|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-228 |
5.19e-109 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 312.75 E-value: 5.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPsLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR 80
Cdd:COG1136 1 MSP-LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRGRNVGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARA 160
Cdd:COG1136 80 LARLRRRHIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFTRVVELSDGRILSQSE 228
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSDER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-223 |
4.00e-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: 287.46 E-value: 4.00e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGR 87
Cdd:cd03255 3 LKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAG-VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLA-VEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-232 |
4.44e-82 |
|
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: 244.65 E-value: 4.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRGRNVGVVFQFFQLLPTLTVVENIMLPMDfchFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARA 160
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLE---LAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFTRVVELSDGRILSQSEVSVR 232
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATAA 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-223 |
1.16e-80 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 240.72 E-value: 1.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgR 87
Cdd:COG2884 4 FENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFCHFlPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGK-SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMpKRVLELEDGRL 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
3.29e-68 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 210.33 E-value: 3.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 latwrgrnvGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARA 160
Cdd:COG1116 83 ---------GVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 161 LANDPPIIVADEPTGNLDSRT----SDEVIELFAGlavEGKAVAMVTHERD----LSrhfTRVVELSD--GRI 223
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTrerlQDELLRLWQE---TGKTVLFVTHDVDeavfLA---DRVVVLSArpGRI 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
5-222 |
1.30e-64 |
|
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: 199.78 E-value: 1.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPtgqFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATW 84
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RgRNVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRgRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAND 164
Cdd:TIGR02673 78 R-RRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQR-RVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFT-RVVELSDGR 222
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAhRVIILDDGR 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-229 |
2.57e-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: 193.84 E-value: 2.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedrlatwRGR 87
Cdd:cd03293 3 VRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------PGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERD----LSrhfTRVVELS--DGRILSQSEV 229
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDeavfLA---DRVVVLSarPGRIVAEVEV 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-230 |
3.33e-62 |
|
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: 193.95 E-value: 3.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgR 87
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVALPLEI-AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHF-TRVVELSDGRILSQSEVS 230
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-224 |
5.46e-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: 201.67 E-value: 5.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDT-PTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGED 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 80 RLATWRgRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGR-YADNLPADLSGGQQQRAA 156
Cdd:COG1123 336 SLRELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 157 IARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDLS--RHFT-RVVELSDGRIL 224
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISH--DLAvvRYIAdRVAVMYDGRIV 484
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-223 |
4.42e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 191.81 E-value: 4.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAT 83
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 84 WRgRNVGVVFQFFQLLPTLTVVENIM--------LPMDFCHFLPTSKRRgRAMELLEKLSIGRYADNlPAD-LSGGQQQR 154
Cdd:COG3638 78 LR-RRIGMIFQQFNLVPRLSVLTNVLagrlgrtsTWRSLLGLFPPEDRE-RALEALERVGLADKAYQ-RADqLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 155 AAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSR-HFTRVVELSDGRI 223
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARrYADRIIGLRDGRV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-229 |
3.53e-60 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 192.21 E-value: 3.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgR 87
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:COG1135 83 KIGMIFQHFNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHF-TRVVELSDGRILSQSEV 229
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRIcDRVAVLENGRIVEQGPV 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-223 |
2.09e-59 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 186.94 E-value: 2.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEdRLATW 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR-RLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RGRNVGVVFQ--FFQLLPTLTVVENIMLPMdFCHFLPTSKRRGRAMELLEKLSIG---RYADNLPADLSGGQQQRAAIAR 159
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPL-RIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 160 ALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDLS--RHFT-RVVELSDGRI 223
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITH--DLGvvAKIAdRVAVMYAGKI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-223 |
3.10e-59 |
|
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: 186.07 E-value: 3.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtPTGqFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgR 87
Cdd:cd03292 3 FINVTKTY--PNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDfCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALE-VTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDL-SRHFTRVVELSDGRI 223
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-224 |
1.77e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.81 E-value: 1.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfGEDRLATWRgR 87
Cdd:COG1126 4 IENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:COG1126 78 KVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE----RDLSrhfTRVVELSDGRIL 224
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEmgfaREVA---DRVVFMDGGRIV 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-223 |
