PRK10070 5 LEIKNLYKIFGEHPQRAfkYIEQGLSKEqilektglslgvkdaslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 63 ITIQGKTISTLKEKDLTNYRRNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNKE-----ELLQTLGLKEHRYKQPNQ 137
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERrekalDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 138 LSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEV 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-214 |
7.83e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.81 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGK--TISTLKEKdl 78
Cdd:COG3845 4 PALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 79 tnyRRNHLGYVFQMYNLISHLNVEQNI------DVGKYLSKNPLNKE--ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGR 150
Cdd:COG3845 78 ---IALGIGMVHQHFMLVPNLTVAENIvlglepTKGGRLDRKAARARirELSERYGLDVDPDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 151 AIIKNPDLLLCDEPTGALdyhTSKDILQLIEDVN--KKYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:COG3845 155 ALYRGARILILDEPTAVL---TPQEADELFEILRrlAAEGKSIIFITHKlREVMAIADRVTVLRRGK 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-215 |
8.56e-29 |
|
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: 107.94 E-value: 8.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 19 TEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnYRRNHLGYVFQMYNLISH 98
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK----YLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 lNVEQNIDVGkyLSKNPLNK-EELLQTLG------LKEHRY-----KQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:cd03248 103 -SLQDNIAYG--LQSCSFECvKEAAQKAHahsfisELASGYdtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1466369044 167 ALDYHTSKDILQLIEDVNKKygNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:cd03248 180 ALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-215 |
8.91e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 108.71 E-value: 8.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTN 80
Cdd:PRK13548 1 AMLEARNLSVRLG----GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YR-----RNHLGYVFqmynlishlNVEQNIDVGKY-LSKNPLNKEELLQT-------LGLKEHRYKqpnQLSGGQQQRTS 147
Cdd:PRK13548 77 RRavlpqHSSLSFPF---------TVEEVVAMGRApHGLSRAEDDALVAAalaqvdlAHLAGRDYP---QLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 148 IGRAI--IKNPD----LLLCDEPTGALD-YHtSKDILQLIEDVNKKYGNTIIIVTHndaikDM------ADRVIYLHDGR 214
Cdd:PRK13548 145 LARVLaqLWEPDgpprWLLLDEPTSALDlAH-QHHVLRLARQLAHERGLAVIVVLH-----DLnlaaryADRIVLLHQGR 218
|
.
gi 1466369044 215 I 215
Cdd:PRK13548 219 L 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-217 |
1.24e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.95 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 2 FLSIKDLkkSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTistLKEKDLTNY 81
Cdd:PRK13635 5 IIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 RRNhLGYVFQMY-NLISHLNVEQNIDVGkyLSKNPLNKEEL-------LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAII 153
Cdd:PRK13635 80 RRQ-VGMVFQNPdNQFVGATVQDDVAFG--LENIGVPREEMvervdqaLRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 154 KNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdmADRVIYLHDGRIRE 217
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHdlDEAAQ--ADRVIVMNKGEILE 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-217 |
3.04e-28 |
|
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: 106.42 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGE---ICvllGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYNLIS 97
Cdd:cd03244 19 VLKNISFSIKPGEkvgIV---GRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HlNVEQNIDvgkylsknPLNK---EELLQTL---GLKEHRYKQP-----------NQLSGGQQQRTSIGRAIIKNPDLLL 160
Cdd:cd03244 92 G-TIRSNLD--------PFGEysdEELWQALervGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDMaDRVIYLHDGRIRE 217
Cdd:cd03244 163 LDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRlDTIIDS-DRILVLDKGRVVE 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-215 |
6.21e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.51 E-value: 6.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI-STLKEKDLTNYRRNhLGYVFQM-YN 94
Cdd:PRK13643 17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsSTSKQKEIKPVRKK-VGVVFQFpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LISHLNVEQNIDVGKY---LSKNPLNK--EELLQTLGL-KEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGAL 168
Cdd:PRK13643 96 QLFEETVLKDVAFGPQnfgIPKEKAEKiaAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1466369044 169 DYHTSKDILQLIEDVNKKyGNTIIIVTH-NDAIKDMADRVIYLHDGRI 215
Cdd:PRK13643 176 DPKARIEMMQLFESIHQS-GQTVVLVTHlMDDVADYADYVYLLEKGHI 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-217 |
1.23e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.69 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGI-----DQPDSGTITIQGKTISTlKEKDLTNYRRnHLGYVFQMYN 94
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVRR-EVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LISHLNVEQNIDVGKYLSKNPLNKEEL-------LQTLGL----KEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDE 163
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGLVKSKKELdervewaLKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 164 PTGALDYHTSKDILQLIEDVNKKYgnTIIIVTHNDA-IKDMADRVIYLHDGRIRE 217
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAqAARVSDYVAFLYLGKLIE 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-217 |
1.46e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.41 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKST----LLNIIggidqPDSGTITIQGKTISTLKEKDLTNYRRnHLGYVFQMYN-- 94
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LISHLNVEQNIDVGKYLSKNPLNKEE-------LLQTLGLK-EHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTLSAAQreqqviaVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 167 ALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDlHVVRALCHQVIVLRQGEVVE 506
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-224 |
1.54e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.81 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnYRRNHLGYVFQMYNLISHlN 100
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH----YLHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNIDVGkyLSKNPlnKEELLQT---------LGLKEHRY-----KQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:TIGR00958 571 VRENIAYG--LTDTP--DEEIMAAakaanahdfIMEFPNGYdtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 167 ALDyhtsKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIREniKNTHK 224
Cdd:TIGR00958 647 ALD----AECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE--MGTHK 698
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-215 |
1.68e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEDEYKTeVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTistLKEKDLTNYRRn 84
Cdd:PRK13650 7 VKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIRH- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 HLGYVFQMY-NLISHLNVEQNIDVG---KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDL 158
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGlenKGIPHEEMKErvNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 159 LLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-217 |
2.10e-27 |
|
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: 109.52 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVF 90
Cdd:COG5265 364 SFGYDP-ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 Q---------MYNLI------SHLNVEQNID---VGKYLSKNPlnkeELLQTL----GLKehrykqpnqLSGGQQQRTSI 148
Cdd:COG5265 439 QdtvlfndtiAYNIAygrpdaSEEEVEAAARaaqIHDFIESLP----DGYDTRvgerGLK---------LSGGEKQRVAI 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 149 GRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDmADRVIYLHDGRIRE 217
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRlSTIVD-ADEILVLEAGRIVE 572
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-216 |
2.21e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.20 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYR 82
Cdd:COG4559 2 LEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 ---RNHlgyvfqmynliSHLN----VEQNIDVGKY--LSKNPLNKEELLQTL------GLKEHRYkqpNQLSGGQQQRTS 147
Cdd:COG4559 78 avlPQH-----------SSLAfpftVEEVVALGRAphGSSAAQDRQIVREALalvglaHLAGRSY---QTLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 148 IGRAI--IKNPD-----LLLCDEPTGALD-YHTSkDILQLIEDVNKKyGNTIIIVTHndaikDM------ADRVIYLHDG 213
Cdd:COG4559 144 LARVLaqLWEPVdggprWLFLDEPTSALDlAHQH-AVLRLARQLARR-GGGVVAVLH-----DLnlaaqyADRILLLHQG 216
|
...
gi 1466369044 214 RIR 216
Cdd:COG4559 217 RLV 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-232 |
2.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.68 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI-STLKEKDLTNYRRNhLGYVFQM-YN 94
Cdd:PRK13641 18 MEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKK-VSLVFQFpEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LISHLNVEQNIDVGkylsknPLN--------KEELLQTL---GLKEHRY-KQPNQLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:PRK13641 97 QLFENTVLKDVEFG------PKNfgfsedeaKEKALKWLkkvGLSEDLIsKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIrenIKntHKIPA---KDLNW 232
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHGKL---IK--HASPKeifSDKEW 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-215 |
3.84e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSG-TITIQGKTISTLKEKDLTNYRRNHLGYVFQM--Y 93
Cdd:PRK13645 22 FEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKIKEVKRLRKEIGLVFQFpeY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 94 NLISHlNVEQNIDVGKY---LSKNPLNKE--ELLQTLGL-KEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVnlgENKQEAYKKvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1466369044 168 LDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-197 |
7.14e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 104.08 E-value: 7.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRNhLGYVFQMYNLISHLNVEQN 104
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 105 idVGKYLSKNPLNKEELLQT--------LGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDI 176
Cdd:PRK11831 105 --VAYPLREHTQLPAPLLHStvmmkleaVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180
....*....|....*....|.
gi 1466369044 177 LQLIEDVNKKYGNTIIIVTHN 197
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHD 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-215 |
8.19e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 107.62 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIdQPDSGTITIQGKTistLKEKDLTNYRRnHLGYVFQMYNLIsHLNVEQN 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIE---LRELDPESWRK-HLSWVGQNPQLP-HGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 105 IdvgkYLSKNPLNKEELLQTL---GLKEHRYKQPN-----------QLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDY 170
Cdd:PRK11174 443 V----LLGNPDASDEQLQQALenaWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1466369044 171 HTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDMaDRVIYLHDGRI 215
Cdd:PRK11174 519 HSEQLVMQALNAASR--RQTTLMVTHQlEDLAQW-DQIWVMQDGQI 561
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-214 |
8.72e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.50 E-value: 8.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkekdLTNYR 82
Cdd:PRK13537 8 IDFRNVEKRYGD----KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-----RARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDV-GKYLSKNPLNKEELLQTL----GLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVfGRYFGLSAAAARALVPPLlefaKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTH-NDAIKDMADRVIYLHDGR 214
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHfMEEAERLCDRLCVIEEGR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-217 |
9.27e-27 |
|
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: 107.20 E-value: 9.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQ--PDSGTITIQ-------------- 66
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 67 ---------GKTIsTLKEKDLTN----YRRN-------HLGYVFQMY-------NLISHLNveqniDVGkYLSKNPLNKE 119
Cdd:TIGR03269 77 kvgepcpvcGGTL-EPEEVDFWNlsdkLRRRirkriaiMLQRTFALYgddtvldNVLEALE-----EIG-YEGKEAVGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 120 -ELLQTLGLkEHRYKQ-PNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH- 196
Cdd:TIGR03269 150 vDLIEMVQL-SHRITHiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHw 228
|
250 260
....*....|....*....|.
