|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-220 |
1.38e-111 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 318.91 E-value: 1.38e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYG----ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSA 81
Cdd:COG1136 3 PLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-220 |
2.38e-99 |
|
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: 287.85 E-value: 2.38e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGA----TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALR 83
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 RSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
7-220 |
4.21e-76 |
|
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: 228.78 E-value: 4.21e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYG----ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAL 82
Cdd:TIGR02211 1 LLKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQ 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-220 |
1.44e-74 |
|
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: 225.39 E-value: 1.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESR 78
Cdd:COG4181 4 SSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 79 RSALRRSDFGFVFQFGQLVPELSCVENVALPLRLNGvkRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARAL 158
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 159 VTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGR 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-220 |
7.88e-68 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 208.76 E-value: 7.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesRRSALR- 83
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAL---RGRALRr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 -RSDFGFVFQFGQLVPELSCVENV---ALP----LR--LNGVKRKEAEKAAYAwMERLEVEDLAAKRPGEVSGGQGQRVA 153
Cdd:COG3638 78 lRRRIGMIFQQFNLVPRLSVLTNVlagRLGrtstWRslLGLFPPEDRERALEA-LERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 154 VARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE---ARvaAYSDREVVVRDGR 220
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQvdlAR--RYADRIIGLRDGR 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-220 |
7.96e-67 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 205.29 E-value: 7.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATN-ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSdFGF 89
Cdd:COG2884 5 ENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR-IGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 VFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759535873 170 PTGALDSLNGERVMELLTEA-ARGTnaAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEInRRGT--TVLIATHDLElVDRMPKRVLELEDGR 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-220 |
9.35e-66 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 203.78 E-value: 9.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 1 MIPSGSLLSAEGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPE 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 77 SRrsalrrsdfGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVAR 156
Cdd:COG1116 81 DR---------GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 157 ALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAY-SDReVVV---RDGR 220
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADR-VVVlsaRPGR 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-220 |
7.94e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 204.56 E-value: 7.94e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 4 SGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalr 83
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 rsDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:COG3842 78 --NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTH---EArvAAYSDREVVVRDGR 220
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdqeEA--LALADRIAVMNDGR 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-220 |
5.88e-64 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 198.68 E-value: 5.88e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlPESRRSALRRsD 86
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLRR-K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVAL-PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVV 165
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 166 FADEPTGALD-SLNGE--RVMELLteAARGTnaAVVLVTHE---ARVAAysDREVVVRDGR 220
Cdd:COG1126 159 LFDEPTSALDpELVGEvlDVMRDL--AKEGM--TMVVVTHEmgfAREVA--DRVVFMDGGR 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-220 |
1.79e-63 |
|
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: 197.51 E-value: 1.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAL 82
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRsDFGFVFQFGQLVPELSCVENVALPLRLN-GVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:COG1127 81 RR-RIGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGK 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-220 |
4.63e-63 |
|
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: 195.43 E-value: 4.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalrrsDF 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR------NI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGR 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-220 |
1.12e-62 |
|
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: 203.21 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY-----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSA 81
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRsDFGFVFQ--FGQLVPELSCVENVALPLRLNGV-KRKEAEKAAYAWMERLE-VEDLAAKRPGEVSGGQGQRVAVARA 157
Cdd:COG1123 340 LRR-RVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGlPPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 158 LVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGR 482
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-220 |
1.76e-62 |
|
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: 195.09 E-value: 1.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGA-TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALR--RSDF 87
Cdd:cd03256 4 ENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLK---GKALRqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENV---ALPLR------LNGVKRKEAEKAAYAwMERLEVEDLAAKRPGEVSGGQGQRVAVARAL 158
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRstwrslFGLFPKEEKQRALAA-LERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 159 VTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGR 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-220 |
1.85e-62 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 194.23 E-value: 1.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYG----ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpesrrsalR 83
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 RSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAY-SDReVVV---RDGR 220
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADR-VVVlsaRPGR 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-220 |
3.36e-61 |
|
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: 191.18 E-value: 3.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSaL 82
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRSDFGFVFQ--FGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEV---EDLAAKRPGEVSGGQGQRVAVARA 157
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 158 LVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAY-SDREVVVRDGR 220
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGK 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-223 |
1.05e-58 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 185.02 E-value: 1.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYG----ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSA 81
Cdd:PRK11629 4 ILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGRSRD 223
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-220 |
2.83e-57 |
|
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: 181.55 E-value: 2.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSdFGFV 90
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR-MGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 91 FQFGQLVPELSCVENVALPLRLNGV-KRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759535873 170 PTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGK 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-220 |
1.35e-56 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 180.24 E-value: 1.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRrsd 86
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 fGFVFQFGQLVPELSCVENVAL---P-LRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAP 162
Cdd:COG1120 78 -AYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAArYADRLVLLKDGR 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-220 |
1.75e-56 |
|
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: 178.49 E-value: 1.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpESRRSALRRSDF 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD--DKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVAL-PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 167 ADEPTGALD-SLNGErVMELLTEAARgTNAAVVLVTHE---ARVAAysDREVVVRDGR 220
Cdd:cd03262 159 FDEPTSALDpELVGE-VLDVMKDLAE-EGMTMVVVTHEmgfAREVA--DRVIFMDDGR 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-220 |
4.03e-56 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.81 E-value: 4.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRsD 86
Cdd:COG1135 5 ENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEA----RVAaysDREVVVRDGR 220
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMdvvrRIC---DRVAVLENGR 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-220 |
9.14e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.56 E-value: 9.14e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELsalPESRRSALRRsdF 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV---ARDPAEVRRR--I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 168 DEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRElAAEGK--TVLLSTHYlEEAERLCDRVAIIDKGR 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-215 |
2.31e-55 |
|
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: 176.62 E-value: 2.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATN----ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRsD 86
Cdd:cd03258 5 KNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARR-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEA--------RVAAYSDREVV 215
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMevvkricdRVAVMEKGEVV 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-220 |
4.45e-55 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 175.60 E-value: 4.45e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpESRRSALRRsD 86
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELRR-K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQF--GQLVpELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRV 164
Cdd:COG1122 77 VGLVFQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 165 VFADEPTGALDSLNGERVMELLTEAARgTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDlVAELADRVIVLDDGR 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-212 |
7.34e-55 |
|
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: 174.34 E-value: 7.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSDFGFV 90
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 91 FQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEP 170
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 759535873 171 TGALDSLNGERVMELLTEAARgTNAAVVLVTHEARVAAYSDR 212
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELND-EGKTIIIVTHDPEVAKQADR 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-220 |
1.80e-54 |
|
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: 173.42 E-value: 1.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 9 SAEGLRKSY--GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrrSALRRSD 86
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS----LKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQF--GQLVpELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRV 164
Cdd:cd03225 77 VGLVFQNpdDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 165 VFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKlKAEGK--TIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-220 |
1.95e-54 |
|
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: 181.64 E-value: 1.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY--GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD---EGAIHYNGTELSALPEsrrsA 81
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE----A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFVFQ--FGQLVPeLSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALV 159
Cdd:COG1123 80 LRGRRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 160 TAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGR 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-220 |
5.03e-54 |
|
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: 173.45 E-value: 5.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATN----ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpesRRSAL 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR----RRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRSDFGFVFQ--FGQLVPELSCVENVALPLRLNGVKRKEAEkaAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVARALV 159
Cdd:COG1124 77 FRRRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 160 TAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAY-SDREVVVRDGR 220
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGR 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-220 |
6.49e-53 |
|
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: 168.52 E-value: 6.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpeSRRSALRRSDFGFV 90
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL--EDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 91 FQFGQLVPELSCVENVALPLrlngvkrkeaekaayawmerlevedlaakrpgevSGGQGQRVAVARALVTAPRVVFADEP 170
Cdd:cd03229 82 FQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759535873 171 TGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAY-SDREVVVRDGR 220
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-220 |
2.29e-52 |
|
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: 169.02 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYG-ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesRRSALR-- 83
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKL---RGKKLRkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 RSDFGFVFQFGQLVPELSCVENV---------ALPLRLNGVKRKEAEKAAYAwMERLEVEDLAAKRPGEVSGGQGQRVAV 154
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEEDKERALSA-LERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 155 ARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGE 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
15-220 |
4.17e-52 |
|
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: 167.43 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 15 KSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSdFGFVFQF 93
Cdd:TIGR02673 9 KAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR-IGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 94 GQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGA 173
Cdd:TIGR02673 88 FRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759535873 174 LDSLNGERVMELLTEA-ARGTnaAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:TIGR02673 168 LDPDLSERILDLLKRLnKRGT--TVIVATHDLSlVDRVAHRVIILDDGR 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-220 |
4.30e-52 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 171.79 E-value: 4.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalrrsDF 87
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR------NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 168 DEPTGALD-SLngeRVmELLTEAA---RGTNAAVVLVTH---EARvaAYSDREVVVRDGR 220
Cdd:COG3839 158 DEPLSNLDaKL---RV-EMRAEIKrlhRRLGTTTIYVTHdqvEAM--TLADRIAVMNDGR 211
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
8-220 |
4.33e-52 |
|
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: 167.89 E-value: 4.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNA----LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALR 83
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLrkqvLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 RSdFGFVFQFGQLVPELSCVENVALPLRLN-GVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAP 162
Cdd:TIGR02982 82 RR-IGYIFQAHNLLGFLTARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGK 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-220 |
1.08e-51 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 167.80 E-value: 1.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNG-----TELSALPESRRSA 81
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFVFQFGQ--LVPELSCVENVALPLRLNGVKR-KEAEKAAYAWMERLEvedLAAKR----PGEVSGGQGQRVAV 154
Cdd:PRK11701 86 LLRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVE---IDAARiddlPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 155 ARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMKQGR 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-220 |
1.11e-51 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 176.84 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSA 81
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEaARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQAERVIEIRDGE 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-220 |
1.65e-51 |
|
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: 166.64 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrrsdF 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP------V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGK 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-220 |
2.45e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 169.56 E-value: 2.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpeSRRSALRRsDF 87
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLPPRER-RV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 168 DEPTGALDS-----LngERVM-ELLTEaargTNAAVVLVTH---EA-RVAaysDREVVVRDGR 220
Cdd:COG1118 158 DEPFGALDAkvrkeL--RRWLrRLHDE----LGGTTVFVTHdqeEAlELA---DRVVVMNQGR 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-220 |
7.52e-51 |
|
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: 165.42 E-value: 7.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALrrsd 86
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 fGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:COG4555 77 -GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 167 ADEPTGALDSLNGERVMELLtEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:COG4555 156 LDEPTNGLDVMARRLLREIL-RALKKEGKTVLFSSHIMQeVEALCDRVVILHKGK 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-202 |
1.18e-50 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 165.42 E-value: 1.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATN----ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlPESRRsa 81
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 lrrsdfGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTH 202
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-216 |
2.64e-50 |
|
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: 166.00 E-value: 2.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPP---DEGAIHYNGTELSALPESRR 79
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 80 SALRRSDFGFVFQ--FGQLVPELSCVENVALPLRL-NGVKRKEAEKAAYAWMERL---EVEDLAAKRPGEVSGGQGQRVA 153
Cdd:COG0444 81 RKIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVglpDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 154 VARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAY-SDReVVV 216
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADR-VAV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-220 |
3.47e-50 |
|
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: 162.58 E-value: 3.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 15 KSYGA-TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSdFGFVFQF 93
Cdd:cd03292 8 KTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 94 GQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGA 173
Cdd:cd03292 87 FRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759535873 174 LDSLNGERVMELLTEA-ARGTnaAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:cd03292 167 LDPDTTWEIMNLLKKInKAGT--TVVVATHAKElVDTTRHRVIALERGK 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-223 |
3.99e-50 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 163.03 E-value: 3.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 2 IPSGSLLSAEGLRKSYG----ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPES 77
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 78 RRSALRRSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARA 157
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 158 LVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGRSRD 223
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-220 |
4.10e-50 |
|
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: 161.45 E-value: 4.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 9 SAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRrsdfG 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 89 FVFQfgqlvpelscvenvalplrlngvkrkeaekaayaWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFAD 168
Cdd:cd03214 77 YVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759535873 169 EPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGR 175
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-220 |
5.15e-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: 162.89 E-value: 5.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNaLDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalrrsDF 87
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR------DI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGK 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-220 |
7.26e-50 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 163.58 E-value: 7.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 9 SAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSDFG 88
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 89 FVFQ-FGqLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03294 106 MVFQsFA-LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARGTNAAVVLVTH---EA-RVAaysDREVVVRDGR 220
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHdldEAlRLG---DRIAIMKDGR 238
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-220 |
1.59e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.75 E-value: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALRRSdF 87
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQ-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPElSCVENVALPLRLNgvKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLR--ERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTH-EARVAAYSDREVVVRDGR 220
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHdPEQIERVADRVLTLEAGR 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-216 |
6.31e-49 |
|
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: 160.59 E-value: 6.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 4 SGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSA-- 81
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSdfgfvFQFGQLVPELSCVENVALP-------------LRLNGVKRKEAE--KAAYAWMERLEVEDLAAKRPGEVSG 146
Cdd:COG0411 81 IART-----FQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEREarERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 147 GQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDReVVV 216
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDlVMGLADR-IVV 225
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-220 |
6.37e-49 |
|
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: 163.67 E-value: 6.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalrrsDF 87
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR------DY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGV 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-220 |
7.25e-49 |
|
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: 159.52 E-value: 7.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY------GAT-NALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYN----GTELSALP 75
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 76 ESRRSALRRSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAV 154
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 155 ARALVTAPRVVFADEPTGALDSLNGERVMELLTEA-ARGTnaAVVLVTH-EARVAAYSDREVVVRDGR 220
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGT--AIIGIFHdEEVREAVADRVVDVTPFS 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-220 |
9.96e-48 |
|
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: 156.57 E-value: 9.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVP-----PDEGAIHYNGTELSALPEsRRSAL 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDV-DVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRSdFGFVFQFGQLVPeLSCVENVALPLRLNGVKRKEAEKAAYAW-MERLEVEDLAAKR--PGEVSGGQGQRVAVARALV 159
Cdd:cd03260 80 RRR-VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEaLRKAALWDEVKDRlhALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 160 TAPRVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTHE----ARVAaysDREVVVRDGR 220
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNmqqaARVA---DRTAFLLNGR 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-171 |
4.65e-47 |
|
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: 152.42 E-value: 4.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpeSRRSALRRSDFGFVFQFGQLVPELSC 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT----DDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 103 VENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKR----PGEVSGGQGQRVAVARALVTAPRVVFADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-220 |
9.60e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.17 E-value: 9.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELsalpesrrsAL 82
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---------RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRSDFGFVFQFGQLVPE--LSCVENVAL----PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVAR 156
Cdd:COG1121 73 ARRRIGYVPQRAEVDWDfpITVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 157 ALVTAPRVVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGK--TILVVTHDlGAVREYFDRVLLLNRGL 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-220 |
2.36e-45 |
|
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: 149.94 E-value: 2.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALrrsd 86
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 fGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAekAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:COG4133 78 -AYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 167 ADEPTGALDSLNGERVMELLTE-AARGtnAAVVLVTHEARVAAySDREVVVRDGR 220
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAhLARG--GAVLLTTHQPLELA-AARVLDLGDFK 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-215 |
2.51e-45 |
|
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: 150.67 E-value: 2.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAL--RRS 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgiGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dfgfvFQFGQLVPELSCVENVALPLRL----------NGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVA 155
Cdd:cd03219 81 -----FQIPRLFPELTVLENVMVAAQArtgsglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 156 RALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGtNAAVVLVTHE-ARVAAYSDREVV 215
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDmDVVMSLADRVTV 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-220 |
6.03e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 149.91 E-value: 6.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 26 AEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRR--SALrrsdfgfvFQFGQLVPELSCV 103
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpvSML--------FQENNLFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 104 ENVAL---P-LRLNGVKRKEAEKAAyawmERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD-SLN 178
Cdd:COG3840 90 QNIGLglrPgLKLTAEQRAQVEQAL----ERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 759535873 179 GErVMELLTEAARGTNAAVVLVTH---EARVAAysDREVVVRDGR 220
Cdd:COG3840 166 QE-MLDLVDELCRERGLTVLMVTHdpeDAARIA--DRVLLVADGR 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-220 |
1.04e-44 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 148.56 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalrrsDFGFV 90
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR------DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 91 FQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEP 170
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759535873 171 TGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQ 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-203 |
1.08e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.47 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 15 KSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGteLSALPESRRSALRRSDFGFVFQFG 94
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLIRQEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 95 QLVPELSCVENVAL-PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGA 173
Cdd:PRK09493 87 YLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190
....*....|....*....|....*....|...