2.69e-58 |
|
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: 183.50 E-value: 2.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDrLATWRgR 87
Cdd:cd03262 3 IKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN-INELR-Q 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-226 |
7.52e-58 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 182.92 E-value: 7.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgeDRLATWRgR 87
Cdd:COG1122 3 LENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQF--FQLLpTLTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAND 164
Cdd:COG1122 76 KVGLVFQNpdDQLF-APTVEEDVAFgPENLG--LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDL-SRHFTRVVELSDGRILSQ 226
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLvAELADRVIVLDDGRIVAD 215
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
5-223 |
2.67e-57 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 181.07 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATW 84
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RGRNVGVVFQFFQLLPTLTVVENIMLPMDFCHFlPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAND 164
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGV-AKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-218 |
6.20e-57 |
|
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: 179.73 E-value: 6.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGR 87
Cdd:TIGR03608 1 LKNISKKF----GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKY-KKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVEL 218
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-224 |
1.37e-56 |
|
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: 180.18 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRgRNVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARA 160
Cdd:COG1127 77 LYELR-RRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHF-TRVVELSDGRIL 224
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIaDRVAVLADGKII 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-222 |
2.20e-56 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 178.43 E-value: 2.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgR 87
Cdd:cd03225 2 LKNLSFSY--PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFF--QLLpTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:cd03225 76 KVGLVFQNPddQFF-GPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERD-LSRHFTRVVELSDGR 222
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-224 |
9.79e-55 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 174.24 E-value: 9.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedrLATWRgR 87
Cdd:cd03259 3 LKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPER-R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03259 73 NIGMVFQDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERD----LSrhfTRVVELSDGRIL 224
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEealaLA---DRIAVMNEGRIV 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-227 |
1.07e-54 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 185.31 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAT 83
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 84 WRGRNVGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAG-LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQS 227
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNP 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
1.44e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 178.37 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIekfgeDR 80
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRgRNVGVVFQFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARA 160
Cdd:COG3842 72 LPPEK-RNVGMVFQDYALFPHLTVAENVAFGLRM-RGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEV-IELFAGLAVEGKAVAMVTHERD----LSrhfTRVVELSDGRIL 224
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMrEELRRLQRELGITFIYVTHDQEealaLA---DRIAVMNDGRIE 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-223 |
2.39e-54 |
|
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: 174.29 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGR 87
Cdd:cd03256 3 VENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 nVGVVFQFFQLLPTLTVVENIMLPM-DFCHF------LPTSKRRGRAMELLEKLSIGRYAdNLPAD-LSGGQQQRAAIAR 159
Cdd:cd03256 80 -IGMIFQQFNLIERLSVLENVLSGRlGRRSTwrslfgLFPKEEKQRALAALERVGLLDKA-YQRADqLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 160 ALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSR-HFTRVVELSDGRI 223
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAReYADRIVGLKDGRI 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-226 |
5.73e-54 |
|
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: 173.07 E-value: 5.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgR 87
Cdd:cd03261 3 LRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMdFCHF-LPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPP 166
Cdd:cd03261 78 RMGMLFQSGALFDSLTVFENVAFPL-REHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 167 IIVADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHerDLSRHFT---RVVELSDGRILSQ 226
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTH--DLDTAFAiadRIAVLYDGKIVAE 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-231 |
1.01e-53 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 172.69 E-value: 1.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 2 SPSLLClRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRL 81
Cdd:PRK11629 3 KILLQC-DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 82 ATWRGRNVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRgRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARAL 161
Cdd:PRK11629 82 AELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINS-RALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGLAV-EGKAVAMVTHERDLSRHFTRVVELSDGRIlsQSEVSV 231
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLEMRDGRL--TAELSL 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-226 |
1.11e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.56 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedRLATWRgR 87
Cdd:COG1131 3 VRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLpmdFCHF--LPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:COG1131 74 RIGYVPQEPALYPDLTVRENLRF---FARLygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE-RDLSRHFTRVVELSDGRILSQ 226
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIVAD 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
2.35e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.50 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedr 80
Cdd:COG1121 2 MMMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 latwRGRNVGVVFQFFQLLPT--LTVVENIMLPMDFCHFL---PTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRA 155
Cdd:COG1121 73 ----ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERD-LSRHFTRVVELSDGRI 223
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGaVREYFDRVLLLNRGLV 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-223 |