gi 1466369044 197 NDAIKDMADRVIYLHDGRIRE 217
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKE 249
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
1.30e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.77 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 19 TEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStLKEKDLTNYRRNhLGYVFQMY-NLIS 97
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRES-VGMVFQDPdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HLNVEQNIDVGKY---LSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHT 172
Cdd:PRK13636 97 SASVYQDVSFGAVnlkLPEDEVRKrvDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1466369044 173 SKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRV 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-215 |
1.41e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 106.67 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYR 82
Cdd:PRK15439 12 LCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-----RLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLG-Y-VFQMYNLISHLNVEQNIDVGkyLSKNPLNK---EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK15439 83 AHQLGiYlVPQEPLLFPNLSVKENILFG--LPKRQASMqkmKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKlPEIRQLADRISVMRDGTI 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-216 |
1.73e-26 |
|
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: 106.76 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQmynlishlN 100
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL----GRHIGYLPQ--------D 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VE-------QNI----DVgkylsknplNKEELL---QTLGLKE------HRYKQP-----NQLSGGQQQRTSIGRAIIKN 155
Cdd:COG4618 415 VElfdgtiaENIarfgDA---------DPEKVVaaaKLAGVHEmilrlpDGYDTRigeggARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIR 216
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-217 |
2.95e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.51 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 7 DLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI---STLKEKDltnyRR 83
Cdd:PRK11308 16 PVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKL----LR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQmyNLISHLNVEQNidVGKYLSK-----NPLNKEE-------LLQTLGLK-EH--RYkqPNQLSGGQQQRTSI 148
Cdd:PRK11308 92 QKIQIVFQ--NPYGSLNPRKK--VGQILEEpllinTSLSAAErrekalaMMAKVGLRpEHydRY--PHMFSGGQRQRIAI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 149 GRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDA-IKDMADRVIYLHDGRIRE 217
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSvVEHIADEVMVMYLGRCVE 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-214 |
3.15e-26 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 100.62 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTE-VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtistlkekdltny 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 rrnhLGYVFQmYNLISHLNVEQNIDVGKylsknPLNKEELLQTL---GLKEHRYKQPNQ-----------LSGGQQQRTS 147
Cdd:cd03250 68 ----IAYVSQ-EPWIQNGTIRENILFGK-----PFDEERYEKVIkacALEPDLEILPDGdlteigekginLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 148 IGRAIIKNPDLLLCDEPTGALDYHTSKDIlqlIEDV---NKKYGNTIIIVTHNDAIKDMADRVIYLHDGR 214
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHI---FENCilgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-218 |
4.08e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.56 E-value: 4.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKS-TLLNIIGGIDQPD----SGTITIQGKTISTLKEKD 77
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRNHLGYVFQ--MYNLISHLNVEQNI----DVGKYLSKNPLNKEEL--LQTLGLKE--HRYKQ-PNQLSGGQQQRT 146
Cdd:PRK15134 86 LRGVRGNKIAMIFQepMVSLNPLHTLEKQLyevlSLHRGMRREAARGEILncLDRVGIRQaaKRLTDyPHQLSGGERQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 147 SIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAI-KDMADRVIYLHDGRIREN 218
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIvRKLADRVAVMQNGRCVEQ 238
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-214 |
4.33e-26 |
|
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: 98.67 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITiqgkTISTLKekdltnyr 82
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT----WGSTVK-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnhLGYVfqmynlishlnveqnidvgkylsknplnkeellqtlglkehrykqpNQLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:cd03221 65 ---IGYF----------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 163 EPTGALDYHTskdiLQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:cd03221 96 EPTNHLDLES----IEALEEALKEYPGTVILVSHDrYFLDQVATKIIELEDGK 144
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-216 |
4.92e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.15 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTn 80
Cdd:PRK09536 2 PMIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 yRRnhLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNK---------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRA 151
Cdd:PRK09536 77 -RR--VASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTwtetdraavERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 152 IIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNdaiKDMA----DRVIYLHDGRIR 216
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHD---LDLAarycDELVLLADGRVR 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-215 |
5.51e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.11 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTnyr 82
Cdd:PRK11614 6 LSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNPLNKEELLQTLG----LKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDL 158
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYElfprLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 159 LLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQnaNQALK-LADRGYVLENGHV 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
19-217 |
8.57e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 8.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 19 TEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltNYRRnHLGYVFQMYNLISH 98
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQ-QVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 lNVEQNIDVGKYLSKNPLNKEELLQTL---GLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSK 174
Cdd:PRK10247 96 -TVYDNLIFPWQIRNQQPDPAIFLDDLerfALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1466369044 175 DILQLIEDVNKKYGNTIIIVTHN-DAIKDmADRVIYL--HDGRIRE 217
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDkDEINH-ADKVITLqpHAGEMQE 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-215 |
1.02e-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: 104.35 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 18 KTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtistlkekDLTNYRRN----HLGYVFQMY 93
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGA--------DLKQWDREtfgkHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 94 NLISHlNVEQNIdvgKYLSKNPLNKE--ELLQTLGLKEHRYKQPN-----------QLSGGQQQRTSIGRAIIKNPDLLL 160
Cdd:TIGR01842 402 ELFPG-TVAENI---ARFGENADPEKiiEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.52e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.32 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGED-EYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITI-----QGKTISTLK 74
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 75 EKDL-------TNYR--------RNHLGYVFQM--YNLISHlNVEQNIDVGKY---LSKNPLNK--EELLQTLGLKE-HR 131
Cdd:PRK13651 81 EKVLeklviqkTRFKkikkikeiRRRVGVVFQFaeYQLFEQ-TIEKDIIFGPVsmgVSKEEAKKraAKYIELVGLDEsYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 132 YKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYL 210
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTIFF 238
|
250
....*....|....*..
gi 1466369044 211 HDGRIrenIK--NTHKI 225
Cdd:PRK13651 239 KDGKI---IKdgDTYDI 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-215 |
1.62e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIstlkekDLTNYR---RNHLGYV---FQMY 93
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV------RIRSPRdaiRAGIAYVpedRKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 94 NLISHLNVEQNI---DVGKYLSKNPLNK-------EELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:COG1129 340 GLVLDLSIRENItlaSLDRLSRGGLLDRrreralaEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVNKKyGNTIIIVThNDA--IKDMADRVIYLHDGRI 215
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAE-GKAVIVIS-SELpeLLGLSDRILVMREGRI 472
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-214 |
2.08e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 7 DLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYRRNHL 86
Cdd:PRK13536 46 GVSKSYGD----KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-----ARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 87 GYVFQMYNLISHLNVEQNIDV-GKYLSKNPLNKEE----LLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLC 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVfGRYFGMSTREIEAvipsLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 162 DEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTH-NDAIKDMADRVIYLHDGR 214
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHfMEEAERLCDRLCVLEAGR 249
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-215 |
2.31e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 99.37 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGID--QPDSGTITIQGKTIStlkekDLTN 80
Cdd:COG0396 1 LEIKNLHVSVEG----KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDIL-----ELSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRRNHLG--YVFQ---------MYNLishLNVEQNIDVGKYLSKNPLNKE--ELLQTLGLKE---HRYKqpNQ-LSGGQQ 143
Cdd:COG0396 72 DERARAGifLAFQypveipgvsVSNF---LRTALNARRGEELSAREFLKLlkEKMKELGLDEdflDRYV--NEgFSGGEK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 144 QRTSIGRAIIKNPDLLLCDEPTGALDYhtskDILQLIEDVNKKY---GNTIIIVTHNDAIKDM--ADRVIYLHDGRI 215
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDI----DALRIVAEGVNKLrspDRGILIITHYQRILDYikPDFVHVLVDGRI 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-214 |
3.56e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekDLTNYR 82
Cdd:PRK11300 6 LSVSGLMMRFG----GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-----GLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYV--FQMYNLISHLNVEQNIDVGKY----------LSKNP----LNKEEL------LQTLGLKEHRYKQPNQLSG 140
Cdd:PRK11300 77 IARMGVVrtFQHVRLFREMTVIENLLVAQHqqlktglfsgLLKTPafrrAESEALdraatwLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 141 GQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHndaikDM------ADRVIYLHDGR 214
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH-----DMklvmgiSDRIYVVNQGT 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-217 |
3.93e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.35 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEK---DLTNYRRnHLGYVFQMYNLIS 97
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqiDAIKLRK-EVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HLNVEQNI----DVGKYLSKNPLNK--EELLQTLGLKEHRYKQPN----QLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:PRK14246 104 HLSIYDNIayplKSHGIKEKREIKKivEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 168 LDYHTSKDILQLIEDVNKKYgnTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNpQQVARVADYVAFLYNGELVE 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-217 |
4.54e-25 |
|
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: 98.75 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITI-----QGKTISTLKEKD 77
Cdd:TIGR02323 4 LQVSGLSKSYG----GGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRNHLGYVFQ------MYNLISHLNV-EQNIDVG-KYLSKNPLNKEELLQTLGLKEHRYK-QPNQLSGGQQQRTSI 148
Cdd:TIGR02323 80 RRRLMRTEWGFVHQnprdglRMRVSAGANIgERLMAIGaRHYGNIRATAQDWLEEVEIDPTRIDdLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 149 GRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAI-KDMADRVIYLHDGRIRE 217
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVaRLLAQRLLVMQQGRVVE 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
5.62e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.64 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTN 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRV----LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YrrnhLGYVFQMYNlisHLNVEQNIDV-GKYLSKNPLNKEELLQTLGLK--EHRykQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK13539 77 Y----LGHRNAMKP---ALTVAENLEFwAAFLGGEELDIAAALEAVGLAplAHL--PFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHND 198
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQ-GGIVIAATHIP 187
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-215 |
7.32e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI-STLKEKDLTNYRRnHLGYVFQMYNliSHLN 100
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRK-KVGLVFQFPE--SQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VE----------QNIDVGKylSKNPLNKEELLQTLGLKEHRY-KQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALD 169
Cdd:PRK13649 100 EEtvlkdvafgpQNFGVSQ--EEAEALAREKLALVGISESLFeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1466369044 170 YHTSKDILQLIEDVNKKyGNTIIIVTH-NDAIKDMADRVIYLHDGRI 215
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHlMDDVANYADFVYVLEKGKL 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-215 |
9.87e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTn 80
Cdd:PRK11231 1 MTLRTENLTVGYG----TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 yrrNHLGYVFQmynlisHLNVEQNIDVGKYLS--KNP-------LNKE---------ELLQTLGLKEHRYkqpNQLSGGQ 142
Cdd:PRK11231 76 ---RRLALLPQ------HHLTPEGITVRELVAygRSPwlslwgrLSAEdnarvnqamEQTRINHLADRRL---TDLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 143 QQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHdlNQASR-YCDHLVVLANGHV 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-215 |
1.27e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQmynlishlNV 101
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQ--------NP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQNI-------DVGKYLSKNPLNKEEL-------LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:PRK13648 93 DNQFvgsivkyDVAFGLENHAVPYDEMhrrvseaLKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1466369044 168 LDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-217 |
1.41e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.03 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKS-TLLNIIG-----GIDqpdSGTITIQGKTISTLKEK 76
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGllaanGRI---GGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 77 DLTNYRRNHLGYVFQ--MYNLISHLNV-EQNIDV---GKYLSKNPLNKE--ELLQTLGLKEHRYKQ---PNQLSGGQQQR 145
Cdd:PRK09473 90 ELNKLRAEQISMIFQdpMTSLNPYMRVgEQLMEVlmlHKGMSKAEAFEEsvRMLDAVKMPEARKRMkmyPHEFSGGMRQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 146 TSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGRTME 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-215 |
1.48e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 101.03 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSF-GEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQ-GKTISTLKEKDLTN 80
Cdd:TIGR03269 280 IKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRR--NHLGYVFQMYNLISHLNVEQN------IDVGKYLSKnpLNKEELLQTLGLKEHRY-----KQPNQLSGGQQQRTS 147
Cdd:TIGR03269 360 RGRakRYIGILHQEYDLYPHRTVLDNlteaigLELPDELAR--MKAVITLKMVGFDEEKAeeildKYPDELSEGERHRVA 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 148 IGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-217 |
2.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTI-STLKEKDLTNYRRNhLGYVFQMYNl 95
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRKR-IGMVFQFPE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 96 iSHL---NVEQNIDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQ-PNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:PRK13646 96 -SQLfedTVEREIIFGPKNFKMNLDEvknyaHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 167 ALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
11-215 |
2.39e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.56 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDS---GTITIQGktiSTLKEKDLTNYRrNHLG 87
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG---ITLTAKTVWDIR-EKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 88 YVFQMY-NLISHLNVEQNIDVG---KYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLC 161
Cdd:PRK13640 88 IVFQNPdNQFVGATVGDDVAFGlenRAVPRPEMIKivRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 162 DEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
12-217 |
2.82e-24 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 100.59 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 12 FGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLkekDLTNYRRNhLGYVFQ 91
Cdd:TIGR01846 463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA---DPAWLRRQ-MGVVLQ 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 92 MYNLISHlNVEQNIDvgkyLSKNPLNKEELLQT----------LGLKeHRYKQP-----NQLSGGQQQRTSIGRAIIKNP 156
Cdd:TIGR01846 539 ENVLFSR-SIRDNIA----LCNPGAPFEHVIHAaklagahdfiSELP-QGYNTEvgekgANLSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-198 |
3.16e-24 |
|
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: 95.12 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnyR 82
Cdd:TIGR01189 1 LAARNLACSRGERM----LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDV-GKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLC 161
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALENLHFwAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1466369044 162 DEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHND 198
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLAR-GGIVLLTTHQD 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-215 |
3.89e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.12 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPD---SGTITIQGKTIsTLKEKdltnyrRNHLGYVFQMYNLI 96
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEM------RAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 97 SHLNVEQNIDVGKYLS-KNPLNK-------EELLQTLGLK---EHRYKQPNQ---LSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRmPRRVTKkekrervDEVLQALGLRkcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDA--IKDMADRVIYLHDGRI 215
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPSseLFELFDKIILMAEGRV 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-216 |
5.31e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.59 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 19 TEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGktISTLKEKDLTNYRRnHLGYVFQmyNLISH 98
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRK-LVGIVFQ--NPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 L---NVEQNIDVG-KYLSKNPLNKEEL----LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDY 170
Cdd:PRK13644 90 FvgrTVEEDLAFGpENLCLPPIEIRKRvdraLAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1466369044 171 HTSKDILQLIEDVNKKyGNTIIIVTHNDAIKDMADRVIYLHDGRIR 216
Cdd:PRK13644 170 DSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-215 |
1.01e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 94.13 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGID--QPDSGTITIQGKTIstlkeKDLTN 80
Cdd:cd03217 1 LEIKDLHVSVGG----KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDI-----TDLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRRNHLG--YVFQMYNLISHLNVEQ---NIDVGkylsknplnkeellqtlglkehrykqpnqLSGGQQQRTSIGRAIIKN 155
Cdd:cd03217 72 EERARLGifLAFQYPPEIPGVKNADflrYVNEG-----------------------------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 156 PDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDAIKDM--ADRVIYLHDGRI 215
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYikPDRVHVLYDGRI 183
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
2.86e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGED-EYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQ----------GKTIS 71
Cdd:PRK13631 22 LRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 72 TLKEKDLTNYR--RNHLGYVFQM--YNLISHlNVEQNIDVGKY---LSKNPLNK--EELLQTLGLKE-HRYKQPNQLSGG 141
Cdd:PRK13631 102 NPYSKKIKNFKelRRRVSMVFQFpeYQLFKD-TIEKDIMFGPValgVKKSEAKKlaKFYLNKMGLDDsYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 142 QQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDvNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-217 |
3.91e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.23 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKST----LLNIIggidQPDSGTITIQGKTISTLKEKDLTNYRRNhLGYVFQ--------- 91
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTtgraLLRLV----ESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQdpyasldpr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 92 ---MYNLISHLNVEQNIDvGKYLSKNplnKEELLQTLGLK-EHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:PRK10261 418 qtvGDSIMEPLRVHGLLP-GKAAAAR---VAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 168 LDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKD-MADRVIYLHDGRIRE 217
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVErISHRVAVMYLGQIVE 544
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-217 |
7.07e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.39 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSF---GEDEY---KTEVLK---GIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTL 73
Cdd:PRK15079 9 LEVADLKVHFdikDGKQWfwqPPKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 74 KEKDLTNyRRNHLGYVFQmyNLISHLNVEQNIdvGKYLSKnPL-------NKEE-------LLQTLGLKEH---RYkqPN 136
Cdd:PRK15079 89 KDDEWRA-VRSDIQMIFQ--DPLASLNPRMTI--GEIIAE-PLrtyhpklSRQEvkdrvkaMMLKVGLLPNlinRY--PH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 137 QLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAI-KDMADRVIYLHDGRI 215
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVvKHISDRVLVMYLGHA 240
|
..