gi 759535873 174 LD-SLNGE--RVMELLTEAArgtnAAVVLVTHE 203
Cdd:PRK09493 167 LDpELRHEvlKVMQDLAEEG----MTMVIVTHE 195
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
8-214 |
1.35e-44 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 149.57 E-value: 1.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELsALPESRRSALR---- 83
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDRDGELVpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 ------RSDFGFVFQFGQLVPELSCVENVAL-PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVAR 156
Cdd:COG4598 88 rqlqriRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 157 ALVTAPRVVFADEPTGALD-SLNGE--RVMELLTEAARgtnaAVVLVTHEARVAaysdREV 214
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDpELVGEvlKVMRDLAEEGR----TMLVVTHEMGFA----RDV 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-222 |
1.50e-44 |
|
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: 148.20 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRrsalrrsdF 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR--------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 168 DEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHE-ARVAAYSDREVVVRDGRSR 222
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRElARAGK--TVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-220 |
1.95e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.79 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALRRsd 86
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRDAQAA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 fG--FVFQFGQLVPELSCVENVAL---PLRLNGVKRKEAEKAAYAWMERLEVeDLAAKRP-GEVSGGQGQRVAVARALVT 160
Cdd:COG1129 80 -GiaIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGL-DIDPDTPvGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 161 APRVVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTH---EarVAAYSDREVVVRDGR 220
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRlKAQGV--AIIYISHrldE--VFEIADRVTVLRDGR 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-220 |
3.57e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.47 E-value: 3.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 9 SAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrrSALRRSDFG 88
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP----LEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 89 FVFQFgqlvpelscvenvalplrlngvkrkeaekaayawmerlevedlaakrpgevSGGQGQRVAVARALVTAPRVVFAD 168
Cdd:cd00267 77 YVPQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759535873 169 EPTGALDSLNGERVMELLTEAARGtNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
7-220 |
1.95e-43 |
|
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: 146.51 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHY-----NGTELSALPESRRSA 81
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFVFQFGQ--LVPELSCVENVALPLRLNGVKR-KEAEKAAYAWMERLEVE-DLAAKRPGEVSGGQGQRVAVARA 157
Cdd:TIGR02323 83 LMRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 158 LVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGR 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-220 |
2.96e-42 |
|
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: 142.64 E-value: 2.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYG--ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpeSRRSALRRS 85
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVV 165
Cdd:cd03263 77 -LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 166 FADEPTGALDSLNGERVMELLTEAARGTnaAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAeALCDRIAIMSDGK 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-220 |
3.82e-42 |
|
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: 140.61 E-value: 3.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESrrsalRRSDF 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-----VKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALplrlngvkrkeaekaayawmerlevedlaakrpgevSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 168 DEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTH-EARVAAYSDREVVVRDGR 220
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGK--TILLSSHiLEEAERLCDRVAILNNGR 172
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-207 |
4.45e-42 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 142.85 E-value: 4.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTE--LSALPESRRSALRRS 85
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 DFGFVFQFGQLVPELSCVEN-VALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRV 164
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 759535873 165 VFADEPTGALDSLNGERVMELLTEAArGTNAAVVLVTHEARVA 207
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVA 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-220 |
4.81e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 145.33 E-value: 4.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSd 86
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGR 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-220 |
5.48e-42 |
|
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: 142.44 E-value: 5.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGA-TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRrsaLRRSdFGF 89
Cdd:cd03295 4 ENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRK-IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 VFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWME--RLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARGTNAAVVLVTH---EARVAAysDREVVVRDGR 220
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHdidEAFRLA--DRIAIMKNGE 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-220 |
6.20e-42 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 149.14 E-value: 6.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPEsrrsA 81
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP----A 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFVFQFGQLVPElSCVENVALplrlngvKRKEAEKAA-YAWMERLEVEDLAAKRP-------GE----VSGGQG 149
Cdd:COG4988 408 SWRRQIAWVPQNPYLFAG-TIRENLRL-------GRPDASDEElEAALEAAGLDEFVAALPdgldtplGEggrgLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 150 QRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGtnAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQADRILVLDDGR 548
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-227 |
1.08e-41 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 142.15 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlPESRRsalrrsd 86
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 fGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDRE-VVVRDGRSRDMERL 227
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATElVLLSPGPGRVVERL 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-220 |
2.38e-41 |
|
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: 140.12 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 33 GEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSA------LPESRRSalrrsdFGFVFQFGQLVPELSCVENV 106
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRK------IGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 107 A--LPLRLNGVKRKEAEKAayawMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVME 184
Cdd:cd03297 97 AfgLKRKRNREDRISVDEL----LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 759535873 185 LLTEAARGTNAAVVLVTHEARVAAY-SDREVVVRDGR 220
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGR 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-175 |
2.43e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 143.33 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 1 MIPSGSLLSAEGLRKSY-----------GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGT 69
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 70 ELSALPESRRSALRRsDFGFVFQ--FGQLVPELSCVENVALPLRLNGVK-RKEAEKAAYAWMER--LEVEDlAAKRPGEV 144
Cdd:COG4608 81 DITGLSGRELRPLRR-RMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLAsKAERRERVAELLELvgLRPEH-ADRYPHEF 158
|
170 180 190
....*....|....*....|....*....|.
gi 759535873 145 SGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-220 |
2.80e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 144.32 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalrrs 85
Cdd:PRK09452 13 PLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 DFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAyawMERL---EVEDLAAKRPGEVSGGQGQRVAVARALVTAP 162
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRV---MEALrmvQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 163 RVVFADEPTGALD-SLNGERVMElLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:PRK09452 164 KVLLLDESLSALDyKLRKQMQNE-LKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGR 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-220 |
3.27e-41 |
|
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: 140.55 E-value: 3.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrrsaLRRSDFGFV 90
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 91 FQFGQLVPELSCVENVALPLRLNGVKRK--EAEKAAYAwMERLEV---EDLAAKRPGEVSGGQGQRVAVARALVTAPRVV 165
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERppEAEIRAKV-HELLKLvqlDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 166 FADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGR 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-220 |
4.64e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 140.68 E-value: 4.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPeSRRSALRR-- 84
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELARRRav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 85 ----SDFGFVFQfgqlvpelscVENV----ALPLRLNgvkRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVAR 156
Cdd:PRK13548 81 lpqhSSLSFPFT----------VEEVvamgRAPHGLS---RAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 157 ALV------TAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAArYADRIVLLHQGR 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-207 |
5.58e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 5.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 12 GLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTE--LSALPESRRSALRRSDFGF 89
Cdd:COG4161 7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKAIRLLRQKVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 VFQFGQLVPELSCVEN-VALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFAD 168
Cdd:COG4161 87 VFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 759535873 169 EPTGALDSLNGERVMELLTEAArGTNAAVVLVTHEARVA 207
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFA 204
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
7-220 |
6.79e-41 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 142.52 E-value: 6.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNaLDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrrsd 86
Cdd:NF040840 1 MIRIENLSKDWKEFK-LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:NF040840 74 IAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:NF040840 154 LDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEAlSLADRVGIMLNGR 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-220 |
1.84e-40 |
|
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: 144.83 E-value: 1.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY-----------GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPdEGAIHYNGTELSALP 75
Cdd:COG4172 275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 76 ESRRSALRRsDFGFVFQ--FGQLVPELSCVENVALPLRLNGVK--RKEAEKAAYAWMErlEV---EDLAAKRPGEVSGGQ 148
Cdd:COG4172 354 RRALRPLRR-RMQVVFQdpFGSLSPRMTVGQIIAEGLRVHGPGlsAAERRARVAEALE--EVgldPAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 149 GQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARV-AAYSDREVVVRDGR 220
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVvRALAHRVMVMKDGK 503
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-220 |
4.44e-40 |
|
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: 138.35 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 19 ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRsDFGFVFQF--GQL 96
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK-KVGLVFQFpeHQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 97 VpELSCVENVAL-PLRLnGVKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGAL 174
Cdd:TIGR04521 96 F-EETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 759535873 175 DSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGK 220
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-220 |
5.72e-40 |
|
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: 139.55 E-value: 5.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 38 IMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrrsdFGFVFQFGQLVPELSCVENVALPLRLNGVKR 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH------INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 118 KEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAV 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....
gi 759535873 198 VLVTHEARVA-AYSDREVVVRDGR 220
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-220 |
6.11e-40 |
|
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: 136.41 E-value: 6.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrRSDF 87
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---RAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRlngVKRKEAEKAAYAWMERL--EVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVV 165
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAY---ARRRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 166 FADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRElRDEGV--TILLVEQNARFAlEIADRAYVLERGR 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-212 |
8.14e-40 |
|
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: 136.12 E-value: 8.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 9 SAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGtelsalpesRRSALRRSDFG 88
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG---------KPLEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 89 FVFQFGQLVPE--LSCVENVALPLR-----LNGVKRKEAEKAAYAwMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:cd03235 72 YVPQRRSIDRDfpISVRDVVLMGLYghkglFRRLSKADKAKVDEA-LERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEAARgTNAAVVLVTHE-ARVAAYSDR 212
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDlGLVLEYFDR 201
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-220 |
1.01e-39 |
|
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: 134.43 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATN--ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALRRS 85
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dFGFVFQFGQLVPElSCVENValplrlngvkrkeaekaayawmerlevedlaakrpgeVSGGQGQRVAVARALVTAPRVV 165
Cdd:cd03228 78 -IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 166 FADEPTGALDSLNGERVMELLTEAARGTnaAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-202 |
1.63e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 137.55 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSA--------LPESRR 79
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigyLPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 80 salrrsdfgfvfqfgqLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALV 159
Cdd:COG4152 82 ----------------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 160 TAPRVVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTH 202
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRElAAKGT--TVIFSSH 187
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-220 |
3.40e-39 |
|
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: 143.05 E-value: 3.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 18 GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALRRSdFGFVFQFGQLV 97
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQ-IGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PElSCVENVAL--PlrlnGVKRKEAEKAAyawmERLEVEDLAAKRP-------GE----VSGGQGQRVAVARALVTAPRV 164
Cdd:COG2274 562 SG-TIRENITLgdP----DATDEEIIEAA----RLAGLHDFIEALPmgydtvvGEggsnLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 165 VFADEPTGALDSLNGERVMELLTEAARGtnAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGR 686
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-220 |
1.29e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.09 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALR--- 83
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 --RSDFGFVFqfgqlvpelSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALV-- 159
Cdd:COG4559 81 pqHSSLAFPF---------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 160 -----TAPRVVFADEPTGALDSLNGERVMELLTEAARgTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAqYADRILLLHQGR 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-220 |
5.96e-38 |
|
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: 129.47 E-value: 5.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALRRSdF 87
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--FASPRDARRAG-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFgqlvpelscvenvalplrlngvkrkeaekaayawmerlevedlaakrpgevSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03216 78 AMVYQL---------------------------------------------------SVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 168 DEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTH-EARVAAYSDREVVVRDGR 220
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRlRAQGV--AVIFISHrLDEVFEIADRVTVLRDGR 159
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-204 |
2.53e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 129.52 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD---EGAIHYNGTELSALP-ESRRsalr 83
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPaEQRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 rsdFGFVFQFGQLVPELSCVENVALPLRlNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:COG4136 78 ---IGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEA 204
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-212 |
2.72e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.93 E-value: 2.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCL---------AGIvppdEGAIHYNGTELSAlPESR 78
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgARV----EGEILLDGEDIYD-PDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 79 RSALRRSdFGFVFQfgQLVP-ELSCVENVALPLRLNGVKRK--------EAEKAAYAWMerlEVED-LaaKRPG-EVSGG 147
Cdd:COG1117 87 VVELRRR-VGMVFQ--KPNPfPKSIYDNVAYGLRLHGIKSKseldeiveESLRKAALWD---EVKDrL--KKSAlGLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 148 QGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTHE----ARVaaySDR 212
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNmqqaARV---SDY 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-215 |
1.04e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 129.32 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPES---------R 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 79 RSALRRSDFGFVFQFGQLVPELSCVENV-ALPLRLNGVKRKEAEKAAYAWMERLEVEDLA-AKRPGEVSGGQGQRVAVAR 156
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 157 ALVTAPRVVFADEPTGALD-SLNGE--RVMELLTEAARgtnaAVVLVTHEARVAAYSDREVV 215
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDpELVGEvlRIMQQLAEEGK----TMVVVTHEMGFARHVSSHVI 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-219 |
1.06e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 129.42 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSY---------GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPE 76
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 77 SRRSALRRsDFGFVFQ--FGQLVPELSCVENVALPLR-LNGVKRKEAEKAAYAWMERLEVED-LAAKRPGEVSGGQGQRV 152
Cdd:PRK10419 82 AQRKAFRR-DIQMVFQdsISAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 153 AVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDG 219
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-220 |
1.19e-36 |
|
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: 134.89 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEGLRKSY--GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPEsrrS 80
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE---D 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 81 ALRRSdFGFVFQ----FGQlvpelSCVENvalpLRLngvKRKEA-EKAAYAWMERLEVEDLAAKRP-------GE----V 144
Cdd:COG4987 406 DLRRR-IAVVPQrphlFDT-----TLREN----LRL---ARPDAtDEELWAALERVGLGDWLAALPdgldtwlGEggrrL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 145 SGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGtnAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERMDRILVLEDGR 546
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-220 |
1.35e-36 |
|
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: 127.87 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 10 AEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGteLSALPESRRsaLRRSdFGF 89
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPRE--VRRR-IGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 VFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759535873 170 PTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGR 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-220 |
1.56e-36 |
|
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: 134.04 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGA----TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD----EGAIHYNGTELSALPES 77
Cdd:COG4172 5 PLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 78 RRSALRRSDFGFVFQ--FGQLVPELSCVENVALPLRL-NGVKRKEAEKAAYAWMERLEVEDlAAKR----PGEVSGGQGQ 150
Cdd:COG4172 85 ELRRIRGNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPD-PERRldayPHQLSGGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 151 RVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlGVVRRFADRVAVMRQGE 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-220 |
2.30e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 131.00 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 13 LRKSYGATnALDgAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSA------LPESRRSalrrsd 86
Cdd:TIGR02142 5 FSKRLGDF-SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENValplrLNGVKRKEAEKAAYAW---MERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:TIGR02142 77 IGYVFQEARLFPHLSVRGNL-----RYGMKRARPSERRISFervIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:TIGR02142 152 LLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGR 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-220 |
3.47e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.87 E-value: 3.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 2 IPSGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesrrsa 81
Cdd:PRK11247 7 LNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 lrRSDFGFVFQFGQLVPELSCVENVALPLRlnGVKRKEAEKAayawMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:PRK11247 80 --REDTRLMFQDARLLPWKKVIDNVGLGLK--GQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGK 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-220 |
4.11e-36 |
|
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: 126.45 E-value: 4.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 29 SIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAlrrsdfGFVFQFGQLVPELSCVENVAL 108
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV------SMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 109 P----LRLNGVKRKEAEKAAyawmERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVME 184
Cdd:cd03298 94 GlspgLKLTAEDRQAIEVAL----ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 759535873 185 LLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGR 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-220 |
1.07e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.85 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRR--SALrrsdfgfvFQFGQLVPELSCVEN 105
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRpvSML--------FQENNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 106 VAL---P-LRLNGVKRKEAEKAAyawmERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD-SLNGE 180
Cdd:PRK10771 92 IGLglnPgLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 181 rVMELLTEAARGTNAAVVLVTHE----ARVAaysDREVVVRDGR 220
Cdd:PRK10771 168 -MLTLVSQVCQERQLTLLMVSHSledaARIA---PRSLVVADGR 207
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-220 |
1.70e-35 |
|
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: 124.97 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 29 SIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrrsdFGFVFQFGQLVPELSCVENVAL 108
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 109 ----PLRLNGVKRKEAEKAAyawmERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVME 184
Cdd:TIGR01277 94 glhpGLKLNAEQQEKVVDAA----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 759535873 185 LLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGK 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-220 |
2.21e-35 |
|
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: 125.09 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRrs 85
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEK--AAYAWMERLEveDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:COG0410 80 -IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADleRVYELFPRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRlNREGV--TILLVEQNARFAlEIADRAYVLERGR 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-224 |
2.82e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 125.25 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTEL-SALPESRRSAL-- 82
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 -RRSDFGFVFQFGQLVPELSCVENVAL-PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVT 160
Cdd:PRK11264 82 qLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 161 APRVVFADEPTGALDSlngERVMELLT--EAARGTNAAVVLVTHE-------ARVAAYSDREVVVRDGRSRDM 224
Cdd:PRK11264 162 RPEVILFDEPTSALDP---ELVGEVLNtiRQLAQEKRTMVIVTHEmsfardvADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-224 |
7.25e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 124.25 E-value: 7.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIV-----PPDEGAIHYNGTELSALPESRrs 80
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 81 aLRRSdFGFVFQFGQLVPELSCVENVALPLRLNGV--KRKEAEKAAYAWMERL----EVEDLAAKRPGEVSGGQGQRVAV 154
Cdd:PRK14247 80 -LRRR-VQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAqlwdEVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 155 ARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTH----EARVA---AYSDREVVVRDGRSRDM 224
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHfpqqAARISdyvAFLYKGQIVEWGPTREV 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-220 |
1.05e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 123.06 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSdFGF 89
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 VFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759535873 170 PTGALDSLNGERVMELLTEAARgTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDiGLISRRSYRMLTLSDGH 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
13-220 |
1.21e-34 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 126.37 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 13 LRKSYGATnALDgAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTEL------SALPESRRSalrrsd 86
Cdd:COG4148 7 FRLRRGGF-TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRR------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENvalpLRLnGVKRKEAEKAAYAW---MERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGN----LLY-GRKRAPRAERRISFdevVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGR 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-220 |
1.99e-34 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 121.92 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGeVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALrrsdf 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759535873 168 DEPTGALDSLNGERVMELLTEAarGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEdVESLCNQVAVLNKGK 206
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-207 |
2.85e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 125.72 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrrsd 86
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA 207
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEA 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-219 |
4.45e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 4.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 9 SAEGLRKSYG-ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGtelsalpESRRSALRRSDF 87
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-------KPIKAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQ------FGqlvpelscvENVALPLRLnGVKRKEAEKA-AYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVT 160
Cdd:cd03226 74 GYVMQdvdyqlFT---------DSVREELLL-GLKELDAGNEqAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 161 APRVVFADEPTGALDSLNGERVMEL-LTEAARGTnaAVVLVTHEARVAA-YSDREVVVRDG 219
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELiRELAAQGK--AVIVITHDYEFLAkVCDRVLLLANG 202
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-220 |
4.74e-34 |
|
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: 121.16 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALRRsDFGFVFQFGQLVPE 99
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRR-NIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 lSCVENVALPLRLngVKRKEAEKAAyawmERLEVEDLAAKRP-------GE----VSGGQGQRVAVARALVTAPRVVFAD 168
Cdd:cd03245 93 -TLRDNITLGAPL--ADDERILRAA----ELAGVTDFVNKHPngldlqiGErgrgLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759535873 169 EPTGALDSLNGERVMELLTEAARGTnaAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGR 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-223 |
1.12e-33 |
|
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: 120.17 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATN----ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSAL 82
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP---AEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRsdFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAP 162
Cdd:cd03266 78 RR--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLtEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGRSRD 223
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFI-RQLRALGKCILFSTHImQEVERLCDRVVVLHRGRVVY 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-220 |
1.46e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 121.66 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 5 GSLLSAEGLRKSY--GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpESRRSAL 82
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRSdFGFVFQF--GQLVPelSCVEN-VALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALV 159
Cdd:PRK13635 80 RRQ-VGMVFQNpdNQFVG--ATVQDdVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 160 TAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGE 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-171 |
3.18e-33 |
|
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: 119.55 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrRSDF 87
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA---RAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEveDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
....