2.78e-52 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 168.80 E-value: 2.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAT 83
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 84 WRGRNVGVVFQFFQLLPTLTVVENIMLPMdFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPA-LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-222 |
8.67e-52 |
|
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: 165.82 E-value: 8.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwRGR 87
Cdd:cd03229 3 LKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--LRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPmdfchflptskrrgramelleklsigryadnlpadLSGGQQQRAAIARALANDPPI 167
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGR 222
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-230 |
4.29e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 4.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNI---EKFGEDRLATW 84
Cdd:COG4161 5 LKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RgRNVGVVFQFFQLLPTLTVVEN-IMLPmdfCHFLPTSKR--RGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARAL 161
Cdd:COG4161 81 R-QKVGMVFQQYNLWPHLTVMENlIEAP---CKVLGLSKEqaREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRILSQSEVS 230
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIEQGDAS 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-230 |
8.03e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 165.74 E-value: 8.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgR 87
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRILSQSEVS 230
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICdRVAVIDAGRLVEQGTVS 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-223 |
3.17e-49 |
|
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: 161.31 E-value: 3.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 11 VSKSYdtPTGQfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgRNVG 90
Cdd:TIGR02315 7 LSKVY--PNGK-QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR-RRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 91 VVFQFFQLLPTLTVVENIMLP----MDF---CHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:TIGR02315 83 MIFQHYNLIERLTVLENVLHGrlgyKPTwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYaDRIVGLKAGEI 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-220 |
1.81e-48 |
|
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: 161.76 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTP---TRGSVAAVGKNIEKFGEDRL 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 82 ATWRGRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI---GRYADNLPADLSGGQQQRAA 156
Cdd:COG0444 81 RKIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 157 IARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDLS--RHFT---------RVVELSD 220
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITH--DLGvvAEIAdrvavmyagRIVEEGP 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-222 |
6.61e-48 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 155.62 E-value: 6.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrLATWR 85
Cdd:cd03228 1 IEFKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTlTVVENImlpmdfchflptskrrgramelleklsigryadnlpadLSGGQQQRAAIARALANDP 165
Cdd:cd03228 76 -KNIAYVPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGR 222
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-230 |
1.29e-47 |
|
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: 157.27 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedRLATW 84
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR----RRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RGRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEkLSiGRYADNLPADLSGGQQQRAAIARALA 162
Cdd:COG1124 77 FRRRVQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVG-LP-PSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 163 NDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHF-TRVVELSDGRILSQSEVS 230
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVA 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-224 |
3.79e-47 |
|
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: 156.65 E-value: 3.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 19 TGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGRNVGVVFQFFQL 98
Cdd:cd03294 34 TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 LPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:cd03294 114 LPHRTVLENVAFGLEVQG-VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 179 S--RT--SDEVIELFAGLaveGKAVAMVTHERDLS-RHFTRVVELSDGRIL 224
Cdd:cd03294 193 PliRRemQDELLRLQAEL---QKTIVFITHDLDEAlRLGDRIAIMKDGRLV 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-226 |
7.96e-47 |
|
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: 155.59 E-value: 7.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtw 84
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 rgRNVGVVFQFFQLLPTLTVVENIML---PMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARAL 161
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDL-SRHFTRVVELSDGRILSQ 226
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQ 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
8.52e-47 |
|
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: 161.61 E-value: 8.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPsLLCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPT---RGSVAAVGKNIEKFG 77
Cdd:COG1123 1 MTP-LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 78 EDrlatWRGRNVGVVFQFF--QLLPtLTVVENIMLPMDfCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRA 155
Cdd:COG1123 78 EA----LRGRRIGMVFQDPmtQLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHE-RDLSRHFTRVVELSDGRILSQ 226
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDlGVVAEIADRVVVMDDGRIVED 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-223 |
8.92e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 155.34 E-value: 8.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 2 SPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIE----KFG 77
Cdd:COG4598 5 APPALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdRDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 78 EDRLATWRG-----RNVGVVFQFFQLLPTLTVVENIML-PMdfcHFLPTSKR--RGRAMELLEKLSIGRYADNLPADLSG 149
Cdd:COG4598 81 ELVPADRRQlqrirTRLGMVFQSFNLWSHMTVLENVIEaPV---HVLGRPKAeaIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE----RDLSRHftrVVELSDGRI 223
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEmgfaRDVSSH---VVFLHQGRI 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-224 |
1.60e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 157.54 E-value: 1.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIekfgeDRLATWR 85
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:COG3839 75 -RNIAMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 166 PIIVADEPTGNLD--SRTS--DEVIELFAGLaveGKAVAMVTHERD----LSrhfTRVVELSDGRIL 224
Cdd:COG3839 153 KVFLLDEPLSNLDakLRVEmrAEIKRLHRRL---GTTTIYVTHDQVeamtLA---DRIAVMNDGRIQ 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-226 |
2.69e-46 |
|
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: 154.92 E-value: 2.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSY--DTPTgQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWR 85