gi 1466369044 216 RE 217
Cdd:PRK15079 241 VE 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-213 |
7.57e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 92.33 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 7 DLKKSFG--EDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGI--DQPDSGTITIQGKTIStlkekdltnyr 82
Cdd:COG2401 29 IVLEAFGveLRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDNQFG----------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnhlgyvfQMYNLISHLnveqnidvgkYLSKNPLNKEELLQTLGLKE-----HRYKqpnQLSGGQQQRTSIGRAIIKNPD 157
Cdd:COG2401 98 --------REASLIDAI----------GRKGDFKDAVELLNAVGLSDavlwlRRFK---ELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVT-HNDAIKDMA-DRVIYLHDG 213
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVAThHYDVIDDLQpDLLIFVGYG 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-197 |
8.08e-23 |
|
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: 95.89 E-value: 8.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEyktEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyr 82
Cdd:TIGR02868 335 LELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLIsHLNVEQNIDVGkylsKNPLNKEELLQTL---GLKEHRYKQPN-----------QLSGGQQQRTSI 148
Cdd:TIGR02868 408 RRRVSVCAQDAHLF-DTTVRENLRLA----RPDATDEELWAALervGLADWLRALPDgldtvlgeggaRLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1466369044 149 GRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN 197
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-225 |
9.69e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 9.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGedeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQ--PD---SGTITIQGKTISTLKEKd 77
Cdd:PRK14239 6 LQVSDLSVYYN----KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 lTNYRRNHLGYVFQMYNLIShLNVEQNIDVGKYLS----KNPLNK--EELLQTLGL----KEHRYKQPNQLSGGQQQRTS 147
Cdd:PRK14239 81 -TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKgikdKQVLDEavEKSLKGASIwdevKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 148 IGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYgnTIIIVTHN-DAIKDMADRVIYLHDGRIREnIKNTHKI 225
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSmQQASRISDRTGFFLDGDLIE-YNDTKQM 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-217 |
1.25e-22 |
|
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: 91.32 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyr 82
Cdd:cd03369 7 IEVENLSVRYAPD--LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHlNVEQNIDV-GKYlsknplNKEELLQTLGLKEhrykQPNQLSGGQQQRTSIGRAIIKNPDLLLC 161
Cdd:cd03369 81 RSSLTIIPQDPTLFSG-TIRSNLDPfDEY------SDEEIYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 162 DEPTGALDYHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDMaDRVIYLHDGRIRE 217
Cdd:cd03369 150 DEATASIDYATDALIQKTIREEFT--NSTILTIAHRlRTIIDY-DKILVMDAGEVKE 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
14-215 |
1.43e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.85 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 14 EDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkeKDLTNYRRNhLGYVFQMY 93
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRK-IGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 94 -NLISHLNVEQNIDVGkyLSKNPLNKEELLQ-------TLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:PRK13642 91 dNQFVGATVEDDVAFG--MENQGIPREEMIKrvdeallAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDEST 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1466369044 166 GALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-217 |
1.73e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 95.04 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkEKDLTNYRRnHLGYVFQMYNLISHLNV 101
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRK-LFSAVFTDFHLFDQLLG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQNIDVGKYLSKNPLNKEELLQTLGLKEHRYKQPnQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIE 181
Cdd:PRK10522 415 PEGKPANPALVEKWLERLKMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLL 493
|
170 180 190
....*....|....*....|....*....|....*.
gi 1466369044 182 DVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:PRK10522 494 PLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-217 |
2.96e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.53 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeyktevLKG---IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLT 79
Cdd:PRK11701 7 LSVRGLTKLYGP-------RKGcrdVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 NYRRNHL-----GYVFQ--MYNLisHLNVEQNIDVGkylsknplnkeELLQTLGLKEH---RYK---------------- 133
Cdd:PRK11701 80 EAERRRLlrtewGFVHQhpRDGL--RMQVSAGGNIG-----------ERLMAVGARHYgdiRATagdwlerveidaarid 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 134 -QPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAI-KDMADRVIYLH 211
Cdd:PRK11701 147 dLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVaRLLAHRLLVMK 226
|
....*.
gi 1466369044 212 DGRIRE 217
Cdd:PRK11701 227 QGRVVE 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-215 |
5.48e-22 |
|
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: 94.31 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFgeDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkekDLTNYRRN 84
Cdd:TIGR01257 931 VKNLVKIF--EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 hLGYVFQMYNLISHLNVEQNIDV-----GKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLL 159
Cdd:TIGR01257 1005 -LGMCPQHNILFHHLTVAEHILFyaqlkGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 160 LCDEPTGALDYHTSKDILQLIedVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHmDEADLLGDRIAIISQGRL 1138
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-223 |
6.80e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 91.73 E-value: 6.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKS-TLLNIIGGIDQPD---SGTITIQGKTISTLKEKDl 78
Cdd:PRK11022 4 LNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGrvmAEKLEFNGQDLQRISEKE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 79 tnyRRNHLG----YVFQ--M----------YNLISHLNVEQnidvGKYLSKNPLNKEELLQTLGLKEHRYK---QPNQLS 139
Cdd:PRK11022 83 ---RRNLVGaevaMIFQdpMtslnpcytvgFQIMEAIKVHQ----GGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 140 GGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDA-IKDMADRVIYLHDGRIREN 218
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVET 235
|
....*
gi 1466369044 219 IKNTH 223
Cdd:PRK11022 236 GKAHD 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-215 |
1.06e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.90 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIdQPDSGTITIQGKTISTLKEKDLTNYRrnhlGY-------VFQM-- 92
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYlsqqqspPFAMpv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 93 YNLIS-----HLNVEQNIDVgkylsknpLNkeELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIK-----NPD--LLL 160
Cdd:COG4138 87 FQYLAlhqpaGASSEAVEQL--------LA--QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPEgqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 161 CDEPTGALDYHTSKDILQLIedvnKKY---GNTIIIVTH--NDAIKDmADRVIYLHDGRI 215
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLL----RELcqqGITVVMSSHdlNHTLRH-ADRVWLLKQGKL 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-197 |
1.17e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.23 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLL-------NIIGGIDQpdSGTITIQGKTISTlKEKDLTNYRRnHLGYVFQMYN 94
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLYA-PDVDPVEVRR-RIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LISHlNVEQNIDVGKYLSKNPLNKEELLQTlGLKE--------HRYKQPNQ-LSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGYKGDMDELVER-SLRQaalwdevkDKLKQSGLsLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|..
gi 1466369044 166 GALDYHTSKDILQLIEDVNKKYgnTIIIVTHN 197
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHN 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-215 |
1.48e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 32 GEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNyrrnHLGYVFQMYNLISHLNVEQNIDVGKYL 111
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQLPAAEGMTVRELVAIGRYP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 112 SKNPLNK---------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIED 182
Cdd:PRK10575 113 WHGALGRfgaadrekvEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR 192
|
170 180 190
....*....|....*....|....*....|....*..
gi 1466369044 183 VNKKYGNTIIIVTHNdaiKDMA----DRVIYLHDGRI 215
Cdd:PRK10575 193 LSQERGLTVIAVLHD---INMAarycDYLVALRGGEM 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-215 |
1.57e-21 |
|
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: 88.47 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPD---SGTITIQGKTIstlkeKD 77
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-----KE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRNHLGYVFQMYNLISHLNVEQNIDVgkylsknplnkeellqTLGLKEHRYKQpnQLSGGQQQRTSIGRAIIKNPD 157
Cdd:cd03233 77 FAEKYPGEIIYVSEEDVHFPTLTVRETLDF----------------ALRCKGNEFVR--GISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKDMADRVIYLHDGRI 215
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGRQ 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-217 |
1.84e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.46 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 1 MFLSIKDLKKSFgedEYKT--------EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTist 72
Cdd:PRK15112 3 TLLEVRNLSKTF---RYRTgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 73 LKEKDLTnYRRNHLGYVFQmyNLISHLNVEQNI----DVGKYLSK--NPLNKEE-LLQTLG----LKEHRYKQPNQLSGG 141
Cdd:PRK15112 77 LHFGDYS-YRSQRIRMIFQ--DPSTSLNPRQRIsqilDFPLRLNTdlEPEQREKqIIETLRqvglLPDHASYYPHMLAPG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 142 QQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVT-HNDAIKDMADRVIYLHDGRIRE 217
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEVVE 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-197 |
1.88e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.18 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKekdLTNYRRNHLGYVFQMYNLISHLN 100
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNI----DVGKYLSKNPLNK--EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSK 174
Cdd:PRK10895 95 VYDNLmavlQIRDDLSAEQREDraNELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180
....*....|....*....|...