gi 759535873 168 DEPT 171
Cdd:TIGR03410 156 DEPT 159
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-219 |
5.73e-33 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 121.73 E-value: 5.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpesRRSAlRRSDFGFV 90
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-----RLHA-RDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 91 FQFGQLVPELSCVENVALPLRLngVKRKEAEKAAY------AWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRV 164
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTV--LPRRERPNAAAikakvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 165 VFADEPTGALDSlngERVMEL------LTEAARGTNaavVLVTHEARVAA-YSDREVVVRDG 219
Cdd:PRK10851 158 LLLDEPFGALDA---QVRKELrrwlrqLHEELKFTS---VFVTHDQEEAMeVADRVVVMSQG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-220 |
1.37e-32 |
|
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: 118.69 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSY--GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGteLSALPESRRSALRRS 85
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dFGFVFQF--GQLVPelSCVEN-VALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAP 162
Cdd:TIGR04520 79 -VGMVFQNpdNQFVG--ATVEDdVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGK 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-220 |
1.79e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALRRSd 86
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR--IRSPRDAIALG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVAL---PLRLNGVKRKEAEKAAYAWMER--LEVeDLAAKrPGEVSGGQGQRVAVARALVTA 161
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERygLDV-DPDAK-VEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRlAAEGK--SIIFITHKLReVMAIADRVTVLRRGK 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
2.31e-32 |
|
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: 117.18 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlPESRRSAlrrsdfgfVFQFGQLVPELSC 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMV--------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENVALPLR--LNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGE 180
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 759535873 181 RVMELLTEAARGTNAAVVLVTHEARVAAY-SDREVVVRDG 219
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-220 |
3.00e-32 |
|
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: 116.87 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrRSDF 87
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA---RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 168 DEPTGALDSLNGERVMELLTE-AARGTNaavVLVT-HEAR-VAAYSDREVVVRDGR 220
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKIlKDRGIG---VLITdHNVReTLSITDRAYIIYEGK 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-220 |
3.08e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.78 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 4 SGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESR--RSA 81
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiaRMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSdfgfvFQFGQLVPELSCVEN--VALPLRLN-----------GVKRKEAEKAAYA--WMERLEVEDLAAKRPGEVSG 146
Cdd:PRK11300 82 VVRT-----FQHVRLFREMTVIENllVAQHQQLKtglfsgllktpAFRRAESEALDRAatWLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 147 GQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKlVMGISDRIYVVNQGT 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-219 |
3.61e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.20 E-value: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 29 SIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALR--RSDFGFVFQFgqlvPELSCVENV 106
Cdd:PRK13634 29 SIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVIT--AGKKNKKLKplRKKVGIVFQF----PEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 107 AL------PLRLnGVKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNG 179
Cdd:PRK13634 103 VEkdicfgPMNF-GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 180 ERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDG 219
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEdAARYADQIVVMHKG 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-220 |
4.59e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 119.44 E-value: 4.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 15 KSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpesrRSALRRSDFGFVFQFG 94
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT------HRSIQQRDICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 95 QLVPELSCVENVALPLRLNGVKRKEAEKAAyawMERLEVEDLAA---KRPGEVSGGQGQRVAVARALVTAPRVVFADEPT 171
Cdd:PRK11432 88 ALFPHMSLGENVGYGLKMLGVPKEERKQRV---KEALELVDLAGfedRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759535873 172 GALDSlNGERVM-ELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:PRK11432 165 SNLDA-NLRRSMrEKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGK 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-219 |
7.63e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 117.04 E-value: 7.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAihynGTELSALPESRRSALR-- 83
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSA----GSHIELLGRTVQREGRla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 ------RSDFGFVFQFGQLVPELSCVENVAL------PLRLNGVK--RKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQG 149
Cdd:PRK09984 79 rdirksRANTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 150 QRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDG 219
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQG 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-219 |
8.57e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.41 E-value: 8.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCL--AGIVPPD---EGAIHYNGTELSAlPESRRSA 81
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIYS-PRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRsDFGFVFQFGQLVPeLSCVENVALPLRLNGVKRKE--------AEKAAYAWMErleVEDLAAKRPGEVSGGQGQRVA 153
Cdd:PRK14239 84 LRK-EIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQvldeavekSLKGASIWDE---VKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 154 VARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTHEARVAA-YSDREVVVRDG 219
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASrISDRTGFFLDG 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-220 |
9.58e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 117.24 E-value: 9.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALR--RSDFGFVFQFgqlv 97
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT--PETGNKNLKklRKKVSLVFQF---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PELSCVENVAL------PLRLnGVKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEP 170
Cdd:PRK13641 94 PEAQLFENTVLkdvefgPKNF-GFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759535873 171 TGALDSLNGERVMELLTEAARGTNaAVVLVTHEA-RVAAYSDREVVVRDGR 220
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMdDVAEYADDVLVLEHGK 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-170 |
1.25e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 115.51 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrRS 85
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA---RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 DFGF------VFQfgqlvpELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALV 159
Cdd:COG1137 79 GIGYlpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170
....*....|.
gi 759535873 160 TAPRVVFADEP 170
Cdd:COG1137 153 TNPKFILLDEP 163
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-216 |
1.38e-31 |
|
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: 120.47 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPEsrrsALRRSD 86
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA----DSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPElSCVENVAlpLRLNGVKRKEAEKAAyawmERLEVEDLAAKRPG-----------EVSGGQGQRVAVA 155
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIR--LARPDASDAEIREAL----ERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 156 RALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGtnAAVVLVTHEARVAAYSDREVVV 216
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-205 |
2.40e-31 |
|
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: 114.68 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDE---GAIHYNGTELSAlpesrrsALRRSDFGFVFQFGQLVPE 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP-------DQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 LSCVENV--ALPLRL-----NGVKRKEAEKAAyawMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTG 172
Cdd:cd03234 96 LTVRETLtyTAILRLprkssDAIRKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190
....*....|....*....|....*....|...
gi 759535873 173 ALDSLNGERVMELLTEAARGtNAAVVLVTHEAR 205
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARR-NRIVILTIHQPR 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-214 |
3.76e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.10 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 16 SYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAL-PEsrRSALRRSdfgfvfqfg 94
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYvPQ--RSEVPDS--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 95 qlVPeLSCVENVAL----PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEP 170
Cdd:NF040873 70 --LP-LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 171 TGALDSLNGERVMELLTEAARgTNAAVVLVTHEARVAAYSDREV 214
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCV 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-220 |
5.37e-31 |
|
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: 111.92 E-value: 5.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNA--LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesRRSALRRS 85
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dFGFVFQFGQLVPElSCVENValplrlngvkrkeaekaayawmerlevedlaakrpgeVSGGQGQRVAVARALVTAPRVV 165
Cdd:cd03246 78 -VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 166 FADEPTGALDSLNGERVMELLtEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-220 |
7.74e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 7.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 19 ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpeSRRSALR--RSDFGFVFQFgql 96
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT----DKKVKLSdiRKKVGLVFQY--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 97 vPELSCVE-----NVALPLRLNGVKRKEAEKAAYAWME--RLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:PRK13637 92 -PEYQLFEetiekDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759535873 170 PTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGK 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-225 |
7.98e-31 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 115.59 E-value: 7.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 4 SGSLLSAEGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD---EGAIHYNGTELSALPE 76
Cdd:PRK09473 9 ADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 77 SRRSALRRSDFGFVFQ--FGQLVPELSCVENVALPLRLN-GVKRKEAEKAAYAWMERLEVEDlAAKR----PGEVSGGQG 149
Cdd:PRK09473 89 KELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESVRMLDAVKMPE-ARKRmkmyPHEFSGGMR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 150 QRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGRSrdME 225
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGRT--ME 242
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
1.30e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 113.25 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 1 MIpsgsllSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPE---S 77
Cdd:COG4604 1 MI------EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSrelA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 78 RR-SALRRSDfgfvfqfgQLVPELSCVENVAL---PL---RLNGVKRKEAEKAayawMERLEVEDLAAKRPGEVSGGQGQ 150
Cdd:COG4604 75 KRlAILRQEN--------HINSRLTVRELVAFgrfPYskgRLTAEDREIIDEA----IAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 151 RVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAScYADHIVAMKDGR 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-220 |
1.83e-30 |
|
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: 111.54 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPEsrrsALRRsdF 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE----ALRR--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAayawMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759535873 168 DEPTGALDSLnGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:cd03268 151 DEPTNGLDPD-GIKELRELILSLRDQGITVLISSHLlSEIQKVADRIGIINKGK 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-220 |
2.43e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.80 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpeSRRSALRRsdF 87
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML--SSRQLARR--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFgQLVPE-LSCVENVA------LPL--RLNGVKRKEAEKAayawMERLEVEDLAAKRPGEVSGGQGQRVAVARAL 158
Cdd:PRK11231 79 ALLPQH-HLTPEgITVRELVAygrspwLSLwgRLSAEDNARVNQA----MEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 159 VTAPRVVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRElNTQGK--TVVTVLHDLNQASrYCDHLVVLANGH 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-220 |
2.50e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpeSRRSALR-R 84
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY---DKKSLLEvR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 85 SDFGFVFQ------FGQLVPelscvENVAL-PLRLnGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARA 157
Cdd:PRK13639 78 KTVGIVFQnpddqlFAPTVE-----EDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 158 LVTAPRVVFADEPTGALDSLNGERVMELLTEAARgTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDlVPVYADKVYVMSDGK 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-220 |
3.60e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 111.66 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEGL-RKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTelsaLPESRRSA 81
Cdd:cd03267 16 EPGLIGSLKSLfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSdFGFVF-QFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVT 160
Cdd:cd03267 92 FLRR-IGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 161 APRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGR 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-211 |
3.62e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.34 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 1 MIPSGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRrs 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 81 alRRSDFGFVFQ----FGQLVpelscVENVALPLRLNgvKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVA 155
Cdd:PRK10247 79 --YRQQVSYCAQtptlFGDTV-----YDNLIFPWQIR--NQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 156 RALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSD 211
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHAD 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-220 |
1.63e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.82 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 4 SGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIhyngtELSALPESRRSALR 83
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-----SLCGEPVPSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 RSDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 164 VVFADEPTGALDS----LNGERVMELLteaARGTnaAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK13537 159 VLVLDEPTTGLDPqarhLMWERLRSLL---ARGK--TILLTTHFMEEAErLCDRLCVIEEGR 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-220 |
2.30e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.88 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 16 SY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALRRSdFGFVFQFG 94
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQ-IGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 95 QLVpELSCVENVALPlrLNGVKRKEAEKAAyawmERLEVEDLAAKRP-------GE----VSGGQGQRVAVARALVTAPR 163
Cdd:COG1132 424 FLF-SGTIRENIRYG--RPDATDEEVEEAA----KAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTnaAVVLVTHeaRVA--AYSDREVVVRDGR 220
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKGR--TTIVIAH--RLStiRNADRILVLDDGR 551
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-220 |
2.78e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 112.43 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 15 KSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAlrrsdfGFVFQFG 94
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV------GMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 95 QLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGAL 174
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759535873 175 DSlnGERV-MEL-LTEAARGTNAAVVLVTH---EARVAAysDREVVVRDGR 220
Cdd:PRK11000 165 DA--ALRVqMRIeISRLHKRLGRTMIYVTHdqvEAMTLA--DKIVVLDAGR 211
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
7-216 |
3.27e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.21 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY----------GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPE 76
Cdd:PRK11308 5 LLQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 77 SRRSALRRsDFGFVFQ--FGQLVPELSCVENVALPLRLN-GVKRKEAEKAAYAWMERLEVEDLAAKR-PGEVSGGQGQRV 152
Cdd:PRK11308 85 EAQKLLRQ-KIQIVFQnpYGSLNPRKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPEHYDRyPHMFSGGQRQRI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 153 AVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVV 216
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-221 |
3.53e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 111.46 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 12 GLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTelsalPESRRSALRRSDFGFVF 91
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV-----PVPARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 92 QFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPT 171
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 172 GALDS----LNGERVMELLteaARGTnaAVVLVTHEARVAA-YSDREVVVRDGRS 221
Cdd:PRK13536 201 TGLDPharhLIWERLRSLL---ARGK--TILLTTHFMEEAErLCDRLCVLEAGRK 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-220 |
5.01e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.94 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpeSRRSALR-RSDFGFVFQF--GQL 96
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY---SRKGLMKlRESVGMVFQDpdNQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 97 VpELSCVENVAL-PLRLnGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:PRK13636 96 F-SASVYQDVSFgAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 759535873 176 SLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDiVPLYCDNVFVMKEGR 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-209 |
5.16e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.16 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD-----EGAIHYNGTELSAlPESRRSAL 82
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYS-PDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 RRsDFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAE---------KAAYAWMErleVEDLAAKRPGEVSGGQGQRVA 153
Cdd:PRK14267 84 RR-EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldervewalKKAALWDE---VKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 154 VARALVTAPRVVFADEPTGALDSLNGERVMELLTEAArgTNAAVVLVTHE----ARVAAY 209
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSpaqaARVSDY 217
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-205 |
6.69e-29 |
|
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: 107.25 E-value: 6.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAG--IVPPDEGAIHYNGTelsalPESRRSALRRSdfGFVFQFGQLVPEL 100
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGR-----PLDKRSFRKII--GYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 101 SCVENVALPLRLNGvkrkeaekaayawmerlevedlaakrpgeVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGE 180
Cdd:cd03213 98 TVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180
....*....|....*....|....*
gi 759535873 181 RVMELLTEAARgTNAAVVLVTHEAR 205
Cdd:cd03213 149 QVMSLLRRLAD-TGRTIICSIHQPS 172
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-220 |
7.87e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.02 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGA-----TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAL 82
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 rrsdFGFVFQFGQL--VPELSCVENVAL--------PLRLnGVKRKeaEKAAYAwmERLEV-----EDLAAKRPGEVSGG 147
Cdd:COG1101 82 ----IGRVFQDPMMgtAPSMTIEENLALayrrgkrrGLRR-GLTKK--RRELFR--ELLATlglglENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 148 QGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAlDYGNRLIMMHEGR 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-220 |
1.77e-28 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 111.93 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 4 SGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpESRRSALr 83
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF--ASTTAAL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 RSDFGFVFQFGQLVPELSCVENV---ALPLRLNGVKRKEAEKAAYAWMERLEvEDLAAKRP-GEVSGGQGQRVAVARALV 159
Cdd:PRK11288 78 AAGVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLG-VDIDPDTPlKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 160 TAPRVVFADEPTGALDSLNGERVMELLTEaARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRE-LRAEGRVILYVSHRmEEIFALCDAITVFKDGR 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-220 |
2.79e-28 |
|
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: 111.88 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALRRsDFGFVFQ-----FG 94
Cdd:TIGR03375 478 TPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQID---PADLRR-NIGYVPQdprlfYG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 95 QLVpelscvENVALPLRLngVKRKEAEKAAyawmERLEVEDLAAKRP-------GE----VSGGQGQRVAVARALVTAPR 163
Cdd:TIGR03375 554 TLR------DNIALGAPY--ADDEEILRAA----ELAGVTEFVRRHPdgldmqiGErgrsLSGGQRQAVALARALLRDPP 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTnaAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:TIGR03375 622 ILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLDLVDRIIVMDNGR 676
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
14-220 |
3.13e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 108.25 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 14 RKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYN----------------GTELSALPES 77
Cdd:PRK13651 14 KKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekekvLEKLVIQKTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 78 RR-----SALRRSdFGFVFQFG--QLVpELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQG 149
Cdd:PRK13651 94 FKkikkiKEIRRR-VGVVFQFAeyQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 150 QRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARgTNAAVVLVTHEA-RVAAYSDREVVVRDGR 220
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-202 |
6.68e-28 |
|
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: 105.94 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAihyngtELSALPESRRSA---- 81
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN------DVRLFGERRGGEdvwe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSdFGFV-FQFGQLVPELSCVENVAL------PLRLNGVKRKEAEKAAyAWMERLEVEDLAAKRPGEVSGGQGQRVAV 154
Cdd:COG1119 76 LRKR-IGLVsPALQLRFPRDETVLDVVLsgffdsIGLYREPTDEQRERAR-ELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 759535873 155 ARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTH 202
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-227 |
2.05e-27 |
|
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: 108.76 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD--EGAIHYNGTELSAlpeSRRSALRR 84
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKA---SNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 85 SDFGFVFQFGQLVPELSCVENVAL--PLRLNGVKRKEAE--KAAYAWMERLEVEDLAAKRP-GEVSGGQGQRVAVARALV 159
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 160 TAPRVVFADEPTGALDSLNGERVMELLTEAARgTNAAVVLVTHE-ARVAAYSDREVVVRDGR---SRDMERL 227
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKlNEVKAVCDTICVIRDGQhvaTKDMSTM 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-210 |
3.08e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.86 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHC---LAGIVPP--DEGAIHYNGTELSAlPESRRSA 81
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYA-PDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSdFGFVFQFGQLVPElSCVENVALPLRLNGVKRKEAE------KAAYAWMErleVEDLAAKRPGEVSGGQGQRVAVA 155
Cdd:PRK14243 89 VRRR-IGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDElverslRQAALWDE---VKDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 156 RALVTAPRVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTHE----ARVAAYS 210
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNmqqaARVSDMT 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-215 |
3.40e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 105.94 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAlRRSDFGFVFQ--FGQLVPE 99
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA-VRSDIQMIFQdpLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 LSCVENVALPLRLN--GVKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PRK15079 115 MTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 759535873 177 LNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVV 215
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDlAVVKHISDRVLV 234
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-220 |
3.82e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 108.39 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPdEGAIHYNGTELSAL-PESRRSALrrsdfGFVFQFGQLvPELSCVENV 106
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELdPESWRKHL-----SWVGQNPQL-PHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 107 AL--PlRLNGVKRKEAEKAAYAW--MERL------EVEDLAAKrpgeVSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PRK11174 444 LLgnP-DASDEQLQQALENAWVSefLPLLpqgldtPIGDQAAG----LSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 177 LNGERVMELLTEAARGTnaAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK11174 519 HSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-220 |
4.57e-27 |
|
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: 102.13 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRksygATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalRRSD 86
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFV----FQFGqLVPELSCVENVALPLRLngvkrkeaekaayawmerlevedlaakrpgevSGGQGQRVAVARALVTAP 162
Cdd:cd03215 77 IAYVpedrKREG-LVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLTEAARGtNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSElDELLGLCDRILVMYEGR 181
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-220 |
7.25e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.06 E-value: 7.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSDFGFVFQF--GQLVPE 99
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFpeSQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 lSCVENVALPLRLNGVKRKEAEKAAyawMERLEV----EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALA---REKLALvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 759535873 176 SLNGERVMELLTEAARGtNAAVVLVTH-EARVAAYSDREVVVRDGR 220
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHlMDDVANYADFVYVLEKGK 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-220 |
7.50e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 107.53 E-value: 7.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLlSAEGLrkSYGATNA----LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESr 78
Cdd:COG4618 327 PKGRL-SVENL--TVVPPGSkrpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 79 rsalrrsdfgfvfQFGQLV------PEL---SCVENVAlplRLNGVKRKEAEKAAyawmERLEVEDLAAK-------RPG 142
Cdd:COG4618 403 -------------ELGRHIgylpqdVELfdgTIAENIA---RFGDADPEKVVAAA----KLAGVHEMILRlpdgydtRIG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 143 E----VSGGQGQRVAVARALVTAPRVVFADEPTGALDSlNGER-VMELLTEA-ARGtnAAVVLVTHEARVAAYSDREVVV 216
Cdd:COG4618 463 EggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAaLAAAIRALkARG--ATVVVITHRPSLLAAVDKLLVL 539
|
....