gi 1466369044 175 DILQLIEDVnKKYGNTIIIVTHN 197
Cdd:PRK10895 175 DIKRIIEHL-RDSGLGVLITDHN 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-217 |
1.92e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.23 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKS-TLLNIIGGIDQP----DSGTITIQGKT-----IST 72
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSrqvieLSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 73 LKEKDLTNYRRNHLGYVFQ--MYNLISHLNVEQNIDVGKYLSKNPLNKEELLQTLGLKEH-----------RYkqPNQLS 139
Cdd:PRK10261 93 QSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQvripeaqtilsRY--PHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 140 GGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGEAVE 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-214 |
2.01e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.91 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIdQPD---SGTITIQGKtisTLKEKDLT 79
Cdd:PRK13549 6 LEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGE---ELQASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 NYRRNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNP--------LNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRA 151
Cdd:PRK13549 78 DTERAGIAIIHQELALVKELSVLENIFLGNEITPGGimdydamyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 152 IIKNPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-214 |
2.23e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGktistlKEKDLTNYRRN-HLGY--VFQMYNLISH 98
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG------QEMRFASTTAAlAAGVaiIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 LNVEQNIdvgkYLSKNP-----LNKEEL-------LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:PRK11288 94 MTVAENL----YLGQLPhkggiVNRRLLnyeareqLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1466369044 167 ALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:PRK11288 170 SLSAREIEQLFRVIREL-RAEGRVILYVSHRmEEIFALCDAITVFKDGR 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
5-208 |
8.02e-21 |
|
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: 87.46 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEDEYKTEVLKGidfEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekdltnYRRN 84
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 HLGYVFQM--YNLIShlnveqNIDVGKYLSknPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:cd03237 69 YIKADYEGtvRDLLS------SITKDFYTH--PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 163 EPTGALD----YHTSKDILQLIEDVNKkygnTIIIVTHNDAIKDM-ADRVI 208
Cdd:cd03237 141 EPSAYLDveqrLMASKVIRRFAENNEK----TAFVVEHDIIMIDYlADRLI 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-197 |
9.34e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTistlkekdltnyr 82
Cdd:PRK09544 5 VSLENVSVSFGQ----RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnHLGYVFQMYnlisHLNVEQNIDVGKYLSKNP-LNKEELLQTLGL--KEHRYKQPNQ-LSGGQQQRTSIGRAIIKNPDL 158
Cdd:PRK09544 68 --RIGYVPQKL----YLDTTLPLTVNRFLRLRPgTKKEDILPALKRvqAGHLIDAPMQkLSGGETQRVLLARALLNRPQL 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 1466369044 159 LLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN 197
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
9.52e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 9.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLkksFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyR 82
Cdd:COG3845 258 LEVENL---SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER---R 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYV---FQMYNLISHLNVEQNIDVGKYlSKNPLNKEELLQTLGLKEH----------RYKQPNQ----LSGGQQQR 145
Cdd:COG3845 332 RLGVAYIpedRLGRGLVPDMSVAENLILGRY-RRPPFSRGGFLDRKAIRAFaeelieefdvRTPGPDTparsLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 146 TSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDlDEILALSDRIAVMYEGRI 480
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-216 |
2.87e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.24 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEYKteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDsGTITIQGKTI---STLKEKDLT-NYRRNHL 86
Cdd:PRK14258 14 SFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEffnQNIYERRVNlNRLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 87 GYVFQMYNLIShLNVEQNIDVG-KYLSKNP-----------LNKEELLQTLGLKEHryKQPNQLSGGQQQRTSIGRAIIK 154
Cdd:PRK14258 91 SMVHPKPNLFP-MSVYDNVAYGvKIVGWRPkleiddivesaLKDADLWDEIKHKIH--KSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 155 NPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIR 216
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSDFTAFFKGNENR 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-215 |
3.77e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.19 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 18 KTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTnyRRnhLGYVFQMYNLIS 97
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HLNVEQNIDVGKYlSKNPL----NKEE------LLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:PRK10253 95 DITVQELVARGRY-PHQPLftrwRKEDeeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1466369044 168 LDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHdlNQACR-YASHLIALREGKI 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-215 |
5.88e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 88.08 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGiDQP-DSGTITIqgktistlkEKDLTNYR------R 83
Cdd:PRK11147 12 SFSD----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlDDGRIIY---------EQDLIVARlqqdppR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVF--------------QMYNLISHLnVEQNidvgkYLSKNpLNK--------------------EELLQTLGLKE 129
Cdd:PRK11147 78 NVEGTVYdfvaegieeqaeylKRYHDISHL-VETD-----PSEKN-LNElaklqeqldhhnlwqlenriNEVLAQLGLDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 130 HryKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTskdiLQLIEDVNKKYGNTIIIVTHNDA-IKDMADRVI 208
Cdd:PRK11147 151 D--AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDRSfIRNMATRIV 224
|
....*..
gi 1466369044 209 YLHDGRI 215
Cdd:PRK11147 225 DLDRGKL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-214 |
8.00e-20 |
|
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: 87.57 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIdQPD---SGTITIQGktiSTLKEKDLT 79
Cdd:TIGR02633 2 LEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSG---SPLKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 NYRRNHLGYVFQMYNLISHLNVEQNIDVGKYLSKNP---------LNKEELLQTLGLKEHRYKQP-NQLSGGQQQRTSIG 149
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLGNEITLPGgrmaynamyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 150 RAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-217 |
1.36e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.76 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQP-----DSGTITIQGKTIstLKEKDLTNYRRnHLGYVFQMYNL 95
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSI--FNYRDVLEFRR-RVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 96 IShLNVEQNIDVGKYLSKNPLNKE------ELLQTLGL----KEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:PRK14271 113 FP-MSIMDNVLAGVRAHKLVPRKEfrgvaqARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 166 GALDYHTSKDILQLIEDVNKKYgnTIIIVTHNDA-IKDMADRVIYLHDGRIRE 217
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAqAARISDRAALFFDGRLVE 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-215 |
1.73e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.26 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnyrRNHLGYVF-----QMYN 94
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LisHLNVEQNIDVGKYLSKNP---LNK-------EELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCDE 163
Cdd:PRK15439 352 L--YLDAPLAWNVCALTHNRRgfwIKParenavlERYRRALNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 164 PTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-227 |
1.79e-19 |
|
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: 86.39 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkEKDLTNYrRNHLGYVFQMYNLISHL-NVEQ 103
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAY-RQLFSAVFSDFHLFDRLlGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 104 NIDVGKYlsknplnkEELLQTLGLKEH-RYKQ----PNQLSGGQQQRTSIGRAIIKNPDLLLCDEptGALD--------- 169
Cdd:COG4615 427 EADPARA--------RELLERLELDHKvSVEDgrfsTTDLSQGQRKRLALLVALLEDRPILVFDE--WAADqdpefrrvf 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 170 YHTskdILQLIedvnKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIRENIKNTHKIPA 227
Cdd:COG4615 497 YTE---LLPEL----KARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-224 |
2.37e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.23 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGktiSTLKEKDLTNYRrNHLGYVF 90
Cdd:PRK11176 348 TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG---HDLRDYTLASLR-NQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 QMYNLISHlNVEQNIdvgKYLSKNPLNKEELLQTLGLK---EHRYKQPN-----------QLSGGQQQRTSIGRAIIKNP 156
Cdd:PRK11176 424 QNVHLFND-TIANNI---AYARTEQYSREQIEEAARMAyamDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 157 DLLLCDEPTGALDYHTSKDILQLIEDVNKKygNTIIIVTHNDAIKDMADRVIYLHDGRIREniKNTHK 224
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVE--RGTHA 563
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-197 |
6.07e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.01 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNY--RRNHLGYVFQMYnlishl 99
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpQSEEVDWSFPVL------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 nVEQNIDVGKYLSKNPLNK---------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDY 170
Cdd:PRK15056 97 -VEDVVMMGRYGHMGWLRRakkrdrqivTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*..
gi 1466369044 171 HTSKDILQLIEDVNKKyGNTIIIVTHN 197
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-222 |
8.50e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 83.42 E-value: 8.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIdQPDSGTIT-----IQGKTISTLKEKD 77
Cdd:COG4170 4 LDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTadrfrWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRNHLGYVFQmyNLISHLNVEQNIdvGKYLSKNPLNKE-----------------ELLQTLGLKEHR-----YkqP 135
Cdd:COG4170 83 RRKIIGREIAMIFQ--EPSSCLDPSAKI--GDQLIEAIPSWTfkgkwwqrfkwrkkraiELLHRVGIKDHKdimnsY--P 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 136 NQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTITVLYCGQ 236
|
250
....*....|...
gi 1466369044 215 I-----RENIKNT 222
Cdd:COG4170 237 TvesgpTEQILKS 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
4-214 |
1.22e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.16 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEdeyKTeVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDS--GTITIQGKTIS--TLKEkdlt 79
Cdd:PLN03211 70 KISDETRQIQE---RT-ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTkqILKR---- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 nyrrnhLGYVFQMYNLISHLNVEQN------IDVGKYLSKNP--LNKEELLQTLGLKehryKQPNQ---------LSGGQ 142
Cdd:PLN03211 142 ------TGFVTQDDILYPHLTVRETlvfcslLRLPKSLTKQEkiLVAESVISELGLT----KCENTiignsfirgISGGE 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 143 QQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDA--IKDMADRVIYLHDGR 214
Cdd:PLN03211 212 RKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSsrVYQMFDSVLVLSEGR 284
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-214 |
1.27e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 27 FEIEKGEICVLLGPSGSGKSTLLNIIGGIdQPDSGTITIQGKTISTLKEKDLTNYRrnhlGY------------VFQMYN 94
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYlsqqqtppfampVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LisHLNVEQNIDVGKYLsknpLNkeELLQTLGL--KEHRykQPNQLSGGQQQRTSIGRAIIK-----NPD--LLLCDEPT 165
Cdd:PRK03695 92 L--HQPDKTRTEAVASA----LN--EVAEALGLddKLGR--SVNQLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 166 GALDYHTSKDILQLIEDVNKKyGNTIIIVTH--NDAIKDmADRVIYLHDGR 214
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQ-GIAVVMSSHdlNHTLRH-ADRVWLLKQGK 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-215 |
1.88e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKD-LTN---Y---RRNHLGYVFQMyn 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANgivYiseDRKRDGLVLGM-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 lishlNVEQNIDVG--KYLSKNP--LNKEELLQTLG--LKEHRYKQPNQ------LSGGQQQRTSIGRAIIKNPDLLLCD 162
Cdd:PRK10762 346 -----SVKENMSLTalRYFSRAGgsLKHADEQQAVSdfIRLFNIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 163 EPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-213 |
4.26e-18 |
|
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: 82.65 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtIS-----------TLKEKDLTNYRRNH 85
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISfspqtswimpgTIKDNIIFGLSYDE 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 86 LGYVfqmyNLISHLNVEQNIDVGKYLSKNPLNKEELlqtlglkehrykqpnQLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:TIGR01271 516 YRYT----SVIKACQLEEDIALFPEKDKTVLGEGGI---------------TLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 166 GALDYHTSKDILQ-----LIedVNKkygnTIIIVTHNDAIKDMADRVIYLHDG 213
Cdd:TIGR01271 577 THLDVVTEKEIFEsclckLM--SNK----TRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-198 |
4.29e-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: 79.07 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEkdltNYRRNhLGYVFQMYNLISHLN 100
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD----SIARG-LLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNIdvgKYLSknPLNK----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDI 176
Cdd:cd03231 90 VLENL---RFWH--ADHSdeqvEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|..