gi 759535873 217 RDGR 220
Cdd:COG4618 540 RDGR 543
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-220 |
1.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.66 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRrsalRRSDFGFVFQ------F 93
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW----VRSKVGLVFQdpddqvF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 94 GQLVpelscVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGA 173
Cdd:PRK13647 94 SSTV-----WDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759535873 174 LDSLNGERVMELLTE-AARGTnaAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK13647 169 LDPRGQETLMEILDRlHNQGK--TVIVATHDVDLAAeWADQVIVLKEGR 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-220 |
1.25e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRksygATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALRRsd 86
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDAIRA-- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 fGFVF------QFGqLVPELSCVENVALPL-----RLNGVKRKEAEKAAYAWMERLEV-----EDLAakrpGEVSGGQGQ 150
Cdd:COG1129 328 -GIAYvpedrkGEG-LVLDLSIRENITLASldrlsRGGLLDRRRERALAEEYIKRLRIktpspEQPV----GNLSGGNQQ 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 151 RVAVARALVTAPRVVFADEPT-----GAldslngeR--VMELLTE-AARGTnaAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTrgidvGA-------KaeIYRLIRElAAEGK--AVIVISSELPeLLGLSDRILVMREGR 471
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-209 |
1.78e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 35 VVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRR-SALR-RSDFGFVFQFGQLVPELSCVENVALPLRL 112
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQiDAIKlRKEVGMVFQQPNPFPHLSIYDNIAYPLKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 113 NGVK-RKEAEKAAYAWMERL----EVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLT 187
Cdd:PRK14246 118 HGIKeKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
|
170 180
....*....|....*....|....*.
gi 759535873 188 EAARgtNAAVVLVTHE----ARVAAY 209
Cdd:PRK14246 198 ELKN--EIAIVIVSHNpqqvARVADY 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-221 |
1.88e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.43 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHY-NGTELSALPEsrRSALrrsdfgfvfqfgqlvPELS 101
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQ--RPYL---------------PLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 102 CVENVALPLRLNGVKRKEAEKAayawMERLEVEDLAAkRPGEV-------SGGQGQRVAVARALVTAPRVVFADEPTGAL 174
Cdd:COG4178 442 LREALLYPATAEAFSDAELREA----LEAVGLGHLAE-RLDEEadwdqvlSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 759535873 175 DSLNGERVMELLTEAARGTnaAVVLVTHEARVAAYSDREVVVRDGRS 221
Cdd:COG4178 517 DEENEAALYQLLREELPGT--TVISVGHRSTLAAFHDRVLELTGDGS 561
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-219 |
2.63e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.73 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSDF 87
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDG 219
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMrIGDRIAIMQNG 241
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
7-202 |
2.93e-26 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 100.65 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALrrsd 86
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 fgfvFQFGQLV---PELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRpgeVSGGQGQRVAVARALVTAPR 163
Cdd:PRK13538 77 ----LYLGHQPgikTELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQ---LSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTE-AARGtnAAVVLVTH 202
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQhAEQG--GMVILTTH 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-219 |
3.42e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 19 ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSDFGFVFQF--GQL 96
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpeSQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 97 VPElSCVENVALPLRLNGVKRKEAEKAAyawMERLEVEDLAA----KRPGEVSGGQGQRVAVARALVTAPRVVFADEPTG 172
Cdd:PRK13643 98 FEE-TVLKDVAFGPQNFGIPKEKAEKIA---AEKLEMVGLADefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 759535873 173 ALDSLNGERVMELLtEAARGTNAAVVLVTH-EARVAAYSDREVVVRDG 219
Cdd:PRK13643 174 GLDPKARIEMMQLF-ESIHQSGQTVVLVTHlMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-220 |
3.48e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.99 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpESRRSAlrRSDFGFVFQF--GQLV 97
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK--ENLKEI--RKKIGIIFQNpdNQFI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PelSCVE-NVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PRK13632 98 G--ATVEdDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 177 LNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGK 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-205 |
4.13e-26 |
|
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: 100.13 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRrsdf 87
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 gFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEkAAYAWMERLEVEDLAAkrpGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:TIGR01189 77 -YLGHLPGLKPELSALENLHFWAAIHGGAQRTIE-DALAAVGLTGFEDLPA---AQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 759535873 168 DEPTGALDSLNGERVMELLTE-AARGtnAAVVLVTHEAR 205
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAhLARG--GIVLLTTHQDL 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-220 |
4.53e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEGLR-KSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSA 81
Cdd:COG3845 253 PGEVVLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFV----FQFGqLVPELSCVENVAL------PLRLNG-VKRKEAEKAAYAWMERLEV----EDLAAKRpgeVSG 146
Cdd:COG3845 330 RRRLGVAYIpedrLGRG-LVPDMSVAENLILgryrrpPFSRGGfLDRKAIRAFAEELIEEFDVrtpgPDTPARS---LSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 147 GQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGtNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDeILALSDRIAVMYEGR 479
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-220 |
1.76e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.22 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRS 85
Cdd:PRK11831 6 NLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dFGFVFQFGQLVPELSCVENVALPLRLNgvKRKEAEKAAYAWMERLEVEDL--AAK-RPGEVSGGQGQRVAVARALVTAP 162
Cdd:PRK11831 86 -MSMLFQSGALFTDMNVFDNVAYPLREH--TQLPAPLLHSTVMMKLEAVGLrgAAKlMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEA-RVAAYSDREVVVRDGR 220
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVpEVLSIADHAYIVADKK 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-220 |
2.86e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 103.40 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 21 NALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRsDFGFVFQ--FGQLVP 98
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQdpYASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ELSCVENVALPLRLNGVKRKEAEKAAYAWM-ERLEVEDLAAKR-PGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPGKAAAARVAWLlERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 759535873 177 LNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDmAVVERISHRVAVMYLGQ 541
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-220 |
4.40e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.69 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalrrsD 86
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR------D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVALPLRLNGVKRKE----AEKAAYAwmerLEVEDLAAKRPGEVSGGQGQRVAVARALVTAP 162
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEieerVAEAARI----LELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 163 RVVFADEPTGALDS-LngeRV-MEL-LTEAARGTNAAVVLVTH---EARVAAysDREVVVRDGR 220
Cdd:PRK11650 154 AVFLFDEPLSNLDAkL---RVqMRLeIQRLHRRLKTTSLYVTHdqvEAMTLA--DRVVVMNGGV 212
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
7-175 |
6.38e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 98.76 E-value: 6.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY---------GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPES 77
Cdd:COG4167 4 LLEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 78 RRSALRRsdfgFVFQ-----------FGQLVPElscvenvalPLRLN----GVKRKE------------AEKAAYawmer 130
Cdd:COG4167 84 YRCKHIR----MIFQdpntslnprlnIGQILEE---------PLRLNtdltAEEREErifatlrlvgllPEHANF----- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 759535873 131 levedlaakRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:COG4167 146 ---------YPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-219 |
8.17e-25 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 101.62 E-value: 8.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELS-ALPESRRSAlrrs 85
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 DFGFVFQFGQLVPELSCVENVAL----PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 162 PRVVFADEPTGALDSLNGE---RVMELLTEAARGtnaaVVLVTHEAR-VAAYSDREVVVRDG 219
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETEslfRVIRELKSQGRG----IVYISHRLKeIFEICDDVTVFRDG 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-220 |
8.20e-25 |
|
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: 97.68 E-value: 8.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 16 SYGATN-ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALRRSdFGFVFQFG 94
Cdd:cd03254 11 SYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSM-IGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 95 QLVPElSCVENVALPLRLNGVKR-KEAEKAAYA--WMERLE--VEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:cd03254 87 FLFSG-TIMENIRLGRPNATDEEvIEAAKEAGAhdFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759535873 170 PTGALDSLNGERVMELLTEAARGTNAAVvlVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGRTSII--IAHRLSTIKNADKILVLDDGK 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-220 |
8.82e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.39 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 13 LRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTElsalPESRRSALRRsDFGFVF- 91
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PFKRRKEFAR-RIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 92 QFGQLVPELSCVENvalpLRLN----GVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:COG4586 103 QRSQLWWDLPAIDS----FRLLkaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmDDIEALCDRVIVIDHGR 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-220 |
1.17e-24 |
|
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: 97.30 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpESRRSALRRSdFGFVFQFGQLVPElSC 102
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR---EVTLDSLRRA-IGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENVALPlRLNGVKRK--EAEKAAYAWMERLEVEDLAAKRPGE----VSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:cd03253 92 GYNIRYG-RPDATDEEviEAAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 177 LNGERVMELLTEAARGTnaAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03253 171 HTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDGR 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-219 |
1.68e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSDFGFVFQFgqlvPELS 101
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQF----PESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 102 CVENVALPLRLNGVKR-----KEAEKAAYAWMERLEVE-DLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:PRK13646 98 LFEDTVEREIIFGPKNfkmnlDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 759535873 176 SLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDG 219
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEG 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-219 |
2.54e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.47 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 21 NALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpeSRRSALRRSdFGFVFQF--GQLVP 98
Cdd:PRK13642 21 NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRK-IGMVFQNpdNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ElSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLN 178
Cdd:PRK13642 97 A-TVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 179 GERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDG 219
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAG 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-202 |
4.00e-24 |
|
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: 99.74 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALrrsd 86
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVpELSCVENVALplrlngvKRKEA-EKAAYAWMERLEVEDLAAKRPG-----------EVSGGQGQRVAV 154
Cdd:TIGR02868 411 VSVCAQDAHLF-DTTVRENLRL-------ARPDAtDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 759535873 155 ARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTnaAVVLVTH 202
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITH 528
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-220 |
7.24e-24 |
|
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: 93.53 E-value: 7.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATN--ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAlrrs 85
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dFGFVFQFGQLVpELSCVENVALPLrlngvkrkeaekaayawmerlevedlaakrpgevSGGQGQRVAVARALVTAPRVV 165
Cdd:cd03247 77 -ISVLNQRPYLF-DTTLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 166 FADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGK 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-224 |
1.21e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 98.19 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 18 GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpESRRSALRRSdFGFVFQFGQLV 97
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK---QWDRETFGKH-IGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PElSCVENVAlPLRLNGVKRK--EAEKAAyawmerlEVEDLAAKRP-----------GEVSGGQGQRVAVARALVTAPRV 164
Cdd:TIGR01842 405 PG-TVAENIA-RFGENADPEKiiEAAKLA-------GVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 165 VFADEPTGALDSLNGERVMELLTEA-ARGtnAAVVLVTHEARVAAYSDREVVVRDGRSRDM 224
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALkARG--ITVVVITHRPSLLGCVDKILVLQDGRIARF 534
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-223 |
1.86e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 5 GSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTE---LSALPESRRSA 81
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDveaLSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 LRRSDFGFVFQF-GQLVPELSCVENVALPLRLNGVKRKEAEKAayawMERLEVEDLAAKRPGEVSGGQGQRVAVARALVT 160
Cdd:PRK09536 81 SVPQDTSLSFEFdVRQVVEMGRTPHRSRFDTWTETDRAAVERA----MERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 161 APRVVFADEPTGALDSLNGERVMELLTEAARgTNAAVVLVTHEARVAA-YSDREVVVRDGRSRD 223
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAArYCDELVLLADGRVRA 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-219 |
2.20e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.57 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGI--VPPDEGAIHYN------------------ 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 68 -----GTELSA-------LPESRRSALRRSdFGFVFQ--FGqLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEV 133
Cdd:TIGR03269 81 pcpvcGGTLEPeevdfwnLSDKLRRRIRKR-IAIMLQrtFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 134 EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDR 212
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEdLSDK 238
|
....*..