gi 1466369044 177 LQLIEDvNKKYGNTIIIVTHND 198
Cdd:cd03231 165 AEAMAG-HCARGGMVVLTTHQD 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-213 |
7.44e-18 |
|
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: 78.91 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRNHLGYVFQMYNLIShLNV 101
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLN-ATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQNIDVGkylskNPLNKEellqtlglkehRYK--------QPN-----------------QLSGGQQQRTSIGRAIIKNP 156
Cdd:cd03290 96 EENITFG-----SPFNKQ-----------RYKavtdacslQPDidllpfgdqteigergiNLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 157 DLLLCDEPTGALDYHTS-----KDILQLIEDVNKkygnTIIIVTHNDAIKDMADRVIYLHDG 213
Cdd:cd03290 160 NIVFLDDPFSALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-210 |
9.74e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.31 E-value: 9.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 24 GIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKdltnYRRNhLGYvfqmynlISHLN--- 100
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQD-LLY-------LGHQPgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 ----VEQNIDVGKYLSkNPLNKEELLQTL---GLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTS 173
Cdd:PRK13538 87 teltALENLRFYQRLH-GPGDDEALWEALaqvGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1466369044 174 KDILQLIEDvNKKYGNTIIIVTHND-AIKDMADRVIYL 210
Cdd:PRK13538 166 ARLEALLAQ-HAEQGGMVILTTHQDlPVASDKVRKLRL 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-217 |
1.13e-17 |
|
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: 81.53 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtistlkekdltnyrrnhLGYVFQMyNLISHLNV 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQ-AWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQNIDVGKYLSKNP----------LNKEELLQTLGLKEHRYKQPNqLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYH 171
Cdd:TIGR00957 716 RENILFGKALNEKYyqqvleacalLPDLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1466369044 172 TSKDILQ-LIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:TIGR00957 795 VGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-213 |
1.31e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.01 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITI-QGKTI-----------STLKE-----KDLTNYRR 83
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVlflpqrpylplGTLREallypATAEAFSD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQMYNL---ISHLNVEQNIDvgkylsknplnkeellqtlglkehrykqpNQLSGGQQQRTSIGRAIIKNPDLLL 160
Cdd:COG4178 458 AELREALEAVGLghlAERLDEEADWD-----------------------------QVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDvnKKYGNTIIIVTHNDAIKDMADRVIYLHDG 213
Cdd:COG4178 509 LDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-208 |
1.51e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.01 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeYKTEVLKGidfEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtIStlkekdltnyr 82
Cdd:PRK13409 341 VEYPDLTKKLGD--FSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-IS----------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnhlgYVFQmynlisHLNVEQNIDVGKYLSKNPLN------KEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNP 156
Cdd:PRK13409 404 -----YKPQ------YIKPDYDGTVEDLLRSITDDlgssyyKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 157 DLLLCDEPTGALD----YHTSKDILQLIEDVNKkygnTIIIVTHNDAIKDM-ADRVI 208
Cdd:PRK13409 473 DLYLLDEPSAHLDveqrLAVAKAIRRIAEEREA----TALVVDHDIYMIDYiSDRLM 525
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-217 |
1.57e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.59 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 23 KGIDFEIEKGEICVLLGPSGSGKS-TLLNIIG----GIDQPdSGTITIQGKTIStlkekdLTNYRRNHLGYVFQ------ 91
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGilpaGVRQT-AGRVLLDGKPVA------PCALRGRKIATIMQnprsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 92 --MYNLISHLnVEQNIDVGKYLSKNPLnkEELLQTLGLKE-HRYKQ--PNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:PRK10418 93 npLHTMHTHA-RETCLALGKPADDATL--TAALEAVGLENaARVLKlyPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 167 ALDYHTSKDILQLIEDVNKKYGNTIIIVTHndaikDM------ADRVIYLHDGRIRE 217
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTH-----DMgvvarlADDVAVMSHGRIVE 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-196 |
3.41e-17 |
|
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: 79.98 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeyktEVL-KGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIqGKTIstlkekdltny 81
Cdd:TIGR03719 323 IEAENLTKAFGD-----KLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 rrnHLGYVFQMY-NLISHLNVEQNI-------DVGKYlsknPLNKEELLQTLGLK-EHRYKQPNQLSGGQQQRTSIGRAI 152
Cdd:TIGR03719 386 ---KLAYVDQSRdALDPNKTVWEEIsggldiiKLGKR----EIPSRAYVGRFNFKgSDQQKKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1466369044 153 IKNPDLLLCDEPTGALDYHTskdiLQLIEDVNKKYGNTIIIVTH 196
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISH 498
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-232 |
3.70e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.76 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYNLISHlN 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNIDVGKyLSKNPLNKEELLQTLGLKEHRYKQPN-----------QLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALD 169
Cdd:PRK10789 405 VANNIALGR-PDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 170 YHTSKDILQLIEDVNKkyGNTIIIVTHN-DAIKDmADRVIYLHDGRIREniKNTHKIPAKDLNW 232
Cdd:PRK10789 484 GRTEHQILHNLRQWGE--GRTVIISAHRlSALTE-ASEILVMQHGHIAQ--RGNHDQLAQQSGW 542
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-215 |
3.82e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTE-VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTnyRRNHLGYVFQmynl 95
Cdd:PRK13638 11 YQDEpVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLA--LRQQVATVFQ---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 96 ishlNVEQNI-------DVGKYLSKNPLNKEELLQ------TLGLKEHRYKQPNQ-LSGGQQQRTSIGRAIIKNPDLLLC 161
Cdd:PRK13638 85 ----DPEQQIfytdidsDIAFSLRNLGVPEAEITRrvdealTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 162 DEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDiDLIYEISDAVYVLRQGQI 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-213 |
4.03e-17 |
|
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: 77.97 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtIS-----------TLKEKDLTNYRRNH 85
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISfssqfswimpgTIKENIIFGVSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 86 LGYVfqmyNLISHLNVEQNIdvgkylSKNPLNKEELLQTLGLkehrykqpnQLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:cd03291 127 YRYK----SVVKACQLEEDI------TKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1466369044 166 GALDYHTSKDILQliEDVNKKYGN-TIIIVTHNDAIKDMADRVIYLHDG 213
Cdd:cd03291 188 GYLDVFTEKEIFE--SCVCKLMANkTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-224 |
5.86e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.99 E-value: 5.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYkteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyr 82
Cdd:PRK10790 341 IDIDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHlNVEQNIDVGKYLSKNPL-------NKEELLQTL--GLKEHRYKQPNQLSGGQQQRTSIGRAII 153
Cdd:PRK10790 414 RQGVAMVQQDPVVLAD-TFLANVTLGRDISEEQVwqaletvQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 154 KNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKygNTIIIVTHNDAIKDMADRVIYLHDGRIREniKNTHK 224
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAVE--QGTHQ 559
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-215 |
6.15e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.40 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTlkeKDLTNYRRnhLGYVFQMYNLISHLNVEQN 104
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA---GDIATRRR--VGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 105 IDVGKYLSKNPLNK-----EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQL 179
Cdd:NF033858 360 LELHARLFHLPAAEiaarvAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190
....*....|....*....|....*....|....*...
gi 1466369044 180 IEDVNKKYGNTIIIVTH--NDAIKdmADRVIYLHDGRI 215
Cdd:NF033858 440 LIELSREDGVTIFISTHfmNEAER--CDRISLMHAGRV 475
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-230 |
1.10e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.22 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGidQPD----SGTITIQGKTIStlkekDL 78
Cdd:CHL00131 8 LEIKNLHASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESIL-----DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 79 TNYRRNHLG--YVFQMYNLISHLNveqNID--------VGKYLSKNPLNKEELLQTL-------GLKE---HRYKqpNQ- 137
Cdd:CHL00131 77 EPEERAHLGifLAFQYPIEIPGVS---NADflrlaynsKRKFQGLPELDPLEFLEIIneklklvGMDPsflSRNV--NEg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 138 LSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYhtskDILQLI-EDVNK--KYGNTIIIVTHN----DAIKdmADRVIYL 210
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDI----DALKIIaEGINKlmTSENSIILITHYqrllDYIK--PDYVHVM 225
|
250 260
....*....|....*....|
gi 1466369044 211 HDGRIrenIKNTHKIPAKDL 230
Cdd:CHL00131 226 QNGKI---IKTGDAELAKEL 242
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-205 |
1.77e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.99 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 15 DEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIstlkEKDLTNYRRnHLGYVFQMYN 94
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK-QLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LISHLNVEQNIDVGKYLSKNPLNKEELLQTLGLkEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTS 173
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPGAVGITELCRLFSL-EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180 190
....*....|....*....|....*....|..
gi 1466369044 174 KDILQLIEDvNKKYGNTIIIVTHNDAIKDMAD 205
Cdd:PRK13540 164 LTIITKIQE-HRAKGGAVLLTSHQDLPLNKAD 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-208 |
1.87e-16 |
|
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: 77.52 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 7 DLKKSFGEdeYKTEVLKGidfEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtIStlkekdltnyrrnhl 86
Cdd:COG1245 346 DLTKSYGG--FSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-IS--------------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 87 gYVFQMYNLISHLNVEQNID--VGKYLSKNPLnKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEP 164
Cdd:COG1245 405 -YKPQYISPDYDGTVEEFLRsaNTDDFGSSYY-KTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1466369044 165 TGALD----YHTSKDILQLIEdvnkKYGNTIIIVTHNDAIKDM-ADRVI 208
Cdd:COG1245 483 SAHLDveqrLAVAKAIRRFAE----NRGKTAMVVDHDIYLIDYiSDRLM 527
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-169 |
9.06e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 11 SFGEDEykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKekdltnyRRNHLGYVF 90
Cdd:PRK13543 18 AFSRNE--EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 91 QMYNLISHLNVEQNIDV-----GKYLSKNPLNKeelLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:PRK13543 89 HLPGLKADLSTLENLHFlcglhGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....
gi 1466369044 166 GALD 169
Cdd:PRK13543 166 ANLD 169
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-213 |
1.03e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 72.66 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGidQPDSGTITiqGK-TISTLKEKDltNY 81
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT--GEiLINGRPLDK--NF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 RRNhLGYVFQMYNLISHLNVeqnidvgkylsknplnKEELLQTLGLKEhrykqpnqLSGGQQQRTSIGRAIIKNPDLLLC 161
Cdd:cd03232 78 QRS-TGYVEQQDVHSPNLTV----------------REALRFSALLRG--------LSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 162 DEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTH--NDAIKDMADRVIYLHDG 213
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-214 |
1.11e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIdQPD---SGTITIQGKTI--STLKEKDltnyrrnHLGYVF--QMYN 94
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCrfKDIRDSE-------ALGIVIihQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 95 LISHLNVEQNIDVGKYLSKNPL------NKE--ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:NF040905 89 LIPYLSIAENIFLGNERAKRGVidwnetNRRarELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1466369044 167 ALDYHTSKDILQLIEDVnKKYGNTIIIVTH--NDaIKDMADRVIYLHDGR 214
Cdd:NF040905 169 ALNEEDSAALLDLLLEL-KAQGITSIIISHklNE-IRRVADSITVLRDGR 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-212 |
2.52e-15 |
|
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: 71.03 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIqgktistlkekdltnYRRNHLGYVFQMynlishln 100
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------------PEGEDLLFLPQR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 veqnidvgKYLSKNPLnKEELLqtlglkehrYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLI 180
Cdd:cd03223 73 --------PYLPLGTL-REQLI---------YPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180 190
....*....|....*....|....*....|..
gi 1466369044 181 edvnKKYGNTIIIVTHNDAIKDMADRVIYLHD 212
Cdd:cd03223 135 ----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-215 |
1.20e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.59 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGID--QPDSGTITIQGKTISTLKEKDltn 80
Cdd:PRK09580 2 LSIKDLHVSVED----KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 yrRNHLG------YVFQMYNLISHLNVEQNID-VGKYLSKNPLNKEELLQTLGLKEHRYKQPNQL---------SGGQQQ 144
Cdd:PRK09580 75 --RAGEGifmafqYPVEIPGVSNQFFLQTALNaVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvnvgfSGGEKK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 145 RTSIGRAIIKNPDLLLCDEPTGALDYhtskDILQLI-EDVN--KKYGNTIIIVTHNDAIKDM--ADRVIYLHDGRI 215
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDI----DALKIVaDGVNslRDGKRSFIIVTHYQRILDYikPDYVHVLYQGRI 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-222 |
1.36e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTnyrRNHLGYVFQMY--- 93
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV---KKGMAYITESRrdn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 94 NLISHLNVEQNIDVGKYLSKNPLN--------------KEELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDL 158
Cdd:PRK09700 351 GFFPNFSIAQNMAISRSLKDGGYKgamglfhevdeqrtAENQRELLALKCHSVNQNiTELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 159 LLCDEPTGALDYHTSKDILQLIEDVNKKyGNTIIIVTHN-DAIKDMADRVIYLHDGRIRENIKNT 222
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCDRIAVFCEGRLTQILTNR 494
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-208 |
1.92e-14 |
|
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: 68.89 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNiiggidqpdsgtiTIQGKTISTLKEKDLTNYRRNHLGYVFQMYNLishlnv 101
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNKLIFIDQLQFL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 eqnIDVG-KYLsknPLNKEelLQTlglkehrykqpnqLSGGQQQRTSIGRAIIKNPD--LLLCDEPTGALDYhtsKDILQ 178
Cdd:cd03238 72 ---IDVGlGYL---TLGQK--LST-------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ---QDINQ 127
|
170 180 190
....*....|....*....|....*....|..