gi 759535873 213 EVVVRDG 219
Cdd:TIGR03269 239 AIWLENG 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-227 |
2.66e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.31 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD--EGAIHYNGTELSA--LPESRRSAL 82
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQAsnIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 rrsdfGFVFQFGQLVPELSCVENVAL---PLRlNGVKRKEAEKA-AYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARAL 158
Cdd:PRK13549 85 -----AIIHQELALVKELSVLENIFLgneITP-GGIMDYDAMYLrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 159 VTAPRVVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHEA-RVAAYSDREVVVRDGR---SRDMERL 227
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDlKAHGI--ACIYISHKLnEVKAISDTICVIRDGRhigTRPAAGM 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-220 |
2.72e-23 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 93.76 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrrSALRRSDFGFVFQFGQLVpELSC 102
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN----LRWLRSQIGLVSQEPVLF-DGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENVALPLrlNGVKRKEAEKAAYA---------WMERLEVEdlAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGA 173
Cdd:cd03249 94 AENIRYGK--PDATDEEVEEAAKKanihdfimsLPDGYDTL--VGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759535873 174 LDSLNGERVMELLTEAARGTnaAVVLVTHeaRVAA--YSDREVVVRDGR 220
Cdd:cd03249 170 LDAESEKLVQEALDRAMKGR--TTIVIAH--RLSTirNADLIAVLQNGQ 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-219 |
3.28e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.05 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGtelSALPESRRSALRRsDFGFVFQF--GQLVPe 99
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN---QAITDDNFEKLRK-HIGIVFQNpdNQFVG- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 lSCVE-NVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLN 178
Cdd:PRK13648 99 -SIVKyDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 179 GERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDG 219
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-220 |
5.42e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.41 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY-----GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYN-GTELSALPESRRS 80
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 81 ALRRSD--FGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAY----AWMERLEVEDLAAKRPGEVSGGQGQRVAV 154
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVItlkmVGFDEEKAEEILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 155 ARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDfVLDVCDRAALMRDGK 505
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-218 |
1.12e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAI---------HYNGTELSALPESRR----SALRRSdFG 88
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELITNPYSKKiknfKELRRR-VS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 89 FVFQFgqlvPELSCVEN----------VALplrlnGVKRKEAEKAAYAWMERLEVEDLAAKR-PGEVSGGQGQRVAVARA 157
Cdd:PRK13631 120 MVFQF----PEYQLFKDtiekdimfgpVAL-----GVKKSEAKKLAKFYLNKMGLDDSYLERsPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 158 LVTAPRVVFADEPTGALDSlNGERVMELLTEAARGTNAAVVLVTHEA-RVAAYSDrEVVVRD 218
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDP-KGEHEMMQLILDAKANNKTVFVITHTMeHVLEVAD-EVIVMD 250
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-220 |
1.31e-22 |
|
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: 91.91 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 19 ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesRRSALRRSdFGFVFQFGQLVP 98
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ-IGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ElSCVENVALPLRlnGVKRKEAEKAAYA-----WMERLE--VEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPT 171
Cdd:cd03251 90 D-TVAENIAYGRP--GATREEVEEAARAanaheFIMELPegYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759535873 172 GALDSLNGERVMELLTEAARGTNAAVvlVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03251 167 SALDTESERLVQAALERLMKNRTTFV--IAHRLSTIENADRIVVLEDGK 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-202 |
1.50e-22 |
|
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: 91.02 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRrsdf 87
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 gFVFQFGQLVPELSCVENVALPLRLNGvkrKEAEKAAYAWMERLEVEDLAAkrpGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03231 77 -YLGHAPGIKTTLSVLENLRFWHADHS---DEQVEEALARVGLNGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 759535873 168 DEPTGALDSLNGERVMELLT-EAARGtnAAVVLVTH 202
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAgHCARG--GMVVLTTH 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-202 |
2.89e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNG--TELSALPES-----RRS 80
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEAchylgHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 81 ALRrsdfgfvfqfgqlvPELSCVENVALPLRLNGvkrkEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVT 160
Cdd:PRK13539 83 AMK--------------PALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 759535873 161 APRVVFADEPTGALDSLNGERVMELLtEAARGTNAAVVLVTH 202
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELI-RAHLAQGGIVIAATH 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-221 |
3.06e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALrrsD 86
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENV---ALPLR----LNGVKRKEAEKAAYAWMERLEVE-DLAAKrPGEVSGGQGQRVAVARAL 158
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKvDLDEK-VANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 159 VTAPRVVFADEPTGALDSLNGERVMeLLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGRS 221
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLF-LIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSS 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-220 |
3.94e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.72 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSalrRS 85
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA---RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 DFGFVFQFGQLVPELSCVENVALPLRL-NGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRV 164
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 165 VFADEPTGALDSLNGERVMELLtEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRII-EHLRDSGLGVLITDHNVReTLAVCERAYIVSQGH 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-220 |
5.82e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.01 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGA---IHYNGTELSAlpesRRSALRRSDFGFVFQF--GQL 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA----KTVWDIREKVGIVFQNpdNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 97 VPElSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PRK13640 98 VGA-TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 177 LNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGK 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-219 |
6.05e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALrrsD 86
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---G 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVALPLrlngVKRKEAEKAAYAWMERLEVE-DLAAKrPGEVSGGQGQRVAVARALVTAPRVV 165
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQlDLDSS-AGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 166 FADEPTGALDSLNGERVMELLtEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDG 219
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKLPeIRQLADRISVMRDG 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-220 |
6.94e-22 |
|
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: 89.85 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATN--ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrrSALRRSDFG 88
Cdd:cd03252 4 EHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD----PAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 89 FVFQFGQLVPElSCVENVALPlrLNGVKRKEAEKA-----AYAWMERLE--VEDLAAKRPGEVSGGQGQRVAVARALVTA 161
Cdd:cd03252 80 VVLQENVLFNR-SIRDNIALA--DPGMSMERVIEAaklagAHDFISELPegYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEAARGTnaAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGR 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-225 |
7.97e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.53 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNG---TELSALPESRRSAlrrsdfGFVFQF--GQL 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtSDEENLWDIRNKA------GMVFQNpdNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 97 VPELsCVENVAL-PLRLnGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:PRK13633 99 VATI-VEEDVAFgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 759535873 176 SLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDReVVVRDGRSRDME 225
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGITIILITHYMEEAVEADR-IIVMDSGKVVME 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-223 |
2.74e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYnGTELSalpesrrsalrrsd 86
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQ-FGQLVPELSCVENVAlplrlnGVKRKEAEKAAYAWMERL-----EVEdlaaKRPGEVSGGQGQRVAVARALVT 160
Cdd:COG0488 380 IGYFDQhQEELDPDKTVLDELR------DGAPGGTEQEVRGYLGRFlfsgdDAF----KPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 161 APRVVFADEPTGALD--SLngervmELLTEAARGTNAAVVLVTHE----ARVAaysDREVVVRDGRSRD 223
Cdd:COG0488 450 PPNVLLLDEPTNHLDieTL------EALEEALDDFPGTVLLVSHDryflDRVA---TRILEFEDGGVRE 509
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-202 |
2.87e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 10 AEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIhyngtelsalpeSRRSALRrsdFGF 89
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------------SIPKGLR---IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 VFQFGQLVPELSCVENV--------ALPLRLNGVKRKEAEK---------------AAYAW---------MERLEVEDLA 137
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVldgdaelrALEAELEELEAKLAEPdedlerlaelqeefeALGGWeaearaeeiLSGLGFPEED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 138 AKRP-GEVSGGQGQRVAVARALVTAPRVVFADEPTGALDsLNGervMELLTEAARGTNAAVVLVTH 202
Cdd:COG0488 146 LDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES---IEWLEEFLKNYPGTVLVVSH 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-222 |
3.12e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 1 MIPSgslLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD-----EGAIHYNGTELSalp 75
Cdd:PRK14258 4 LIPA---IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 76 ESRRSALR-RSDFGFVFQFGQLVPeLSCVENVALPLRLNGVKRK--------EAEKAAYAWMErleVEDLAAKRPGEVSG 146
Cdd:PRK14258 78 ERRVNLNRlRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddiveSALKDADLWDE---IKHKIHKSALDLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 147 GQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVVVRDGRSR 222
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSDFTAFFKGNENR 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-202 |
3.44e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.93 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 35 VVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAL-------PESRRsalrrsdFGFVFQFGQLVPELSCVENva 107
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAekgiclpPEKRR-------IGYVFQDARLFPHYKVRGN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 108 lpLRLnGVKRKEAEKAAYAwMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLT 187
Cdd:PRK11144 97 --LRY-GMAKSMVAQFDKI-VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170
....*....|....*
gi 759535873 188 EAARGTNAAVVLVTH 202
Cdd:PRK11144 173 RLAREINIPILYVSH 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-220 |
4.49e-21 |
|
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: 87.59 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTeLSALPEsrrsalrrsdFGFVFQfgqlvPELS 101
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLG----------LGGGFN-----PELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 102 CVENVALPLRLNGVKRKEAeKAAYAWMERL-EVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGE 180
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEI-DEKIDEIIEFsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 181 RVMELLTEAARGTnAAVVLVTH-EARVAAYSDREVVVRDGR 220
Cdd:cd03220 180 KCQRRLRELLKQG-KTVILVSHdPSSIKRLCDRALVLEKGK 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-220 |
5.00e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 87.53 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 19 ATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesrRSALRRSDFGFVFQFGQLVP 98
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY----EHKYLHSKVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ElSCVENVALPLRLNGVKR-KEAEKAAYAWMERLEVED----LAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGA 173
Cdd:cd03248 102 R-SLQDNIAYGLQSCSFECvKEAAQKAHAHSFISELASgydtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 759535873 174 LDSLNGERVMELLTEAARgtNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03248 181 LDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-219 |
1.17e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 13 LRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKST----LLHCLAGivppdEGAIHYNGTELSALpeSRRSALR-RSDF 87
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNL--NRRQLLPvRHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQ--FGQLVPELSCVENVALPLR-----LNGVKRKEAEKAAyawMErlEVEDLAAKR---PGEVSGGQGQRVAVARA 157
Cdd:PRK15134 365 QVVFQdpNSSLNPRLNVLQIIEEGLRvhqptLSAAQREQQVIAV---ME--EVGLDPETRhryPAEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 158 LVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVA-AYSDREVVVRDG 219
Cdd:PRK15134 440 LILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVrALCHQVIVLRQG 502
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-226 |
1.20e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 88.26 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATN----ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIV--PPDEGA--IHYNGTELSALPES 77
Cdd:PRK11022 2 ALLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRVMAekLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 78 RRSALRRSDFGFVFQ--FGQLVPELSCVENVALPLRLN-GVKRKEAEKAAYAWMERLEVEDLAAK---RPGEVSGGQGQR 151
Cdd:PRK11022 82 ERRNLVGAEVAMIFQdpMTSLNPCYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 152 VAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDREVV------VRDGRSRDM 224
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVmyagqvVETGKAHDI 241
|
..
gi 759535873 225 ER 226
Cdd:PRK11022 242 FR 243
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
12-220 |
1.91e-20 |
|
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: 85.62 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 12 GLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrRSALRRSdFGFVF 91
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR-ISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 92 Q---------------FGQLVPE--LSCVENVALplrlngvkrKEAekaayawmerleVEDLAAKRPGEVSGG-----QG 149
Cdd:cd03244 85 QdpvlfsgtirsnldpFGEYSDEelWQALERVGL---------KEF------------VESLPGGLDTVVEEGgenlsVG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 150 QR--VAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03244 144 QRqlLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLDTIIDSDRILVLDKGR 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-220 |
1.92e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.99 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 24 DGAEFSIHAGEVVAIMGPSGSGKS----TLLHCLAGivPPDE---GAIHYNGTELSALPESRRSALRRSDFGFVFQ--FG 94
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLPS--PPVVypsGDIRFHGESLLHASEQTLRGVRGNKIAMIFQepMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 95 QLVPELSCVENVALPLRLN-GVKRKEAEKAAYAWMERLEVEDlAAKR----PGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:PRK15134 104 SLNPLHTLEKQLYEVLSLHrGMRREAARGEILNCLDRVGIRQ-AAKRltdyPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759535873 170 PTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSiVRKLADRVAVMQNGR 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-220 |
2.78e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 14 RKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTeLSALPEsrrsalrrsdFGFVFQf 93
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSALLE----------LGAGFH- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 94 gqlvPELSCVENVALPLRLNGVKRKEAEkaayawmERL-EVEDLAakrpgEV-----------SGGQGQRVAVARALVTA 161
Cdd:COG1134 101 ----PELTGRENIYLNGRLLGLSRKEID-------EKFdEIVEFA-----ELgdfidqpvktySSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:COG1134 165 PDILLVDEVLAVGDAAFQKKCLARIRElRESGR--TVIFVSHSMGaVRRLCDRAIWLEKGR 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-220 |
2.81e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpESRRSALRRSdFGFVFQF--GQLVPel 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIRHK-IGMVFQNpdNQFVG-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 101 SCVEN-VALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNG 179
Cdd:PRK13650 97 ATVEDdVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 180 ERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK13650 177 LELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQ 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-214 |
3.19e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 83.74 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 27 EFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYngtelsalPESRRSAlrrsdfgFVFQFGQLVPelscvenv 106
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------PEGEDLL-------FLPQRPYLPL-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 107 alplrlnGVKRkeaEKAAYAWMERLevedlaakrpgevSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELL 186
Cdd:cd03223 78 -------GTLR---EQLIYPWDDVL-------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180
....*....|....*....|....*...
gi 759535873 187 TEAArgtnAAVVLVTHEARVAAYSDREV 214
Cdd:cd03223 135 KELG----ITVISVGHRPSLWKFHDRVL 158
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-220 |
8.14e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 1 MIPSGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpeSRRS 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY--ASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 81 ALRRsdFGFVFQFGQLVPELSCVENVAL------PLRLNGvkRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAV 154
Cdd:PRK10253 79 VARR--IGLLAQNATTPGDITVQELVARgryphqPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 155 ARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK10253 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACrYASHLIALREGK 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-220 |
8.86e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 8.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGI--VPPDEGAIHYNGTELSALPESRRSalrRSDFGFVFQFGQLVPEL 100
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERA---RAGIFLAFQYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 101 ScVEN---VAL-PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEV--SGGQGQRVAVARALVTAPRVVFADEP-TGA 173
Cdd:COG0396 93 S-VSNflrTALnARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgfSGGEKKRNEILQMLLLEPKLAILDETdSGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 759535873 174 -LDSLngeRVMELLTEAARGTNAAVVLVTHEARVAAY--SDREVVVRDGR 220
Cdd:COG0396 172 dIDAL---RIVAEGVNKLRSPDRGILIITHYQRILDYikPDFVHVLVDGR 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-220 |
9.29e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGaIHYNGTEL---SALPESRRSALRR 84
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggRSIFNYRDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 85 SDFGFVFQFGQLVPeLSCVENVALPLRLNG-VKRKEAEKAAYAWMERL----EVEDLAAKRPGEVSGGQGQRVAVARALV 159
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVglwdAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 160 TAPRVVFADEPTGALDSLNGERVMELLTEAArgTNAAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNlAQAARISDRAALFFDGR 239
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-203 |
1.85e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.25 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 33 GEVVAIMGPSGSGKSTLLHCLAGIVPPD---EGAIHYNGTELSALPESRRSAlrrsdfgFVFQFGQLVPELSCVEN---- 105
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISA-------YVQQDDLFIPTLTVREHlmfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 106 --VALPLRLNGVKRKEAEKAAyawMERLEVEDLAAKR---PGEV---SGGQGQRVAVARALVTAPRVVFADEPTGALDSL 177
Cdd:TIGR00955 124 ahLRMPRRVTKKEKRERVDEV---LQALGLRKCANTRigvPGRVkglSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180
....*....|....*....|....*..
gi 759535873 178 NGERVMELLTE-AARGTnaAVVLVTHE 203
Cdd:TIGR00955 201 MAYSVVQVLKGlAQKGK--TIICTIHQ 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-220 |
1.93e-19 |
|
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: 82.52 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTelsalpesrrsalrrsdFGFVFQFGQLVPElS 101
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQEPWIQNG-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 102 CVENVALPLRLNgvkrkeaekaayawMERLE-VEDLAAKRP-------------GE----VSGGQGQRVAVARALVTAPR 163
Cdd:cd03250 82 IRENILFGKPFD--------------EERYEkVIKACALEPdleilpdgdlteiGEkginLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 164 VVFADEPTGALDSLNGERVME-LLTEAARGtNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFEnCILGLLLN-NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-220 |
2.66e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSA-LPESRRSALRRSDFGFVFQFG--QLVP 98
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnLKKIKEVKRLRKEIGLVFQFPeyQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ElSCVENVAL-PLRLnGVKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PRK13645 106 E-TIEKDIAFgPVNL-GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 759535873 177 LNGERVMELLTEAARGTNAAVVLVTHEA-RVAAYSDREVVVRDGR 220
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGK 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-219 |
6.95e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 21 NALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRsdfgFVFQ--FGQLVP 98
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIR----MIFQdpSTSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ELSCVENVALPLRLN-GVKRKEAEKAAYAWMERLEV-EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PRK15112 103 RQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 177 LNGERVMELLTEAARGTNAAVVLVT-HEARVAAYSDREVVVRDG 219
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQG 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-221 |
9.65e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 9.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 2 IPSGSLLSAEGLRKSY----GATNALDGAEFSIHAGEVVAIMGPSGSGKST-------LLHCLAGIVPPDEGAIHYNGTE 70
Cdd:PRK10261 7 LDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 71 LSALPESRRSALRR---SDFGFVFQ--FGQLVPELSCVENVALPLRLN-GVKRKEAEKAAYAWMERL---EVEDLAAKRP 141
Cdd:PRK10261 87 VIELSEQSAAQMRHvrgADMAMIFQepMTSLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVripEAQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 142 GEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAeIADRVLVMYQGE 246
|
.