gi 1466369044 179 LIEDVNK--KYGNTIIIVTHNDAIKDMADRVI 208
Cdd:cd03238 128 LLEVIKGliDLGNTVILIEHNLDVLSSADWII 159
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-213 |
2.57e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSF-GedeykTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDltnY 81
Cdd:PRK10762 5 LQLKGIDKAFpG-----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS---S 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 RRNHLGYVFQMYNLISHLNVEQNIdvgkYLSKNPLNK-------------EELLQTLGLKEHRYKQPNQLSGGQQQRTSI 148
Cdd:PRK10762 77 QEAGIGIIHQELNLIPQLTIAENI----FLGREFVNRfgridwkkmyaeaDKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 149 GRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDG 213
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRlKEIFEICDDVTVFRDG 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-215 |
1.08e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKD--------LTNYRRNHLGYvfqmy 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalVTEERRSTGIY----- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 94 nliSHLNVEQNIDVGKYlsKNPLNKEELLQTLGLKEH--------RYKQPNQ------LSGGQQQRTSIGRAIIKNPDLL 159
Cdd:PRK10982 339 ---AYLDIGFNSLISNI--RNYKNKVGLLDNSRMKSDtqwvidsmRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 160 LCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:PRK10982 414 MLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-217 |
1.21e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.77 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYNLISH-- 98
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQAPVLFSGtv 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 99 ------LNVEQNIDVGKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHT 172
Cdd:PLN03130 1330 rfnldpFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1466369044 173 SKDILQLIEDVNKKYgnTIIIVTHN-DAIKDmADRVIYLHDGRIRE 217
Cdd:PLN03130 1410 DALIQKTIREEFKSC--TMLIIAHRlNTIID-CDRILVLDAGRVVE 1452
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-231 |
2.19e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKD-------LTNYRRNHLGyvfqmynLIS 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairagimLCPEDRKAEG-------IIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HLNVEQNIDVGKYLSKNPL-----------NKEELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:PRK11288 345 VHSVADNINISARRHHLRAgclinnrweaeNADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 166 GALDYHTSKDILQLIEDVNKKyGNTIIIVTHNDA-IKDMADRVIYLHDGRIRENIKNTHKIPAKDLN 231
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPeVLGVADRIVVMREGRIAGELAREQATERQALS 490
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-196 |
5.44e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 6 KDLKKSFGEdeyktEVL-KGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIqGKTIstlkekdltnyrrn 84
Cdd:PRK11819 328 ENLSKSFGD-----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 85 HLGYVFQMYnliSHLNVEQN-----------IDVGK-------YLSK-NplnkeellqtlglkehrYKQPNQ------LS 139
Cdd:PRK11819 388 KLAYVDQSR---DALDPNKTvweeisggldiIKVGNreipsraYVGRfN-----------------FKGGDQqkkvgvLS 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 140 GGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTskdiLQLIEDVNKKYGNTIIIVTH 196
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET----LRALEEALLEFPGCAVVISH 500
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-214 |
5.94e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNyrrNHLGYVFQMYNLISHLNV 101
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---NGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQNIDVGKYLSKNPL--------NKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALdyhTS 173
Cdd:PRK10982 91 MDNMWLGRYPTKGMFvdqdkmyrDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1466369044 174 KDILQLIEDVNK--KYGNTIIIVTHN-DAIKDMADRVIYLHDGR 214
Cdd:PRK10982 168 KEVNHLFTIIRKlkERGCGIVYISHKmEEIFQLCDEITILRDGQ 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-217 |
9.79e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDlkKSFGEDEyKTE--VLKGIDFEIEKGEICVLLGPSGSGKSTLLN-IIGGIDQPDSGTITIQGKtistlkekdlt 79
Cdd:PLN03130 615 ISIKN--GYFSWDS-KAErpTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT----------- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 80 nyrrnhLGYVFQMyNLISHLNVEQNIDVGKYLSKNPLNKE----------ELLQTLGLKEHRYKQPNqLSGGQQQRTSIG 149
Cdd:PLN03130 681 ------VAYVPQV-SWIFNATVRDNILFGSPFDPERYERAidvtalqhdlDLLPGGDLTEIGERGVN-ISGGQKQRVSMA 752
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 150 RAIIKNPDLLLCDEPTGALDYHTSKDILQ--LIEDVNKKygnTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-196 |
1.07e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.50 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKKSFGEdeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQ-GKTISTL-KEKDL--- 78
Cdd:TIGR03719 6 TMNRVSKVVPP---KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLpQEPQLdpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 79 TNYRRN------HLGYVFQMYNLISHLNVEQNIDVGKYLSKNPlNKEELLQTLGLKEHRYK---------------QPNQ 137
Cdd:TIGR03719 83 KTVRENveegvaEIKDALDRFNEISAKYAEPDADFDKLAAEQA-ELQEIIDAADAWDLDSQleiamdalrcppwdaDVTK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 138 LSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTskdiLQLIEDVNKKYGNTIIIVTH 196
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-215 |
1.15e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.69 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 18 KTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRrnhLGYVFQMY--NL 95
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPR---IAYMPQGLgkNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 96 ISHLNVEQNIDV-----GkylsknpLNKEE-------LLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDE 163
Cdd:NF033858 90 YPTLSVFENLDFfgrlfG-------QDAAErrrrideLLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 164 PTgaldyhTSKDIL------QLIEDVNKKY-GNTIIIVThndAIKDMADR---VIYLHDGRI 215
Cdd:NF033858 163 PT------TGVDPLsrrqfwELIDRIRAERpGMSVLVAT---AYMEEAERfdwLVAMDAGRV 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-215 |
1.37e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.45 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEykteVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTItiqgktistlKEKDLTNyr 82
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENAN-- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 rnhLGYVFQMYnliSHlNVEQNIDVGKYLS--KNPLNKEELLQ-TLGL----KEHRYKQPNQLSGGQQQRTSIGRAIIKN 155
Cdd:PRK15064 384 ---IGYYAQDH---AY-DFENDLTLFDWMSqwRQEGDDEQAVRgTLGRllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 156 PDLLLCDEPTGALDyhtskdiLQLIEDVN---KKYGNTIIIVTHNDA-IKDMADRVIYLHDGRI 215
Cdd:PRK15064 457 PNVLVMDEPTNHMD-------MESIESLNmalEKYEGTLIFVSHDREfVSSLATRIIEITPDGV 513
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-218 |
2.07e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.21 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDEYKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQpDSGTITIQGKTISTLKEKDLTNY- 81
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDLLRLSPRe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 82 RRNHLGY----VFQMYNliSHLNVEQNIDV------------GKYLSKNPLNKE---ELLQTLGLKEHR---YKQPNQLS 139
Cdd:PRK15093 83 RRKLVGHnvsmIFQEPQ--SCLDPSERVGRqlmqnipgwtykGRWWQRFGWRKRraiELLHRVGIKDHKdamRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 140 GGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIREN 218
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKINVLYCGQTVET 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-215 |
2.40e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGiDQPD--SGTITI------QGKTISTLKEkdltnyrrnHLGYVFQM 92
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTLfgrrrgSGETIWDIKK---------HIGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 93 YNL-----ISHLNVeqnIDVGKYLS---------KNPLNKEELLQTLGLKEHRYKQPNQ-LSGGQQQRTSIGRAIIKNPD 157
Cdd:PRK10938 345 LHLdyrvsTSVRNV---ILSGFFDSigiyqavsdRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIeDVNKKYGNT-IIIVTHN--DAIKDMADRVIYLHDGRI 215
Cdd:PRK10938 422 LLILDEPLQGLDPLNRQLVRRFV-DVLISEGETqLLFVSHHaeDAPACITHRLEFVPDGDI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-213 |
2.58e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 17 YKTE---VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGidQPDSGTITiQGKTISTLKEKDLTNYRRnhLGYVFQMY 93
Cdd:TIGR00956 771 IKKEkrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVIT-GGDRLVNGRPLDSSFQRS--IGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 94 NLISHLNVEQNIDVGKYLSK-NPLNKEE----------LLQTLGLKEHRYKQPNQ-LSGGQQQRTSIGRAIIKNPDLLL- 160
Cdd:TIGR00956 846 LHLPTSTVRESLRFSAYLRQpKSVSKSEkmeyveevikLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHNDAIKDMA--DRVIYLHDG 213
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-215 |
3.88e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.19 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 20 EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTItiqgktistLKEKDLtnyrrnhlGYVFQMyNLISHL 99
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERSI--------AYVPQQ-AWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 NVEQNIdvgkyLSKNPLNKEEL------------LQTL--GLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:PTZ00243 736 TVRGNI-----LFFDEEDAARLadavrvsqleadLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 166 GALDYHTSKDIlqlIEDV--NKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:PTZ00243 811 SALDAHVGERV---VEECflGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-215 |
8.34e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 8 LKKSFGEDEYKT-EVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGG-IDQ---PDSGTITIQGktistLKEKDLTNYR 82
Cdd:TIGR00956 62 FRKLKKFRDTKTfDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGfhiGVEGVITYDG-----ITPEEIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNHLGYVFQMYNLISHLNVEQNIDVGKYLsKNPLNKEELLQ--------------TLGLKEHR-YKQPNQL----SGGQQ 143
Cdd:TIGR00956 137 RGDVVYNAETDVHFPHLTVGETLDFAARC-KTPQNRPDGVSreeyakhiadvymaTYGLSHTRnTKVGNDFvrgvSGGER 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 144 QRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDA--IKDMADRVIYLHDGRI 215
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQ 289
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-203 |
9.92e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 62.77 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 32 GEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITiqgktistlKEKD----LTNYRRNHL-GYVFQMYN-LISHLNVEQNI 105
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD---------DPPDwdeiLDEFRGSELqNYFTKLLEgDVKVIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 106 D---------VGKYLSKNPLN--KEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSK 174
Cdd:cd03236 97 DlipkavkgkVGELLKKKDERgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|....*....
gi 1466369044 175 DILQLIEDVNKKyGNTIIIVTHNDAIKDM 203
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHDLAVLDY 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-212 |
1.13e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 59 DSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMyNLISHLNVEQNIDVGKYLSKNPLNK--------EELLQTLGLKEH 130
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDL----RNLFSIVSQE-PMLFNMSIYENIKFGKEDATREDVKrackfaaiDEFIESLPNKYD 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 131 RYKQP--NQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVI 208
Cdd:PTZ00265 1350 TNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
....
gi 1466369044 209 YLHD 212
Cdd:PTZ00265 1430 VFNN 1433
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-223 |
1.54e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLN-IIGGIDQPDSGTITIQGKTISTLKEKDLTnyrRNHLGYVFQ---MYNLISHLN 100
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQAI---AQGIAMVPEdrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNIDV---GKYLSKNPLNKEELLQTLG--LKEHRYKQPN------QLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALD 169
Cdd:PRK13549 358 VGKNITLaalDRFTGGSRIDDAAELKTILesIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 170 YHTSKDILQLIEDVNKKyGNTIIIVTHNDA-IKDMADRVIYLHDGRIRENIKNTH 223
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQ-GVAIIVISSELPeVLGLSDRVLVMHEGKLKGDLINHN 491
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-215 |
2.71e-11 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 61.12 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLL---------------------NIIGGIDQPDSGTITIQGKTIStLKEKDLTN 80
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIA-IDQKTTSR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRRNHLGYVFQMYNLISHL--------NVEQNIDVG-KYLSknpLNKEEllqtlglkehrykqpNQLSGGQQQRTSIGRA 151
Cdd:cd03270 90 NPRSTVGTVTEIYDYLRLLfarvgireRLGFLVDVGlGYLT---LSRSA---------------PTLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466369044 152 IIKNPD--LLLCDEPTGAL---DYHTSKDILQLIEDVnkkyGNTIIIVTHNDAIKDMADRVIYL------HDGRI 215
Cdd:cd03270 152 IGSGLTgvLYVLDEPSIGLhprDNDRLIETLKRLRDL----GNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEI 222
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-208 |
3.17e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.89 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 28 EIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIStlkekdltnyrrnhlgyvfqmynlishlnveqnidv 107
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 108 gkylsknplnkeellqtlglkehrYK-QPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALD----YHTSKDILQLIED 182
Cdd:cd03222 65 ------------------------YKpQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*..
gi 1466369044 183 VNKkygnTIIIVTHNDAIKD-MADRVI 208
Cdd:cd03222 121 GKK----TALVVEHDLAVLDyLSDRIH 143
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-217 |
3.59e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLN-IIGGIDQPDSGTITIQGKtistlkekdltnyrrnhLGYVFQMyNLISHLN 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-----------------VAYVPQV-SWIFNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNIDVG---------KYLSKNPLNKE-ELLQTLGLKEHRYKQPNqLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDY 170
Cdd:PLN03232 695 VRENILFGsdfeserywRAIDVTALQHDlDLLPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1466369044 171 HTSKDIL-QLIEDVNKkyGNTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:PLN03232 774 HVAHQVFdSCMKDELK--GKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
5-217 |
5.85e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 5 IKDLKKSFGEDEYKTeVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGK----TISTLKEKDLTN 80
Cdd:PRK13545 24 LKDLFFRSKDGEYHY-ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaaliAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 81 YRRnhlgyvFQMYNLISHLNVEQNIDVgkylsknplnKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLL 160
Cdd:PRK13545 103 IEN------IELKGLMMGLTKEKIKEI----------IPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 161 CDEPTGALDYHTSKDILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK13545 167 IDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSlSQVKSFCTKALWLHYGQVKE 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-222 |
1.13e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGEICVLLGPSGSGKSTLLN-IIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRNHLGYVFQMYNLISHLNVEQ 103
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 104 NIDVG---KYLSKNPLNKEELLQTLGLKEHRYK----QPN----QLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHT 172
Cdd:TIGR02633 359 NITLSvlkSFCFKMRIDAAAELQIIGSAIQRLKvktaSPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 173 SKDILQLIEDVNKKyGNTIIIVTHNDA-IKDMADRVIYLHDGRIRENIKNT 222
Cdd:TIGR02633 439 KYEIYKLINQLAQE-GVAIIVVSSELAeVLGLSDRVLVIGEGKLKGDFVNH 488
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-217 |
1.84e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLkekDLTNYRRNhLGYVFQMYNLIS--- 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRRV-LSIIPQSPVLFSgtv 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HLNVE-----QNIDVGKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHT 172
Cdd:PLN03232 1327 RFNIDpfsehNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1466369044 173 SKDILQLIEDVNKKYgnTIIIVTHN-DAIKDmADRVIYLHDGRIRE 217
Cdd:PLN03232 1407 DSLIQRTIREEFKSC--TMLVIAHRlNTIID-CDKILVLSSGQVLE 1449
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-214 |
1.85e-10 |
|
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: 57.38 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 31 KGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTItiqgktistlkekdltnyrrnhlgyvfqmynlishlnveqnidvgKY 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------------------------IY 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 111 LSKNPLNKEELLQTLGLKEHRYKqpNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIE----DVNKK 186
Cdd:smart00382 36 IDGEDILEEVLDQLLLIIVGGKK--ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllLLLKS 113
|
170 180 190
....*....|....*....|....*....|....*
gi 1466369044 187 YGNTIIIVTHND-------AIKDMADRVIYLHDGR 214
Cdd:smart00382 114 EKNLTVILTTNDekdlgpaLLRRRFDRRIVLLLIL 148
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-218 |
3.40e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 4 SIKDLKK------SFGEDEYK-TEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtiSTLKEK 76
Cdd:PTZ00265 376 KLKDIKKiqfknvRFHYDTRKdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 77 DLtNYRRNHLGYVFQMYNLISHlNVEQNIDVGKYLSK--------------------------------------NPLNK 118
Cdd:PTZ00265 454 NL-KWWRSKIGVVSQDPLLFSN-SIKNNIKYSLYSLKdlealsnyynedgndsqenknkrnscrakcagdlndmsNTTDS 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 119 EELL------QTLGLKE----------HRY-------------KQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALD 169
Cdd:PTZ00265 532 NELIemrknyQTIKDSEvvdvskkvliHDFvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1466369044 170 YHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDgriREN 218
Cdd:PTZ00265 612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN---RER 657
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-207 |
5.73e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 30 EKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtistlKEKDLTNYRRNHLGYVFQM-YN---LISHLNveQNI 105
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPS-----WDEVLKRFRGTELQDYFKKlANgeiKVAHKP--QYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 106 D-VGKYLSKNP---LNK-------EELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSK 174
Cdd:COG1245 170 DlIPKVFKGTVrelLEKvdergklDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL 249
|
170 180 190
....*....|....*....|....*....|....
gi 1466369044 175 DILQLIEDVNKKyGNTIIIVTHNDAIKDM-ADRV 207
Cdd:COG1245 250 NVARLIRELAEE-GKYVLVVEHDLAILDYlADYV 282
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-197 |
7.52e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.49 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 29 IEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTIstlkekdLTNYRRNH--LGYVFQMYNLISHLNVEQNID 106
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-------LTNISDVHqnMGYCPQFDAIDDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 107 VGKYLSKNPLNKEEL-----LQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIE 181
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKvanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170
....*....|....*.
gi 1466369044 182 DVNKKyGNTIIIVTHN 197
Cdd:TIGR01257 2115 SIIRE-GRAVVLTSHS 2129
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-196 |
1.45e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 37 LLGPSGSGKSTLLNIIGGIDQPDSGTITIQ-GKTIstlkekdltnyrrnhlGYVFQMYNLISHLNVEQNIDVGKYLSKNP 115
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV----------------GYLPQEPQLDPEKTVRENVEEGVAEVKAA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 116 LNK-------------------------EELLQTLGLK--EHRYKQ-------P------NQLSGGQQQRTSIGRAIIKN 155
Cdd:PRK11819 102 LDRfneiyaayaepdadfdalaaeqgelQEIIDAADAWdlDSQLEIamdalrcPpwdakvTKLSGGERRRVALCRLLLEK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1466369044 156 PDLLLCDEPTGALDyhtskdilqlIEDVN------KKYGNTIIIVTH 196
Cdd:PRK11819 182 PDMLLLDEPTNHLD----------AESVAwleqflHDYPGTVVAVTH 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-215 |
2.28e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGiDQPDS---------GTITIQGKTISTLKEKDLTNYR-----RNHL 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRavlpqAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 87 GYVFQMYNLISHLNVEQNIDVGKYLSKNPLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAI---------IKNPD 157
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTH--NDAIKdMADRVIYLHDGRI 215
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHdpNLAAR-HADRIAMLADGAI 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-202 |
3.72e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtistLKEKDLTNYRRNhlgyvfqmynLISHLNV 101
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFDQHRAE----------LDPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQNIDVGKylsknplnkeellQTL---GLKEH-------------RYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCDEP 164
Cdd:PRK11147 401 MDNLAEGK-------------QEVmvnGRPRHvlgylqdflfhpkRAMTPvKALSGGERNRLLLARLFLKPSNLLILDEP 467
|
170 180 190
....*....|....*....|....*....|....*...
gi 1466369044 165 TGALDYHTskdiLQLIEDVNKKYGNTIIIVTHNDAIKD 202
Cdd:PRK11147 468 TNDLDVET----LELLEELLDSYQGTVLLVSHDRQFVD 501
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-207 |
1.05e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 29 IEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKtistlKEKDLTNYRRNHLG-YVFQMYN---LISHLNveQN 104
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS-----WDEVLKRFRGTELQnYFKKLYNgeiKVVHKP--QY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 105 ID---------VGKYLSKNPL--NKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTS 173
Cdd:PRK13409 169 VDlipkvfkgkVRELLKKVDErgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR 248
|
170 180 190
....*....|....*....|....*....|....*
gi 1466369044 174 KDILQLIEDVNKkyGNTIIIVTHNDAIKDM-ADRV 207
Cdd:PRK13409 249 LNVARLIRELAE--GKYVLVVEHDLAVLDYlADNV 281
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-217 |
1.10e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.95 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYNLISHlN 100
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQDPVLFSG-S 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNID-VGKYlsknplNKEEL---LQTLGLKEHRYKQPNQ-----------LSGGQQQRTSIGRAIIKNPDLLLCDEPT 165
Cdd:TIGR00957 1376 LRMNLDpFSQY------SDEEVwwaLELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1466369044 166 GALDYHTSKDILQLI----EDVnkkygnTIIIVTHN-DAIKDMAdRVIYLHDGRIRE 217
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIrtqfEDC------TVLTIAHRlNTIMDYT-RVIVLDKGEVAE 1499
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-221 |
1.52e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 29 IEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLTNYRRNHLGYVF-------QMYNLISHLNv 101
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdreyrQLEAQLHDAN- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQN--------------IDVGKYLSKnplnKEELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCDEPTG 166
Cdd:PRK10636 103 ERNdghaiatihgkldaIDAWTIRSR----AASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1466369044 167 ALDYhtskDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRENIKN 221
Cdd:PRK10636 179 HLDL----DAVIWLEKWLKSYQGTLILISHDrDFLDPIVDKIIHIEQQSLFEYTGN 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-212 |
4.11e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 26 DFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTL------KEKDLTNYRRNHlgyvfqmyNLIShl 99
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfeqlqKLVSDEWQRNNT--------DMLS-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 nvEQNIDVGKYL-------SKNPLNKEELLQTLG---LKEHRYKQpnqLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALD 169
Cdd:PRK10938 93 --PGEDDTGRTTaeiiqdeVKDPARCEQLAQQFGitaLLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1466369044 170 YHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHD 212
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-176 |
4.16e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.55 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDsGTITIQGKTISTLKekdLTNYR 82
Cdd:cd03289 3 MTVKDLTAKYTEG--GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP---LQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHlNVEQNID-VGKYlsknplNKEELLQT---LGLKEHRYKQPNQ-----------LSGGQQQRTS 147
Cdd:cd03289 77 KA-FGVIPQKVFIFSG-TFRKNLDpYGKW------SDEEIWKVaeeVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMC 148
|
170 180
....*....|....*....|....*....
gi 1466369044 148 IGRAIIKNPDLLLCDEPTGALDYHTSKDI 176
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVI 177
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-215 |
4.92e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGK---TISTLKEKDLTNYRRNHLGYVFQMYNLIS 97
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrmAVFSQHHVDGLDLSSNPLLYMMRCFPGVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 hlnvEQNIdvgkylsknplnkEELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDI 176
Cdd:PLN03073 604 ----EQKL-------------RAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1466369044 177 LQLIedvnKKYGNTIIIVTHND-AIKDMADRVIYLHDGRI 215
Cdd:PLN03073 667 IQGL----VLFQGGVLMVSHDEhLISGSVDELWVVSEGKV 702
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
118-210 |
8.26e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.32 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 118 KEELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIK---NPDLLLCDEPTGALDYHtskDILQLIEDVNK--KYGNTI 191
Cdd:TIGR00630 809 KLQTLCDVGLGYIRLGQPaTTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFD---DIKKLLEVLQRlvDKGNTV 885
|
90 100
....*....|....*....|
gi 1466369044 192 IIVTHN-DAIKdMADRVIYL 210
Cdd:TIGR00630 886 VVIEHNlDVIK-TADYIIDL 904
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
129-215 |
1.13e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 129 EHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTskdILQLiEDVNKKYGNTIIIVTH-----NDAIKDm 203
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWL-ETYLLKWPKTFIVVSHareflNTVVTD- 410
|
90
....*....|..
gi 1466369044 204 adrVIYLHDGRI 215
Cdd:PLN03073 411 ---ILHLHGQKL 419
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-196 |
1.71e-07 |
|
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: 51.45 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEDeyKTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDsGTITIQGKTISTLKekdLTNYR 82
Cdd:TIGR01271 1218 MDVQGLTAKYTEA--GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVT---LQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 83 RNhLGYVFQMYNLISHlNVEQNIDVGKYLSKNPLNKeeLLQTLGLKEHRYKQPNQ-----------LSGGQQQRTSIGRA 151
Cdd:TIGR01271 1292 KA-FGVIPQKVFIFSG-TFRKNLDPYEQWSDEEIWK--VAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1466369044 152 IIKNPDLLLCDEPTGALDYHTskdiLQLIEDVNKK-YGN-TIIIVTH 196
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVT----LQIIRKTLKQsFSNcTVILSEH 1410
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-215 |
2.62e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 3 LSIKDLKKSFGEdeykTEVLKGIDFEIEKGEICVLLGPSGSG--KSTLLNIIGGidqPDSGTITIQGKTISTLKE---KD 77
Cdd:NF000106 14 VEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRalrRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 78 LTNYRRNHLGYVFQMYNLISHLNVEQNIDVGKYLSKnpLNKEELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPD 157
Cdd:NF000106 87 IG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDAR--ARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
22-210 |
8.40e-07 |
|
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: 48.38 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLN----------IIGGIDQPDSGTITIQGKTISTLKEKDLT----NYRRNHLG 87
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarrLHLKKEQPGNHDRIEGLEHIDKVIVIDQSpigrTPRSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 88 YVfQMYNLISHLNVE---------QNIDVgKYLSKN-------------------P--LNKEELLQTLGLKEHRYKQP-N 136
Cdd:cd03271 91 YT-GVFDEIRELFCEvckgkrynrETLEV-RYKGKSiadvldmtveealeffeniPkiARKLQTLCDVGLGYIKLGQPaT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 137 QLSGGQQQRTSIGRAIIK---NPDLLLCDEPTGALDYHtskDILQLIEDVNK--KYGNTIIIVTHN-DAIKdMADRVIYL 210
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFH---DVKKLLEVLQRlvDKGNTVVVIEHNlDVIK-CADWIIDL 244
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-224 |
1.00e-06 |
|
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: 47.35 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 31 KGEICVLLGPSGSGKSTLLNIIGgidqpdsgtitiqgktistlkekdltnyrrnhLGYVFQMYNLISHLNVEQNIDVgky 110
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG--------------------------------LALGGAQSATRRRSGVKAGCIV--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 111 lsknPLNKEELLQTLGlkehrykqpnQLSGGQQQRTSI----GRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKK 186
Cdd:cd03227 65 ----AAVSAELIFTRL----------QLSGGEKELSALalilALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK 130
|
170 180 190
....*....|....*....|....*....|....*...