gi 759535873 221 S 221
Cdd:PRK10261 247 A 247
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-220 |
2.57e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.09 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 18 GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesRRSALRRSdFGFVFQFGQLV 97
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLRRN-IAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PElSCVENvalpLRLNGVKRKEAEKAAYAwmERLEVEDLAAKRP-------GE----VSGGQGQRVAVARALVTAPRVVF 166
Cdd:PRK13657 422 NR-SIEDN----IRVGRPDATDEEMRAAA--ERAQAHDFIERKPdgydtvvGErgrqLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARG-------------TNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKGrttfiiahrlstvRNADRILVFDNGRvVESGSFDELVARGGR 562
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-224 |
4.42e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.46 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpESRRSALRRSdfgfVFQFGQlVPEL-- 100
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV---QYDHHYLHRQ----VALVGQ-EPVLfs 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 101 -SCVENVALplrlnGVKRKEAE------KAAYAWMERLEVEDLAAKRPGE----VSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:TIGR00958 569 gSVRENIAY-----GLTDTPDEeimaaaKAANAHDFIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 170 PTGALDSlngeRVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGRSRDM 224
Cdd:TIGR00958 644 ATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-203 |
5.12e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIhyngtelsalpeSRRSALRrs 85
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dFGFVFQFGQLVPELSCVENVALPLRlNGVKRKEAEKAayawMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVV 165
Cdd:PRK09544 69 -IGYVPQKLYLDTTLPLTVNRFLRLR-PGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 759535873 166 FADEPTGALDsLNGERVM-ELLTEAARGTNAAVVLVTHE 203
Cdd:PRK09544 143 VLDEPTQGVD-VNGQVALyDLIDQLRRELDCAVLMVSHD 180
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-222 |
5.98e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTE---LSALPESRRSAlrrsdfGFVFQ---- 92
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDtgdFSKLQGIRKLV------GIVFQnpet 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 93 --FGQLVPELSCV--ENVALP-LRLngvkRKEAEKAayawMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:PRK13644 89 qfVGRTVEEDLAFgpENLCLPpIEI----RKRVDRA----LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARgTNAAVVLVTHEARVAAYSDREVVVRDGRSR 222
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-219 |
1.18e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.46 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVP--PDEGAIhyngtELSALPESRRSALrr 84
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV-----DVPDNQFGREASL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 85 sdfgfVFQFGQLVPELSCVEnvalplRLNGVKRKEaekaAYAWMerlevedlaaKRPGEVSGGQGQRVAVARALVTAPRV 164
Cdd:COG2401 103 -----IDAIGRKGDFKDAVE------LLNAVGLSD----AVLWL----------RRFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 165 VFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDG 219
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-220 |
1.44e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY--GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPEsrrSALRR 84
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 85 SdFGFVFQ----FGQlvpelSCVENVALPL------RLNGVKRK-------EAEKAAYAWMerlevedlaakrpGE---- 143
Cdd:PRK11160 415 A-ISVVSQrvhlFSA-----TLRDNLLLAApnasdeALIEVLQQvglekllEDDKGLNAWL-------------GEggrq 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 144 VSGGQGQRVAVARALV-TAPrVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK11160 476 LSGGEQRRLGIARALLhDAP-LLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQ 550
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
7-220 |
2.33e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.33 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD--------EGAIHYNGTELSALPESR 78
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 79 RSALR-----RSDFGFVFQFGQLVpELSCVENValplRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVA 153
Cdd:PRK13547 81 LARLRavlpqAAQPAFAFSAREIV-LLGRYPHA----RRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 154 VARAL---------VTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGA 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-212 |
2.84e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 78.79 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 18 GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPP------DEgaIHYNGTELSALPESRRSALRRSDFGFVF 91
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtaDR--FRWNGIDLLKLSPRERRKIIGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 92 Q------------FGQLVPelscvenvALP-LRLNGV---KRKEAEKAAYAWMERLEV---EDLAAKRPGEVSGGQGQRV 152
Cdd:COG4170 96 QepsscldpsakiGDQLIE--------AIPsWTFKGKwwqRFKWRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 153 AVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHE-ARVAAYSDR 212
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADT 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-202 |
4.21e-17 |
|
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: 74.79 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTElsalpesrrsalrrsDF 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV---------------KI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 GFVFQFgqlvpelscvenvalplrlngvkrkeaekaayawmerlevedlaakrpgevSGGQGQRVAVARALVTAPRVVFA 167
Cdd:cd03221 66 GYFEQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....*
gi 759535873 168 DEPTGALDSLNgervMELLTEAARGTNAAVVLVTH 202
Cdd:cd03221 95 DEPTNHLDLES----IEALEEALKEYPGTVILVSH 125
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-207 |
4.40e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.81 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGtelsalpESRRSALRRSD 86
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG-------KTATRGDRSRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKrpgEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:PRK13543 84 MAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 759535873 167 ADEPTGALDsLNGERVMELLTEAARGTNAAVVLVTHEARVA 207
Cdd:PRK13543 161 LDEPYANLD-LEGITLVNRMISAHLRGGGAALVTTHGAYAA 200
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-220 |
5.31e-17 |
|
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: 76.30 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGA--TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRrsaLRRS 85
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dfgfvfqfgqlvpeLSCVENValPLRLNGVKRKEAEKaayaWMERLEVEDLAAKRPGE----VSGGQGQRVAVARALVTA 161
Cdd:cd03369 84 --------------LTIIPQD--PTLFSGTIRSNLDP----FDEYSDEEIYGALRVSEgglnLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 162 PRVVFADEPTGALDSLNGERVMELLTEAArgTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLRTIIDYDKILVMDAGE 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-220 |
1.68e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.13 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELsalpESRRSALRRSdFGFVFQFGQLVPELS 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQS-LGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 102 CVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGER 181
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 759535873 182 VMELLTEAARGTnaAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:TIGR01257 1100 IWDLLLKYRSGR--TIIMSTHHMDEAdLLGDRIAIISQGR 1137
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-221 |
1.83e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.52 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD--EGAIHYNGTELsalpesRRSALRR 84
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVC------RFKDIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 85 S-DFGFVF--QFGQLVPELSCVENVAL--PLRLNGV-KRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARAL 158
Cdd:NF040905 75 SeALGIVIihQELALIPYLSIAENIFLgnERAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 159 VTAPRVVFADEPTGALDSLNGERVMELLTE-AARGTNAavVLVTHE----ARVAaysDREVVVRDGRS 221
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLElKAQGITS--IIISHKlneiRRVA---DSITVLRDGRT 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-220 |
2.13e-16 |
|
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: 74.49 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGI--VPPDEGAIHYNGTELSALPESRRSalrRSDFGFVFQFgqlvpel 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQY------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 101 scvenvalPLRLNGVKrkeaekaayawmerleVEDLAakRPGEV--SGGQGQRVAVARALVTAPRVVFADEPTGALD--- 175
Cdd:cd03217 86 --------PPEIPGVK----------------NADFL--RYVNEgfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDida 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 759535873 176 -SLNGERVMELLTEaargtNAAVVLVTHEARVAAY--SDREVVVRDGR 220
Cdd:cd03217 140 lRLVAEVINKLREE-----GKSVLIITHYQRLLDYikPDRVHVLYDGR 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-220 |
3.25e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRrsaLRRSD 86
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK---IMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQFGQLVPELSCVENVAL-PLRLNGVKRKEAEKAAYAWMERLevEDLAAKRPGEVSGGQGQRVAVARALVTAPRVV 165
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMgGFFAERDQFQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 166 FADEPTGALDSLNGERVMELLtEAARGTNAAVVLVTHEARVA-AYSDREVVVRDGR 220
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTI-EQLREQGMTIFLVEQNANQAlKLADRGYVLENGH 214
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-220 |
4.80e-16 |
|
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: 76.40 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAL-PESRRSALrrsdfGFVFQ----FGQlv 97
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtQASLRAAI-----GIVPQdtvlFND-- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 pelSCVENVALPlRLnGVKRKEAEKAAyawmERLEVEDLAAKRP-------GE----VSGGQGQRVAVARALVTAPRVVF 166
Cdd:COG5265 447 ---TIAYNIAYG-RP-DASEEEVEAAA----RAAQIHDFIESLPdgydtrvGErglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGTNAAVvlVTHEARVAAYSDREVVVRDGR 220
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLV--IAHRLSTIVDADEILVLEAGR 569
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-220 |
6.10e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.07 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAgivppdeGAIHYNGTELSALPESRRSA---LRRSdfGFVFQFGQLVPE 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIQGNNFTGTILANNRKPTkqiLKRT--GFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 LSCVENVALP--LRL-NGVKRKEAEKAAYAWMERLEVEDLAAKRPGE-----VSGGQGQRVAVARALVTAPRVVFADEPT 171
Cdd:PLN03211 155 LTVRETLVFCslLRLpKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 759535873 172 GALDSLNGER-VMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PLN03211 235 SGLDATAAYRlVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
23-220 |
8.79e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.45 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGivPPD----EGAIHYNGTELSALPESRRSALrrsdfGFVFQFgQLVP 98
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDERARA-----GLFLAF-QYPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ELSCVENVALpLR--LNGVKRKEAEKA--AYAWMERLEVEDLAAKRPGEV---------SGGQGQRVAVARALVTAPRVV 165
Cdd:TIGR01978 88 EIPGVSNLEF-LRsaLNARRSARGEEPldLLDFEKLLKEKLALLDMDEEFlnrsvnegfSGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 166 FADEPTGALDsLNGERVMELLTEAARGTNAAVVLVTHEARVAAY--SDREVVVRDGR 220
Cdd:TIGR01978 167 ILDEIDSGLD-IDALKIVAEGINRLREPDRSFLIITHYQRLLNYikPDYVHVLLDGR 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-220 |
1.43e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.77 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpESRRSALrRSDFGFV 90
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--KSSKEAL-ENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 91 FQFGQLVPELSCVENVAL---PLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 168 DEPTgalDSLNGERVMELLT--EAARGTNAAVVLVTHEA-RVAAYSDREVVVRDGR 220
Cdd:PRK10982 159 DEPT---SSLTEKEVNHLFTiiRKLKERGCGIVYISHKMeEIFQLCDEITILRDGQ 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
30-219 |
3.45e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 71.59 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 30 IHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSDFGFVFQFGQLVpELSCVENVALP 109
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATVEENITFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 110 LRLNGVKRKEAEKAAYAW--MERLEVEDLA--AKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGAL-----DSLNGE 180
Cdd:cd03290 103 SPFNKQRYKAVTDACSLQpdIDLLPFGDQTeiGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALdihlsDHLMQE 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 759535873 181 RVMELLTEAARgtnaAVVLVTHEARVAAYSDREVVVRDG 219
Cdd:cd03290 183 GILKFLQDDKR----TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-220 |
3.68e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.90 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpESRRSALRRSdFGFVFQFGQLVPE 99
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR---DYTLASLRNQ-VALVSQNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 lSCVENVALPlRLNGVKRKEAEKAA---YAwMERLE-VEDLAAKRPGE----VSGGQGQRVAVARALVTAPRVVFADEPT 171
Cdd:PRK11176 432 -TIANNIAYA-RTEQYSREQIEEAArmaYA-MDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759535873 172 GALDSlNGERVMELLTEAARgTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK11176 509 SALDT-ESERAIQAALDELQ-KNRTSLVIAHRLSTIEKADEILVVEDGE 555
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-220 |
6.41e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGA--EFSIHAgeVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGtelSALPESRRSALR- 83
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLnlDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG---KPLDYSKRGLLAl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 RSDFGFVFQF-GQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAP 162
Cdd:PRK13638 76 RQQVATVFQDpEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLTE-AARGTNaaVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNH--VIISSHDIDlIYEISDAVYVLRQGQ 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-217 |
9.44e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.45 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGaihyngtELSALPESRRSALRRSDFGFVFQFGQL---VP 98
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-------KISILGQPTRQALQKNLVAYVPQSEEVdwsFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ELscVENVALPLR---LNGVKRKEAEKAAY--AWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGA 173
Cdd:PRK15056 95 VL--VEDVVMMGRyghMGWLRRAKKRDRQIvtAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 759535873 174 LDSLNGERVMELLTEaARGTNAAVVLVTHE-ARVAAYSDREVVVR 217
Cdd:PRK15056 173 VDVKTEARIISLLRE-LRDEGKTMLVSTHNlGSVTEFCDYTVMVK 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-175 |
1.02e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 72.68 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 6 SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNG----TELSALPEsrrsa 81
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivARLQQDPP----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 82 lrRSDFGFVFQFgqlVPElsCVENVALPLR-----LNGVKRKEAEKA-------------AYAW------MERLEVEDLA 137
Cdd:PRK11147 77 --RNVEGTVYDF---VAE--GIEEQAEYLKryhdiSHLVETDPSEKNlnelaklqeqldhHNLWqlenriNEVLAQLGLD 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 759535873 138 AKRP-GEVSGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:PRK11147 150 PDAAlSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-220 |
1.25e-14 |
|
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: 69.60 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD---EGAIHYNGTELSALPESrrsalRRSDFGFVFQFGQLVPE 99
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK-----YPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 LSCVENVALPLRLNG--VKRKeaekaayawmerlevedlaakrpgeVSGGQGQRVAVARALVTAPRVVFADEPTGALDS- 176
Cdd:cd03233 98 LTVRETLDFALRCKGneFVRG-------------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSs 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 759535873 177 --LNGERVMELLTEAARGTNAAVVLvthEARVAAYS--DREVVVRDGR 220
Cdd:cd03233 153 taLEILKCIRTMADVLKTTTFVSLY---QASDEIYDlfDKVLVLYEGR 197
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-175 |
1.47e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPdEGAIHYNGTELSALPESRRSALRrsdfGFVFQFGQLVPELSCVENVA 107
Cdd:COG4138 17 AQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 108 LPLRLNGVkRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVT-------APRVVFADEPTGALD 175
Cdd:COG4138 92 LHQPAGAS-SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-220 |
1.93e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.60 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSY-GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSA--LPESRRSAlr 83
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenIREVRKFV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 rsdfGFVFQ------FGQLVPElscveNVAL-PLRLnGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVAR 156
Cdd:PRK13652 81 ----GLVFQnpddqiFSPTVEQ-----DIAFgPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 157 ALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDlVPEMADYIYVMDKGR 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-220 |
2.03e-14 |
|
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: 71.39 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPD-EGAIHYNGTELSA-------------LPESRRSAlrrsdfg 88
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIrnpaqairagiamVPEDRKRH------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 89 fvfqfgQLVPELSCVENVALPL--RLNGVKRKEA---EKAAYAWMERLEVEDLAAKRP-GEVSGGQGQRVAVARALVTAP 162
Cdd:TIGR02633 349 ------GIVPILGVGKNITLSVlkSFCFKMRIDAaaeLQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 163 RVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-175 |
2.18e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVpPDEGAIHYNGTELSALPES----RRSAL---RRSDFGF-VFQFGQLvpe 99
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelarHRAYLsqqQTPPFAMpVFQYLTL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 lscvenvALPlrlNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVA-------RALVTAPRVVFADEPTG 172
Cdd:PRK03695 93 -------HQP---DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
...
gi 759535873 173 ALD 175
Cdd:PRK03695 163 SLD 165
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-220 |
2.80e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALR---------RSDFGFvfqfgqlVP 98
Cdd:PRK09700 284 FSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKkgmayitesRRDNGF-------FP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ELSCVENVALP--LRLNGVKR-----KEAEKAAYAWMERlevEDLAAK------RPGEVSGGQGQRVAVARALVTAPRVV 165
Cdd:PRK09700 355 NFSIAQNMAISrsLKDGGYKGamglfHEVDEQRTAENQR---ELLALKchsvnqNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 166 FADEPTGALD-SLNGE--RVMELLTEAARGtnaaVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:PRK09700 432 IFDEPTRGIDvGAKAEiyKVMRQLADDGKV----ILMVSSElPEIITVCDRIAVFCEGR 486
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-219 |
3.10e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.36 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEG-------AIHYNGTELSALPESRRSALRRS---DFGFVFQ 92
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdieieldTVSYKPQYIKADYEGTVRDLLSSitkDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 93 FgqlvpelscVENVALPLRLNGVkrkeaekaayawMERlEVEDLaakrpgevSGGQGQRVAVARALVTAPRVVFADEPTG 172
Cdd:cd03237 95 F---------KTEIAKPLQIEQI------------LDR-EVPEL--------SGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 759535873 173 ALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAY-SDReVVVRDG 219
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYlADR-LIVFEG 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-220 |
8.48e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALrrsDFGFVF-----QFGQLV 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV--TRSPQDGL---ANGIVYisedrKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PELSCVENVALP----LRLNGVKRKEAEkaayawmERLEVEDLAA----KRP------GEVSGGQGQRVAVARALVTAPR 163
Cdd:PRK10762 343 LGMSVKENMSLTalryFSRAGGSLKHAD-------EQQAVSDFIRlfniKTPsmeqaiGLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQfKAEGL--SIILVSSEmPEVLGMSDRILVMHEGR 472
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
8-228 |
1.14e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.99 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSG--KSTLLhclAGIVPPDEGAIHYNGTELSAlpesRRSALRRS 85
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP---AHV*GPDAGRRPWRF*TWCA----NRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 dfgfvfqFGQLVP-------ELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARAL 158
Cdd:NF000106 87 -------IG*HRPvr*grreSFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 159 VTAPRVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVT----HEARVAAYS----DREVVVRDGRSRDMERLV 228
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR--DGATVLLTtqymEEAEQLAHEltviDRGRVIADGKVDELKTKV 235
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-220 |
1.16e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.80 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 24 DGAEFSIHAGEVVAIMGPSGSGKStlLHCLA--GIVPPD----EGAIHYNGTELSAlpesrrSALR-----------RSD 86
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAalGILPAGvrqtAGRVLLDGKPVAP------CALRgrkiatimqnpRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGfvfqfgqlvPELSCVENVALPLRLNGVKRKEAekAAYAWMERLEVED---LAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:PRK10418 92 FN---------PLHTMHTHARETCLALGKPADDA--TLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVArLADDVAVMSHGR 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-215 |
5.09e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGatnaldgaEFS-------IHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGA------IHYNGTELSA 73
Cdd:PRK13409 340 LVEYPDLTKKLG--------DFSleveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEvdpelkISYKPQYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 74 LPESRRSALRRS---DFGFVFqfgqLVPELscvenvalplrlngvkrkeaekaayawMERLEVEDLAAKRPGEVSGGQGQ 150
Cdd:PRK13409 412 DYDGTVEDLLRSitdDLGSSY----YKSEI---------------------------IKPLQLERLLDKNVKDLSGGELQ 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 151 RVAVARALVTAPRVVFADEPTGALDSlnGERVMelLTEA----ARGTNAAVVLVTHEARVAAY-SDREVV 215
Cdd:PRK13409 461 RVAIAACLSRDADLYLLDEPSAHLDV--EQRLA--VAKAirriAEEREATALVVDHDIYMIDYiSDRLMV 526
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
36-176 |
6.06e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 36 VAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPEsrrSALRRSdFGFVfQFGQLVPELSCVENVALplrlngv 115
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQG-VAMV-QQDPVVLADTFLANVTL------- 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 116 KRKEAEKAAYAWMERLEVEDLAAKRP-------GE----VSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PRK10790 438 GRDISEEQVWQALETVQLAELARSLPdglytplGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-175 |
7.72e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 2 IPSG-----SLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGT-ELSALP 75
Cdd:TIGR03719 312 IPPGprlgdKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 76 ESRRSalrrsdfgfvfqfgqLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDlAAKRPGEVSGGQGQRVAVA 155
Cdd:TIGR03719 392 QSRDA---------------LDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSD-QQKKVGQLSGGERNRVHLA 455
|
170 180
....*....|....*....|
gi 759535873 156 RALVTAPRVVFADEPTGALD 175
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-212 |
8.94e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.36 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 18 GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGI------VPPDEgaIHYNGTELSALPESRRSALRRSDFGFVF 91
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnwrVTADR--MRFDDIDLLRLSPRERRKLVGHNVSMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 92 QFGQlvpelSCV---ENVALPLRLN--GVKRKEAEKAAYAWMERLEVE-----------DLAAKRPGEVSGGQGQRVAVA 155
Cdd:PRK15093 96 QEPQ-----SCLdpsERVGRQLMQNipGWTYKGRWWQRFGWRKRRAIEllhrvgikdhkDAMRSFPYELTEGECQKVMIA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 156 RALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEAR-VAAYSDR 212
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmLSQWADK 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-211 |
1.06e-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: 65.47 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 33 GEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAI-----------HYNGTEL----SALPESRRSALRRSdfgfvfQFGQLV 97
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELqnyfTKLLEGDVKVIVKP------QYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PElsCVENVALPLrlngVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD-- 175
Cdd:cd03236 100 PK--AVKGKVGEL----LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDik 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 759535873 176 -SLNGERVMELLTEAARgtnaAVVLVTHEARVAAY-SD 211
Cdd:cd03236 174 qRLNAARLIRELAEDDN----YVLVVEHDLAVLDYlSD 207
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-203 |
1.33e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.67 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 33 GEVVAIMGPSGSGKSTLLHCLAGIVppDEGAIHyNGTELSALPESRRSALRRSdfGFVFQFGQLVPELSCVENVALPLRL 112
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERV--TTGVIT-GGDRLVNGRPLDSSFQRSI--GYVQQQDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 113 ---NGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGG----QGQRVAVARALVTAPR-VVFADEPTGALDSLNGERVME 184
Cdd:TIGR00956 864 rqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICK 943
|
170
....*....|....*....