gi 1466369044 187 yGNTIIIVTHNDAIKDMADRVIylhdgRIRENIKNTHK 224
Cdd:cd03227 131 -GAQVIVITHLPELAELADKLI-----HIKKVITGVYK 162
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-210 |
1.45e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 117 NKEELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAII---KNPDLLLCDEPTGALDYHtskDILQLIEDVNK--KYGNT 190
Cdd:PRK00635 788 EKIHALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTH---DIKALIYVLQSltHQGHT 864
|
90 100
....*....|....*....|
gi 1466369044 191 IIIVTHNDAIKDMADRVIYL 210
Cdd:PRK00635 865 VVIIEHNMHVVKVADYVLEL 884
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
120-205 |
1.95e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 120 ELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTskdiLQLIEDVNKKYGNTIIIVTH-- 196
Cdd:PRK15064 137 ELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHdr 212
|
90
....*....|..
gi 1466369044 197 ---NDAIKDMAD 205
Cdd:PRK15064 213 hflNSVCTHMAD 224
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-180 |
2.00e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 34 ICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIqgktistlKEKDLTNYRRNHLGYVFQMYNLISHLNVEQNIdvgKYLSK 113
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--------KNCNINNIAKPYCTYIGHNLGLKLEMTVFENL---KFWSE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 114 nPLNKEELLQT----LGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLI 180
Cdd:PRK13541 97 -IYNSAETLYAaihyFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-217 |
2.22e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITiqgktistlkekdltnyRRNHLGYVFQMYNLISHLNV 101
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 102 EQNIDVgKYLSKNPLNKE------ELLQTLGLKEHRYKQPNQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKD 175
Cdd:PRK13546 103 IENIEF-KMLCMGFKRKEikamtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1466369044 176 ILQLIEDVnKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRIRE 217
Cdd:PRK13546 182 CLDKIYEF-KEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKLKD 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-218 |
2.48e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.21 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTL-LNIIGGIDQPDsGTITIQGKTISTLKEKDLtnyrRNHLGYVFQMYNLISHl 99
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDIFD-GKIVIDGIDISKLPLHTL----RSRLSIILQDPILFSG- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 NVEQNIDVGKYLSKNPLnkEELLQTLGLKEHRYKQPNQL-----------SGGQQQRTSIGRAIIKNPDLLLCDEPTGAL 168
Cdd:cd03288 110 SIRFNLDPECKCTDDRL--WEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1466369044 169 DYHTsKDILQLIedVNKKYGN-TIIIVTHNDAIKDMADRVIYLHDGRIREN 218
Cdd:cd03288 188 DMAT-ENILQKV--VMTAFADrTVVTIAHRVSTILDADLVLVLSRGILVEC 235
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-215 |
2.90e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIqGKTIStlkekdltnyrrnhLGYVFQmyNLISHLN 100
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK--------------LGYFAQ--HQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 101 VEQNidVGKYLSKnpLNKEELLQTL-------GLKEHRYKQPN-QLSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYht 172
Cdd:PRK10636 390 ADES--PLQHLAR--LAPQELEQKLrdylggfGFQGDKVTEETrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL-- 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1466369044 173 skDILQLIEDVNKKYGNTIIIVTHN-DAIKDMADRVIYLHDGRI 215
Cdd:PRK10636 464 --DMRQALTEALIDFEGALVVVSHDrHLLRSTTDDLYLVHDGKV 505
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-196 |
3.19e-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: 47.44 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 27 FEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQgktistlkekdltnyRRNHLGYVFQ---MYN------LIS 97
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------------AKGKLFYVPQrpyMTLgtlrdqIIY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 98 HLNVEQNIDVGkyLSKNPLnkEELLQTLGLkEHRYKQP----------NQLSGGQQQRTSIGRAIIKNPDLLLCDEPTGA 167
Cdd:TIGR00954 538 PDSSEDMKRRG--LSDKDL--EQILDNVQL-THILEREggwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 1466369044 168 LdyhtSKDILQLIEDVNKKYGNTIIIVTH 196
Cdd:TIGR00954 613 V----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-230 |
4.68e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 117 NKEELLQTLGLKehrYKQPNQ----LSGGQQQRTSIGRAIikNPDLL----LCDEPTGALDYHTSKDILQLIEDVNKKyG 188
Cdd:PRK00635 455 SRLSILIDLGLP---YLTPERalatLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQ-G 528
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1466369044 189 NTIIIVTHNDAIKDMADRVI------------YLHDGRIRENIKNTHKIPAKDL 230
Cdd:PRK00635 529 NTVLLVEHDEQMISLADRIIdigpgagifggeVLFNGSPREFLAKSDSLTAKYL 582
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
137-208 |
5.32e-06 |
|
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: 45.68 E-value: 5.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 137 QLSGGQQQ------RTSIGRAIIKNPDLLLCDEPTGALD-YHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVI 208
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeENIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
31-57 |
1.78e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 44.31 E-value: 1.78e-05
10 20
....*....|....*....|....*...
gi 1466369044 31 KGEICVLLGPSGSGKSTLLN-IIGGIDQ 57
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNaLLPELVL 111
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-217 |
4.43e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTITIQGKTISTLKEKDLtnyRRNhlgyvFQMYNLISHL- 99
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQ-----FSMIPQDPVLf 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 100 --NVEQNIDvgKYLSKNPLNKEELLQTLGLKEHRYKQPNQL-----------SGGQQQRTSIGRAIIK-NPDLLLCDEPT 165
Cdd:PTZ00243 1397 dgTVRQNVD--PFLEASSAEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKkGSGFILMDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1466369044 166 GALDYHTSKDILQLIEDVNKKYgnTIIIVTHNDAIKDMADRVIYLHDGRIRE 217
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
138-208 |
5.03e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1466369044 138 LSGGQqqRTSIGRA--------IIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNtIIIVTHNDAIKDMADRVI 208
Cdd:PRK03918 789 LSGGE--RIALGLAfrlalslyLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQ-VIIVSHDEELKDAADYVI 864
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-215 |
6.05e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 21 VLKGIDFEIEKGEICVLLGPSGSGKSTL-LNIIG-----GIdqpdSGTITIQGKTIstlkekDLTNYRR---NHLGYVFQ 91
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrsygrNI----SGTVFKDGKEV------DVSTVSDaidAGLAYVTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 92 ---MYNLISHLNVEQNI---DVGKYLSKNPLNK-------EELLQTLGLKEHRYKQP-NQLSGGQQQRTSIGRAIIKNPD 157
Cdd:NF040905 345 drkGYGLNLIDDIKRNItlaNLGKVSRRGVIDEneeikvaEEYRKKMNIKTPSVFQKvGNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1466369044 158 LLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIKDMADRVIYLHDGRI 215
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-219 |
6.86e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 18 KTEVLKGIDFEIEKGEICVLLGPSGSGKSTLLNIIGGIDQPD---SGTITIQG---------KTISTLKEKDLtnyrrnH 85
Cdd:PLN03140 177 KLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGyrlnefvprKTSAYISQNDV------H 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 86 LGY---------------VFQMYNLISHLnVEQNIDVGKYLS---------------KNPLNKEELLQTLGL---KEHRY 132
Cdd:PLN03140 251 VGVmtvketldfsarcqgVGTRYDLLSEL-ARREKDAGIFPEaevdlfmkatamegvKSSLITDYTLKILGLdicKDTIV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 133 KQPNQ--LSGGQQQRTSIGRAIIKNPDLLLCDEPTGALDYHTSKDILQLIEDVNKKYGNTIIIVTHNDAIK--DMADRVI 208
Cdd:PLN03140 330 GDEMIrgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPEtfDLFDDII 409
|
250
....*....|....*.
gi 1466369044 209 YLHDGRI-----RENI 219
Cdd:PLN03140 410 LLSEGQIvyqgpRDHI 425
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
31-57 |
1.30e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 41.37 E-value: 1.30e-04
10 20
....*....|....*....|....*...
gi 1466369044 31 KGEICVLLGPSGSGKSTLLN-IIGGIDQ 57
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNaLLPELDL 132
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
22-48 |
1.31e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.31e-04
10 20
....*....|....*....|....*..
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTL 48
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
22-50 |
2.68e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 2.68e-04
10 20
....*....|....*....|....*....
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLN 50
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
135-208 |
4.55e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 135 PNQLSGGQQQ------RTSIGRAIIKN-------PDLLLcDEPTGALDY-HTSKdILQLIEDVNKKYGNTIIIVTHNDAI 200
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDSgHVSQ-LVDLVESMRRLGVEQIVVVSHDDEL 856
|
....*...
gi 1466369044 201 KDMADRVI 208
Cdd:PRK02224 857 VGAADDLV 864
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
31-52 |
6.58e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 39.80 E-value: 6.58e-04
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
122-208 |
6.73e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 122 LQTL---GLKEHRYKQP-NQLSGGQQQR---------TSIGRAiiknpdLLLCDEPTGALDYHtskDILQLIEDVNK--K 186
Cdd:PRK00349 811 LQTLvdvGLGYIKLGQPaTTLSGGEAQRvklakelskRSTGKT------LYILDEPTTGLHFE---DIRKLLEVLHRlvD 881
|
90 100
....*....|....*....|...
gi 1466369044 187 YGNTIIIVTHN-DAIKdMADRVI 208
Cdd:PRK00349 882 KGNTVVVIEHNlDVIK-TADWII 903
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-208 |
7.01e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 134 QP-NQLSGGQQQR---------TSIGRAiiknpdLLLCDEPTGALDYHtskDILQLIEDVNK--KYGNTIIIVTHN-DAI 200
Cdd:COG0178 822 QPaTTLSGGEAQRvklaselskRSTGKT------LYILDEPTTGLHFH---DIRKLLEVLHRlvDKGNTVVVIEHNlDVI 892
|
....*...
gi 1466369044 201 KdMADRVI 208
Cdd:COG0178 893 K-TADWII 899
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
22-48 |
1.15e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.15e-03
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
26-53 |
2.04e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 38.76 E-value: 2.04e-03
10 20
....*....|....*....|....*...
gi 1466369044 26 DFEIEKGEICVLLGPSGSGKSTLLNIIG 53
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALR 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
22-48 |
2.98e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 2.98e-03
10 20
....*....|....*....|....*..
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTL 48
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-196 |
3.32e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.67 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 25 IDFEIEKGeICVLLGPSGSGKSTLLNII--------GGIDQPDSGTITIQGKTIST-------------LKEKDLTNYRR 83
Cdd:COG3950 19 IDFDNPPR-LTVLVGENGSGKTTLLEAIalalsgllSRLDDVKFRKLLIRNGEFGDsaklilyygtsrlLLDGPLKKLER 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 84 NHLGYVFQMYNLISHLNVEQNID---------VGKYLSKNPLNKEELLQTL---------GLKEHRYKQ----------- 134
Cdd:COG3950 98 LKEEYFSRLDGYDSLLDEDSNLReflewlreyLEDLENKLSDELDEKLEAVrealnkllpDFKDIRIDRdpgrlvildkn 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466369044 135 -----PNQLSGGQQQRTSIG-----RAIIKNPDL---------LLCDEPtgalDYHTS----KDILQLIEDVNKKygNTI 191
Cdd:COG3950 178 geelpLNQLSDGERSLLALVgdlarRLAELNPALenplegegiVLIDEI----DLHLHpkwqRRILPDLRKIFPN--IQF 251
|
....*
gi 1466369044 192 IIVTH 196
Cdd:COG3950 252 IVTTH 256
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-49 |
3.51e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 3.51e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
22-50 |
4.27e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 4.27e-03
10 20
....*....|....*....|....*....
gi 1466369044 22 LKGIDFEIEKGEICVLLGPSGSGKSTLLN 50
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
10-55 |
9.76e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 35.90 E-value: 9.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1466369044 10 KSFGEdeyKTEvlkgidFEIEKGeICVLLGPSGSGKStllNIIGGI 55
Cdd:cd03278 10 KSFAD---KTT------IPFPPG-LTAIVGPNGSGKS---NIIDAI 42
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
31-63 |
9.89e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 36.45 E-value: 9.89e-03
10 20 30
....*....|....*....|....*....|...
gi 1466369044 31 KGEICVLLGPSGSGKSTLLNIIGGIDQPDSGTI 63
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| |