gi 759535873 185 LLTEAARgTNAAVVLVTHE 203
Cdd:TIGR00956 944 LMRKLAD-HGQAILCTIHQ 961
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-224 |
1.77e-12 |
|
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: 66.12 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTeLSALPESrrsALRRSDfgfvfqfgqlvpelSC 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-VAYVPQQ---AWIQND--------------SL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENVALPLRLNGvKRKEAEKAAYAWMERLEV-----EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSL 177
Cdd:TIGR00957 716 RENILFGKALNE-KYYQQVLEACALLPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 759535873 178 NGERVME-LLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGRSRDM 224
Cdd:TIGR00957 795 VGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM 842
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-222 |
2.28e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 24 DGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVP-PDEGAIHYNGTELSA-------------LPESRRsalrrsdfgf 89
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIrnpqqaiaqgiamVPEDRK---------- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 vfQFGqLVPELSCVENVALPL--RLNGVKR--KEAE-KAAYAWMERLEVE----DLAAKRpgeVSGGQGQRVAVARALVT 160
Cdd:PRK13549 349 --RDG-IVPVMGVGKNITLAAldRFTGGSRidDAAElKTILESIQRLKVKtaspELAIAR---LSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759535873 161 APRVVFADEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHE-ARVAAYSDREVVVRDGRSR 222
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEIYKLINQlVQQGV--AIIVISSElPEVLGLSDRVLVMHEGKLK 484
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-191 |
2.65e-12 |
|
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: 63.03 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLA-----GIVppdEGAIHYNGTELsalpesrRSALRRSdFGFVFQFGQLV 97
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILINGRPL-------DKNFQRS-TGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PELSCVEnvalPLRLNgvkrkeaekaayAWMERLEVEdlaakrpgevsggQGQRVAVARALVTAPRVVFADEPTGALDSL 177
Cdd:cd03232 92 PNLTVRE----ALRFS------------ALLRGLSVE-------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170
....*....|....
gi 759535873 178 NGERVMELLTEAAR 191
Cdd:cd03232 143 AAYNIVRFLKKLAD 156
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-220 |
5.81e-12 |
|
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: 61.24 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 33 GEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRsalrrsdfgfvfqfgqlvpelscvenvalplrl 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQ--------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 113 ngvkrkeaekaayawmerlEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS-----LNGERVMELLT 187
Cdd:smart00382 49 -------------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 759535873 188 EAARGTNAAVVLVTH------EARVAAYSDREVVVRDGR 220
Cdd:smart00382 110 LLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLIL 148
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-202 |
9.12e-12 |
|
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: 64.26 E-value: 9.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATN--ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTE-LSALPESRRSalr 83
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQN--- 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 rsdFGFVFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPR 163
Cdd:TIGR01257 2014 ---MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190
....*....|....*....|....*....|....*....
gi 759535873 164 VVFADEPTGALDSLNGERVMELLTEAARgTNAAVVLVTH 202
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSH 2128
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-64 |
9.31e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 9.31e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 8 LSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAI 64
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-220 |
9.78e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 1 MIPSGSLLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGivPPD----EGAIHYNGTELSALPE 76
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 77 SRRSALrrsdfGFVFQFgQLVPELSCVENVALpLRLN-GVKRKE---AEKAAYAW----MERLEVEDLAAK------RPG 142
Cdd:CHL00131 79 EERAHL-----GIFLAF-QYPIEIPGVSNADF-LRLAyNSKRKFqglPELDPLEFleiiNEKLKLVGMDPSflsrnvNEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 143 eVSGGQGQRVAVARALVTAPRVVFADEPTGALDslngervMELLTEAARGTNA------AVVLVTHEARVAAY--SDREV 214
Cdd:CHL00131 152 -FSGGEKKRNEILQMALLDSELAILDETDSGLD-------IDALKIIAEGINKlmtsenSIILITHYQRLLDYikPDYVH 223
|
....*.
gi 759535873 215 VVRDGR 220
Cdd:CHL00131 224 VMQNGK 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-215 |
1.44e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGatnaldgaEFS-------IHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIH------YNGTELSA 73
Cdd:COG1245 341 LVEYPDLTKSYG--------GFSleveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisYKPQYISP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 74 LPESRRSALRRSDFGFVFQFGQLVPElscvenVALPLRLNGVkrkeaekaayawMERlEVEDLaakrpgevSGGQGQRVA 153
Cdd:COG1245 413 DYDGTVEEFLRSANTDDFGSSYYKTE------IIKPLGLEKL------------LDK-NVKDL--------SGGELQRVA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 154 VARALVTAPRVVFADEPTGALDSlnGERVM--ELLTEAARGTNAAVVLVTHEARVAAY-SDREVV 215
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDV--EQRLAvaKAIRRFAENRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-220 |
1.96e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 26 AEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalPESRRSALRRsdfGFVF-----QFGQLVPEL 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID--IRSPRDAIRA---GIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 101 SCVENVALPLRLNGVK-------RKEAEKAayawmeRLEVEDLAAKRP------GEVSGGQGQRVAVARALVTAPRVVFA 167
Cdd:PRK11288 347 SVADNINISARRHHLRagclinnRWEAENA------DRFIRSLNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 759535873 168 DEPTGALDSLNGERVMELLTE-AARGTnaAVVLVTHE-ARVAAYSDREVVVRDGR 220
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYElAAQGV--AVLFVSSDlPEVLGVADRIVVMREGR 473
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-220 |
3.69e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 16 SYGATNALDGAEFSIH-------------AGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesrrsal 82
Cdd:PRK10575 7 HSDTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 83 rrSDFGFVFQFGQLVPELSCVENVALplrlngvkRKEAEKAAYAW---MERLEVED---------------LAAKRPGEV 144
Cdd:PRK10575 79 --SSKAFARKVAYLPQQLPAAEGMTV--------RELVAIGRYPWhgaLGRFGAADrekveeaislvglkpLAHRLVDSL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 145 SGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAA-YSDREVVVRDGR 220
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGE 225
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-209 |
5.31e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGI--VPPDEGAIHYNGTELSAL-PESRRSalr 83
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELsPEDRAG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 84 rSDFGFVFQFGQLVPELScvENVALPLRLNGVKRKEAEKAayawMERLEVEDLAA------KRPGEV---------SGGQ 148
Cdd:PRK09580 78 -EGIFMAFQYPVEIPGVS--NQFFLQTALNAVRSYRGQEP----LDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 149 GQRVAVARALVTAPRVVFADEPTGALDsLNGERVMELLTEAARGTNAAVVLVTHEARVAAY 209
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTHYQRILDY 210
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-169 |
1.50e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.20 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTelsALPESRRSALRR------SDFgFVFQfgqlvpels 101
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAYRQlfsavfSDF-HLFD--------- 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 102 cvenvalplRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSG---GQGQRvavAR-ALVTA-----PRVVFaDE 169
Cdd:COG4615 420 ---------RLLGLDGEADPARARELLERLELDHKVSVEDGRFSTtdlSQGQR---KRlALLVAlledrPILVF-DE 483
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-177 |
1.87e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 9 SAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlPESRRSALRRSDF- 87
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-ARHRRAVCPRIAYm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 88 ----GfvfqfGQLVPELSCVENVALPLRLNGVKRKEAEkaayAWMERL-EVEDLA--AKRP-GEVSGGQGQRVAVARALV 159
Cdd:NF033858 82 pqglG-----KNLYPTLSVFENLDFFGRLFGQDAAERR----RRIDELlRATGLApfADRPaGKLSGGMKQKLGLCCALI 152
|
170
....*....|....*...
gi 759535873 160 TAPRVVFADEPTGALDSL 177
Cdd:NF033858 153 HDPDLLILDEPTTGVDPL 170
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-213 |
1.96e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELsalpeSRRSALRRSDFGFVFQFGQLVPELSC 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-----KKDLCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENVALPLRLNGVKRKEAEKAAYawmerLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERV 182
Cdd:PRK13540 92 RENCLYDIHFSPGAVGITELCRL-----FSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180 190
....*....|....*....|....*....|.
gi 759535873 183 MELLtEAARGTNAAVVLVTHEARVAAYSDRE 213
Cdd:PRK13540 167 ITKI-QEHRAKGGAVLLTSHQDLPLNKADYE 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-203 |
3.90e-10 |
|
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: 58.79 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 12 GLRKSYGAT-NALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGaihyngtelsalpESRRSALRRsdFGFV 90
Cdd:TIGR03719 9 RVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------------EARPQPGIK--VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 91 FQFGQLVPELSCVENVALPL--------RLNGVKRKEAE-------------------KAAYAW-MER-LEVEDLAAKRP 141
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGVaeikdaldRFNEISAKYAEpdadfdklaaeqaelqeiiDAADAWdLDSqLEIAMDALRCP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 142 ------GEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSlngERVmELLTEAARGTNAAVVLVTHE 203
Cdd:TIGR03719 154 pwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESV-AWLERHLQEYPGTVVAVTHD 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-191 |
4.24e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 10 AEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpesRRSALRRSdFGF 89
Cdd:NF033858 269 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA----GDIATRRR-VGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 VFQFGQLVPELSCVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180
....*....|....*....|..
gi 759535873 170 PTGALDSLNGERVMELLTEAAR 191
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSR 445
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-226 |
6.28e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesRRSALrRSDFGFVFQFGQLVPElS 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSW-RSRLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 102 CVENVAL--PlrlnGVKRKEAEKAAyawmeRL-EVEDLAAKRP-------GE----VSGGQGQRVAVARALVTAPRVVFA 167
Cdd:PRK10789 405 VANNIALgrP----DATQQEIEHVA-----RLaSVHDDILRLPqgydtevGErgvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 168 DEPTGALDSLNGERVMELLTEAARG-------------TNAAVVLVTHEARVAAYSDREVVV-RDGRSRDMER 226
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGrtviisahrlsalTEASEILVMQHGHIAQRGNHDQLAqQSGWYRDMYR 548
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-220 |
1.79e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 30 IHAGEVVAIMGPSGSGKSTLLHCLA----GIVPPDEGAIHYNGTElsalPESRRSALRrsdfGFVFQFGQL---VPELSC 102
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT----PEEIKKHYR----GDVVYNAETdvhFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENVALPLRL-------NGVKRKE-AEKAAYAWMERLEVEDLAAKRPGE-----VSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:TIGR00956 156 GETLDFAARCktpqnrpDGVSREEyAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 759535873 170 PTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYS--DREVVVRDGR 220
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYElfDKVIVLYEGY 288
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-202 |
2.84e-09 |
|
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: 56.33 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 33 GEVVAIMGPSGSGKSTLLHCLAGIV---------PPDEGAI--HYNGTEL----SALPESRRSALRRSdfgfvfQFGQLV 97
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSWDEVlkRFRGTELqdyfKKLANGEIKVAHKP------QYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 PElscvenvalplRLNG-VK--------RKEAEKAAyawmERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFAD 168
Cdd:COG1245 173 PK-----------VFKGtVRellekvdeRGKLDELA----EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*.
gi 759535873 169 EPTGALDSlnGER--VMELLTEAARGtNAAVVLVTH 202
Cdd:COG1245 238 EPSSYLDI--YQRlnVARLIRELAEE-GKYVLVVEH 270
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-175 |
5.58e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 2 IPSGSLL-----SAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGT-ELSALP 75
Cdd:PRK11819 314 IPPGPRLgdkviEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvKLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 76 ESRRSalrrsdfgfvfqfgqLVPELSCVENVALPLRLNGVKRKEAEKAAYawmerlevedLAA---------KRPGEVSG 146
Cdd:PRK11819 394 QSRDA---------------LDPNKTVWEEISGGLDIIKVGNREIPSRAY----------VGRfnfkggdqqKKVGVLSG 448
|
170 180
....*....|....*....|....*....
gi 759535873 147 GQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-202 |
6.75e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 33 GEVVAIMGPSGSGKSTLLHCLAGIVPP-----------DEGAIHYNGTEL----SALPESRRSALRRSdfgfvfQFgqlv 97
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPnlgdyeeepswDEVLKRFRGTELqnyfKKLYNGEIKVVHKP------QY---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 pelscVEnvALPLRLNG-----VKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTG 172
Cdd:PRK13409 169 -----VD--LIPKVFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|..
gi 759535873 173 ALDSlnGER--VMELLTEAARgtNAAVVLVTH 202
Cdd:PRK13409 242 YLDI--RQRlnVARLIRELAE--GKYVLVVEH 269
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-205 |
2.09e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGtELSALPESrrsalrrsdfgfvfqfGQLVPELS 101
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAIS----------------AGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 102 CVENVALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGER 181
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180
....*....|....*....|....
gi 759535873 182 VMELLTEaARGTNAAVVLVTHEAR 205
Cdd:PRK13546 182 CLDKIYE-FKEQNKTIFFVSHNLG 204
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-169 |
2.26e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 8 LSAEGLRKSYGATN-ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpeSRRSALrRSD 86
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDY-RKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 87 FGFVFQfgqlvpelscveNVALPLRLNGVKRKEAEKAAY-AWMERLEVEDLAAKRPGEV-----SGGQGQRVAVARALVT 160
Cdd:PRK10522 399 FSAVFT------------DFHLFDQLLGPEGKPANPALVeKWLERLKMAHKLELEDGRIsnlklSKGQKKRLALLLALAE 466
|
....*....
gi 759535873 161 APRVVFADE 169
Cdd:PRK10522 467 ERDILLLDE 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-220 |
2.40e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSalpesRRSALRRSDFGFVFQ---------FGQLVP 98
Cdd:PRK10982 269 FDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKIN-----NHNANEAINHGFALVteerrstgiYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 EL-SCVENVALPLRLNGVKRKEAEKAAYAWMerleVEDLAAKRP------GEVSGGQGQRVAVARALVTAPRVVFADEPT 171
Cdd:PRK10982 344 GFnSLISNIRNYKNKVGLLDNSRMKSDTQWV----IDSMRVKTPghrtqiGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759535873 172 GALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
28-221 |
3.07e-08 |
|
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: 52.94 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGtelsalpesRRSalrrsdfgFVFQFGQLVPElSCVENVA 107
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG---------RIS--------FSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 108 LPLRLNGVKRKEAEKAAyawmeRLEvEDLaAKRP-------GE----VSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:cd03291 120 FGVSYDEYRYKSVVKAC-----QLE-EDI-TKFPekdntvlGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 759535873 177 LNGERVME-----LLTEAARgtnaavVLVTHEARVAAYSDREVVVRDGRS 221
Cdd:cd03291 193 FTEKEIFEscvckLMANKTR------ILVTSKMEHLKKADKILILHEGSS 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
144-215 |
3.96e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 3.96e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759535873 144 VSGGQGQRVAVARALVTAPRVVFADEPTGALDSlNGERVME-LLTEAARGTNAAVVLVTHEARVAAYSDREVV 215
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIEkTIVDIKDKADKTIITIAHRIASIKRSDKIVV 1430
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-221 |
4.20e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSAlpesrRSALRRSDFGFVF-----QFGQLVPELSC 102
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINA-----LSTAQRLARGLVYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENV-ALPLRLNGVKRKEAEKAAYawMER--------LEVEDLAAKRpgeVSGGQGQRVAVARALVTAPRVVFADEPTGA 173
Cdd:PRK15439 359 AWNVcALTHNRRGFWIKPARENAV--LERyrralnikFNHAEQAART---LSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759535873 174 LDSLNGERVMELLTEAARgTNAAVVLVT---HEarVAAYSDREVVVRDGRS 221
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAA-QNVAVLFISsdlEE--IEQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-216 |
9.23e-08 |
|
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: 50.26 E-value: 9.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 30 IHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrrsalrrsdfgfvfqfgQLVpelscvenvalp 109
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-------------------QYI------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 110 lrlngvkrkeaekaayawmerlevedlaakrpgEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS---LNGERVMELL 186
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|.
gi 759535873 187 TEAARGTnaaVVLVTHEARVAAY-SDREVVV 216
Cdd:cd03222 118 SEEGKKT---ALVVEHDLAVLDYlSDRIHVF 145
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-183 |
1.01e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 33 GEVVAIMGPSGSGKSTLLHCLAGivpPDEGAIHYNGTELSALPESRRSALRRSdfGFVFQFGQLVPELSCVENVALP--L 110
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFARIS--GYCEQNDIHSPQVTVRESLIYSafL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 111 RLNGVKRKEaEKAAYA--WMERLEVEDLA---AKRPG--EVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVM 183
Cdd:PLN03140 981 RLPKEVSKE-EKMMFVdeVMELVELDNLKdaiVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-219 |
1.13e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAihyngtelsalpesrrSALRRSDFGFVfqfgqlvPELSCV---- 103
Cdd:PLN03130 638 LDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA----------------SVVIRGTVAYV-------PQVSWIfnat 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 104 --ENVALPLRLNGVKRKEAEKAAyAWMERLEV---EDLA--AKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDS 176
Cdd:PLN03130 695 vrDNILFGSPFDPERYERAIDVT-ALQHDLDLlpgGDLTeiGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 177 LNGERVME-LLTEAARGTNAavVLVTHEARVAAYSDREVVVRDG 219
Cdd:PLN03130 774 HVGRQVFDkCIKDELRGKTR--VLVTNQLHFLSQVDRIILVHEG 815
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-221 |
1.33e-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: 51.83 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGtelsalpesRRSalrrsdfgFVFQFGQLVPE 99
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG---------RIS--------FSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 lSCVENVALPLRLNGVKRKEAEKAAyawmeRLEvEDLAA-----KRP-GE----VSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:TIGR01271 502 -TIKDNIIFGLSYDEYRYTSVIKAC-----QLE-EDIALfpekdKTVlGEggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 170 PTGALDSLNGERVME-----LLTEAARgtnaavVLVTHEARVAAYSDREVVVRDGRS 221
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEGVC 625
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-220 |
1.35e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEG--LRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELS--ALPESR 78
Cdd:PLN03232 1230 PSRGSIKFEDvhLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 79 RSAlrrsdfgfvfqfgQLVPElscvenvaLPLRLNGVKR-------KEAEKAAYAWMERLEVEDLAAKRP---------- 141
Cdd:PLN03232 1310 RVL-------------SIIPQ--------SPVLFSGTVRfnidpfsEHNDADLWEALERAHIKDVIDRNPfgldaevseg 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 142 GE-VSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARgtNAAVVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PLN03232 1369 GEnFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKILVLSSGQ 1446
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
144-220 |
1.40e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 1.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 144 VSGGQGQRVAVARAlVTAPRVVFA-DEPTGALDSLNGERVM-ELLTEAARGTNAavVLVTHEARVAAYSDREVVVRDGR 220
Cdd:PTZ00243 783 LSGGQKARVSLARA-VYANRDVYLlDDPLSALDAHVGERVVeECFLGALAGKTR--VLATHQVHVVPRADYVVALGDGR 858
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-219 |
1.52e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAihyngtelsalpesrrSALRRSDFGFVfqfgqlvPELSC 102
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS----------------SVVIRGSVAYV-------PQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENVALplRLNGVKRKEAEKAAYaW-----------MERLEVEDLA--AKRPGEVSGGQGQRVAVARALVTAPRVVFADE 169
Cdd:PLN03232 690 IFNATV--RENILFGSDFESERY-WraidvtalqhdLDLLPGRDLTeiGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 759535873 170 PTGALDSLNGERVME-LLTEAARGTNAavVLVTHEARVAAYSDREVVVRDG 219
Cdd:PLN03232 767 PLSALDAHVAHQVFDsCMKDELKGKTR--VLVTNQLHFLPLMDRIILVSEG 815
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-202 |
4.33e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 12 GLRKSYGATNA-LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEG-AIHYNGTELSALPesrrsalrrsdfgf 89
Cdd:PRK11819 11 RVSKVVPPKKQiLKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKVGYLP-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 vfQFGQLVPELSCVENV--------ALPLRLNGVKRKEAEKAAY-----AWMERLEVE-------DLAAK--------R- 140
Cdd:PRK11819 77 --QEPQLDPEKTVRENVeegvaevkAALDRFNEIYAAYAEPDADfdalaAEQGELQEIidaadawDLDSQleiamdalRc 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 759535873 141 -PGE-----VSGGQGQRVAVARALVTAPRVVFADEPTGALDSlngERVMEL---LTEAArGTnaaVVLVTH 202
Cdd:PRK11819 155 pPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLeqfLHDYP-GT---VVAVTH 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-208 |
6.15e-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: 49.52 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 3 PSGSLLSAEGLRKSY--GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVpPDEGAIHYNGTELSALPESRrs 80
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQT-- 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 81 alRRSDFGfvfqfgqLVPELSCVENVALPLRLNGVKRKEAEKaAYAWMERLEVEDLAAKRPGE-----------VSGGQG 149
Cdd:TIGR01271 1290 --WRKAFG-------VIPQKVFIFSGTFRKNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHK 1359
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 150 QRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAArgTNAAVVLVTHeaRVAA 208
Cdd:TIGR01271 1360 QLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF--SNCTVILSEH--RVEA 1414
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-215 |
6.79e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 10 AEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYnGTELSalpesrrsalrrsdfgf 89
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 90 VFQFGQ----LVPELSCVENVA---LPLRLNGVKR-------------KEAekaayawmeRLEVEDLaakrpgevSGGQG 149
Cdd:PRK11147 384 VAYFDQhraeLDPEKTVMDNLAegkQEVMVNGRPRhvlgylqdflfhpKRA---------MTPVKAL--------SGGER 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 759535873 150 QRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEaARGTnaaVVLVTHearvaaysDREVV 215
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQGT---VLLVSH--------DRQFV 500
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-200 |
1.47e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 20 TNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGivppdegaihyngtELSALPESRRSALRRSDFGFVFQFGQLVPE 99
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAG--------------ELPLLSGERQSQFSHITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 100 ---------LSCVEN----VALPLRLNGVKrKEAEKAAYAwmERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVF 166
Cdd:PRK10938 82 ewqrnntdmLSPGEDdtgrTTAEIIQDEVK-DPARCEQLA--QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190
....*....|....*....|....*....|....
gi 759535873 167 ADEPTGALDSLNGERVMELLTEAARGtNAAVVLV 200
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-175 |
1.47e-06 |
|
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: 48.40 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 29 SIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALP-ESRRSALrrsdfgfvfqfgQLVPELSCVENVA 107
Cdd:TIGR00957 1308 TIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlHDLRFKI------------TIIPQDPVLFSGS 1375
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759535873 108 LPLRLNGVKRKEAEKAAYAwMERLEVEDLAAKRP----------GE-VSGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEVWWA-LELAHLKTFVSALPdkldhecaegGEnLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-69 |
1.59e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 1.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 759535873 22 ALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGT 69
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS 86
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-211 |
2.70e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.70e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 759535873 134 EDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVLVTHEARVAAYSD 211
Cdd:PTZ00265 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYAN 647
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-227 |
5.28e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.00 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 18 GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVpPDEGAIHYNGTELSALPESRrsalRRSDFGFVFQfgqlv 97
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQK----WRKAFGVIPQ----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 98 pelsCVENVALPLRLN-GVKRKEAEKAAYAWMERLEVEDLAAKRPGE-----------VSGGQGQRVAVARALVTAPRVV 165
Cdd:cd03289 85 ----KVFIFSGTFRKNlDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759535873 166 FADEPTGALDSLNGERVMELLTEAARGtnAAVVLVTHEARVAAYSDREVVVRDGRSRDMERL 227
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKVRQYDSI 220
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-178 |
5.57e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 16 SYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPpdEGaihYNgTELSALPESRRSALR----RSDFGFVF 91
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QG---YS-NDLTLFGRRRGSGETiwdiKKHIGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 92 QFGQLVPELSC-VENVALPLRLNGVKRKEA-----EKAAYAWMERLEVEDLAAKRP-GEVSGGQgQRVA-VARALVTAPR 163
Cdd:PRK10938 343 SSLHLDYRVSTsVRNVILSGFFDSIGIYQAvsdrqQKLAQQWLDILGIDKRTADAPfHSLSWGQ-QRLAlIVRALVKHPT 421
|
170
....*....|....*
gi 759535873 164 VVFADEPTGALDSLN 178
Cdd:PRK10938 422 LLILDEPLQGLDPLN 436
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-228 |
2.47e-05 |
|
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: 43.47 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 21 NALDGAEFSIHAGEVVAIMGPSGSGKSTLlhCLAGIVppdegaihyngTELSALPESRRSALRRSDFGFVFQFGQLVpel 100
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY-----------ASGKARLISFLPKFSRNKLIFIDQLQFLI--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 101 scveNVALP-LRLNgvkrkeaekaayawmerlevedlaakRP-GEVSGGQGQRVAVARAL-VTAPRVVFA-DEPTGALDS 176
Cdd:cd03238 73 ----DVGLGyLTLG--------------------------QKlSTLSGGELQRVKLASELfSEPPGTLFIlDEPSTGLHQ 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 759535873 177 LNGERVMELLtEAARGTNAAVVLVTHEARVAAYSDREVVVRDGRSRDMERLV 228
Cdd:cd03238 123 QDINQLLEVI-KGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVV 173
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-79 |
3.41e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 4 SGSLLsAEGLRKSY--GATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSA--LPESRR 79
Cdd:PTZ00243 1306 AGSLV-FEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRELRR 1384
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-220 |
5.49e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 28 FSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAI--------------HYNGTELSALPesrrsalrrsdfgfvfqf 93
Cdd:PLN03073 530 FGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSNP------------------ 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 94 gqLVPELSCVENVAlplrlngvkrkeaEKAAYAWMERLEVE-DLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTG 172
Cdd:PLN03073 592 --LLYMMRCFPGVP-------------EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 759535873 173 ALDsLNGervMELLTEAARGTNAAVVLVTHEARVAAYSDREV-VVRDGR 220
Cdd:PLN03073 657 HLD-LDA---VEALIQGLVLFQGGVLMVSHDEHLISGSVDELwVVSEGK 701
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-175 |
5.81e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALpesrrsALR--RSDFGFVFQfgqlvpel 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF------GLMdlRKVLGIIPQ-------- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 101 scvenvaLPLRLNGVKRKEAE-----KAAYAW--MERLEVEDLAAKRP----GEV-------SGGQGQRVAVARALVTAP 162
Cdd:PLN03130 1321 -------APVLFSGTVRFNLDpfnehNDADLWesLERAHLKDVIRRNSlgldAEVseagenfSVGQRQLLSLARALLRRS 1393
|
170
....*....|...
gi 759535873 163 RVVFADEPTGALD 175
Cdd:PLN03130 1394 KILVLDEATAAVD 1406
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-220 |
6.06e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 7 LLSAEGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHY-NGTELSALPESRRSALrRS 85
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEFL-RA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 86 DFGFVFQFGQLVPelscvenvalplrlngvkrKEAEKAAYAWMERLEVE-DLAAKRPGEVSGGQGQRVAVARALVTAPRV 164
Cdd:PRK10636 391 DESPLQHLARLAP-------------------QELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 759535873 165 VFADEPTGALDsLNgerVMELLTEAARGTNAAVVLVTHEAR-VAAYSDREVVVRDGR 220
Cdd:PRK10636 452 LLLDEPTNHLD-LD---MRQALTEALIDFEGALVVVSHDRHlLRSTTDDLYLVHDGK 504
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
29-214 |
6.11e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 29 SIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSAlrrsdfGFVFQFGQLvpelscvenval 108
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSA------ELIFTRLQL------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 109 plrlngvkrkeaekaayawmerlevedlaakrpgevSGGQGQRVAVARALV---TAPR-VVFADEPTGALDSLNGERVME 184
Cdd:cd03227 79 ------------------------------------SGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAE 122
|
170 180 190
....*....|....*....|....*....|
gi 759535873 185 LLTEAARGtNAAVVLVTHEARVAAYSDREV 214
Cdd:cd03227 123 AILEHLVK-GAQVIVITHLPELAELADKLI 151
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-175 |
6.58e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPESRRSALRRSDFGFVF----QFGQLVP 98
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdrEYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 99 ELSCVEN-------VALPLRLNGVKRKEAEKAAYAWMERLEVEDLAAKRP-GEVSGGQGQRVAVARALVTAPRVVFADEP 170
Cdd:PRK10636 97 QLHDANErndghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
....*
gi 759535873 171 TGALD 175
Cdd:PRK10636 177 TNHLD 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
38-199 |
7.83e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 38 IMGPSGSGKSTLLHCLAGIVPPD---EGAIHYNGTELSALPESRRSAlrrsdfgFVFQFGQLVPELSCVENVALPLRLNG 114
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSA-------YISQNDVHVGVMTVKETLDFSARCQG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 115 V----------KRKEAEKAAY-----------AWMERLE---VEDLAAKRPG---------------EVSGGQGQRVAVA 155
Cdd:PLN03140 269 VgtrydllselARREKDAGIFpeaevdlfmkaTAMEGVKsslITDYTLKILGldickdtivgdemirGISGGQKKRVTTG 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 759535873 156 RALVTAPRVVFADEPTGALDSLNGERVMELLTEAARGTNAAVVL 199
Cdd:PLN03140 349 EMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM 392
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
23-206 |
9.32e-05 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 41.97 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 23 LDGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGaiHYNGTELSALPESRRSAlrrsdfgfvfqfgqLVPELSC 102
Cdd:PRK15177 3 LDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEG--DFIGLRGDALPLGANSF--------------ILPGLTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 103 VENVALPLRLNGVKRKEAEKAAYawmERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADeptGALdsLNGERV 182
Cdd:PRK15177 67 EENARMMASLYGLDGDEFSHFCY---QLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIAD---GKL--YTGDNA 138
|
170 180
....*....|....*....|....*..
gi 759535873 183 MELLTEAARG---TNAAVVLVTHEARV 206
Cdd:PRK15177 139 TQLRMQAALAcqlQQKGLIVLTHNPRL 165
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-219 |
1.10e-04 |
|
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: 42.20 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 30 IHAGEVVAIMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALP----ESRRSALRRSD--FGFVFQFgQLVPELSCV 103
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlhtlRSRLSIILQDPilFSGSIRF-NLDPECKCT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 104 ENvALPLRLNGVKRKEAEKAAYAWMERLEVEDlaakrpGE-VSGGQGQRVAVARALVTAPRVVFADEPTGALDsLNGERV 182
Cdd:cd03288 123 DD-RLWEALEIAQLKNMVKSLPGGLDAVVTEG------GEnFSVGQRQLFCLARAFVRKSSILIMDEATASID-MATENI 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 759535873 183 ME--LLTEAARGTnaaVVLVTHEARVAAYSDREVVVRDG 219
Cdd:cd03288 195 LQkvVMTAFADRT---VVTIAHRVSTILDADLVLVLSRG 230
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-67 |
1.28e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.74 E-value: 1.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 759535873 24 DGAEFSIHAGEVVAIMGPSGSGKSTLLHCLAGI-VPPdeGAIHYN 67
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLlVPA--KRARFN 55
|
|
| XRCC2 |
cd19490 |
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ... |
33-74 |
1.49e-04 |
|
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site.
Pssm-ID: 410898 [Multi-domain] Cd Length: 226 Bit Score: 41.56 E-value: 1.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 759535873 33 GEVVAIMGPSGSGKSTLL-HCLA-GIVPPDEGAIHYNGTELSAL 74
Cdd:cd19490 1 GDVIEITGPSGSGKTELLyHLAArCILPSSWGGVPLGGLEAAVV 44
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-211 |
1.86e-04 |
|
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: 41.05 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 35 VVAIMGPSGSGKSTLLHC----LAGIVPPdegaihyNGTELSALPESRRSALRRSDfgfvfqfgqlvpelscvenVALPL 110
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkyaLTGELPP-------NSKGGAHDPKLIREGEVRAQ-------------------VKLAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 111 RL-NGVK----RKEA--EKAAYAWMErlEVEDLAAKRPGEVSGGQgqRVAVARALVTAPRVVFA--------DEPTGALD 175
Cdd:cd03240 78 ENaNGKKytitRSLAilENVIFCHQG--ESNWPLLDMRGRCSGGE--KVLASLIIRLALAETFGsncgilalDEPTTNLD 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 759535873 176 SLNGERVM-ELLTEAARGTNAAVVLVTHEARVAAYSD 211
Cdd:cd03240 154 EENIEESLaEIIEERKSQKNFQLIVITHDEELVDAAD 190
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-202 |
7.36e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 38 IMGPSGSGKSTLLHCLAGIVPPDEGAIHYNGTELSALPesrrsalrRSDFGFVFQFGQLVPELSCVENVALplrlnGVKR 117
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--------KPYCTYIGHNLGLKLEMTVFENLKF-----WSEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 118 KEAEKAAYAWMERLEVEDLAAKRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALDSLNGERVMELLTEAArGTNAAV 197
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKA-NSGGIV 176
|
....*
gi 759535873 198 VLVTH 202
Cdd:PRK13541 177 LLSSH 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-175 |
1.15e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 11 EGLRKSYGATNALDGAEFSIHAGEVVAIMGPSGSGKSTLL-----HCLAGIvPPDEGAIHYN----GTELSAL------- 74
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamHAIDGI-PKNCQILHVEqevvGDDTTALqcvlntd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759535873 75 -------PESRRSALRRSDFGFVFQFGQL-VPELSCVENVALPLRLNGV-KRKE------AEKAAYAWMERLE-VEDLAA 138
Cdd:PLN03073 260 iertqllEEEAQLVAQQRELEFETETGKGkGANKDGVDKDAVSQRLEEIyKRLElidaytAEARAASILAGLSfTPEMQV 339
|
170 180 190
....*....|....*....|....*....|....*..
gi 759535873 139 KRPGEVSGGQGQRVAVARALVTAPRVVFADEPTGALD 175
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
32-55 |
3.35e-03 |
|
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: 37.38 E-value: 3.35e-03
10 20
....*....|....*....|....
gi 759535873 32 AGEVVAIMGPSGSGKSTLLHCLAG 55
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
35-61 |
4.07e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 37.13 E-value: 4.07e-03
10 20
....*....|....*....|....*..
gi 759535873 35 VVAIMGPSGSGKSTLLHCLAGIVPPDE 61
Cdd:COG0572 9 IIGIAGPSGSGKTTFARRLAEQLGADK 35
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
35-55 |
5.29e-03 |
|
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.
Pssm-ID: 206650 Cd Length: 224 Bit Score: 36.92 E-value: 5.29e-03
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
38-53 |
5.31e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 35.97 E-value: 5.31e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
3-51 |
9.18e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 36.91 E-value: 9.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 759535873 3 PSGSLLSAEGLRKsygatNALDGAEFSIHAGEVVAIMGPSGSGKSTLLH 51
Cdd:TIGR00630 609 GNGKFLTLKGARE-----NNLKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| |