Cdd:TIGR04521 3 LKNVSYIYqpGTPF-EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQF--FQLLPTlTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGR-YADNLPADLSGGQQQRAAIARAL 161
Cdd:TIGR04521 82 -KKVGLVFQFpeHQLFEE-TVYKDIAFgPKNLG--LSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHE-RDLSRHFTRVVELSDGRILSQ 226
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSmEDVAEYADRVIVMHKGKIVLD 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-224 |
3.45e-46 |
|
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: 153.36 E-value: 3.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATwRGr 87
Cdd:cd03219 3 VRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-LG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 nVGVVFQFFQLLPTLTVVENIMLPM-----DFCHFLPTSKR----RGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:cd03219 77 -IGRTFQIPRLFPELTVLENVMVAAqartgSGLLLARARREereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRIL 224
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVI 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-226 |
4.50e-46 |
|
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: 153.23 E-value: 4.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgR 87
Cdd:cd03295 3 FENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFCHFlPTSKRRGRAMELLE--KLSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIALVPKLLKW-PKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLS-RHFTRVVELSDGRILSQ 226
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQV 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-223 |
4.68e-46 |
|
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: 151.01 E-value: 4.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLatwrgR 87
Cdd:cd03230 3 VRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENImlpmdfchflptskrrgramelleklsigryadnlpaDLSGGQQQRAAIARALANDPPI 167
Cdd:cd03230 74 RIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH-ERDLSRHFTRVVELSDGRI 223
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHiLEEAERLCDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-223 |
4.87e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 156.08 E-value: 4.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSpslLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaavgknieKFGEDR 80
Cdd:COG1118 1 MS---IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI--------VLNGRD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATW---RGRNVGVVFQFFQLLPTLTVVENIM--LPMdfchfLPTSK--RRGRAMELLEKLSIGRYADNLPADLSGGQQQ 153
Cdd:COG1118 66 LFTNlppRERRVGFVFQHYALFPHMTVAENIAfgLRV-----RPPSKaeIRARVEELLELVQLEGLADRYPSQLSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 154 RAAIARALANDPPIIVADEPTGNLDSRTSDEV-IELFAGLAVEGKAVAMVTHERD----LSRhftRVVELSDGRI 223
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAKVRKELrRWLRRLHDELGGTTVFVTHDQEealeLAD---RVVVMNQGRI 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-204 |
8.00e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 153.09 E-value: 8.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlat 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 84 wrgrnvGVVFQFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTH 204
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITH 193
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-223 |
1.34e-45 |
|
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: 151.62 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatwrgR 87
Cdd:cd03300 3 LENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03300 73 PVNTVFQNYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 168 IVADEPTGNLDSRTSDEV-IELFAGLAVEGKAVAMVTHerDLSRHFT---RVVELSDGRI 223
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMqLELKRLQKELGITFVFVTH--DQEEALTmsdRIAVMNKGKI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-218 |
2.72e-45 |
|
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: 150.38 E-value: 2.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrlatwrgRNVGVVFQFFQLL 99
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---------KRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PT--LTVVENIMLPMD-FCHFL--PTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPT 174
Cdd:cd03235 81 RDfpISVRDVVLMGLYgHKGLFrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1084922189 175 GNLDSRTSDEVIELFAGLAVEGKAVAMVTHERD-LSRHFTRVVEL 218
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDRVLLL 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-230 |
5.08e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 150.55 E-value: 5.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNI---EKFGEDRLATW 84
Cdd:PRK11124 5 LNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RgRNVGVVFQFFQLLPTLTVVEN-IMLPmdfCHFLPTSKR--RGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARAL 161
Cdd:PRK11124 81 R-RNVGMVFQQYNLWPHLTVQQNlIEAP---CRVLGLSKDqaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRILSQSEVS 230
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQGDAS 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-223 |
1.32e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.43 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDTPTGqflaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRLATWR 85
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTlTVVENIMLPMDFCHFLPTskrRGRAMELLEKLSIG-RYADNLPADLSGGQQQRAAIARALAND 164
Cdd:COG4619 74 -RQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFD---RERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERD-LSRHFTRVVELSDGRI 223
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-223 |
2.08e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 148.70 E-value: 2.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgeDRLATWRG- 86
Cdd:PRK09493 4 FKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN----DPKVDERLi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 87 -RNVGVVFQFFQLLPTLTVVENIMlpmdfchFLPTSKR-------RGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:PRK09493 76 rQEAGMVFQQFYLFPHLTALENVM-------FGPLRVRgaskeeaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRI 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-222 |
2.47e-44 |
|
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: 147.63 E-value: 2.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatw 84
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 rGRNVGVVFQFFQLLPTLTVVENIMLpmdFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAND 164
Cdd:COG4133 74 -RRRLAYLGHADGLKPELTVRENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHErDLSRHFTRVVELSDGR 222
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ-PLELAAARVLDLGDFK 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-174 |
1.68e-43 |
|
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: 143.56 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgeDRLATWRGRNVGVVFQFFQLLPTLTV 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT----DDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 105 VENIMLPMDFChFLPTSKRRGRAMELLEKLSIG----RYADNLPADLSGGQQQRAAIARALANDPPIIVADEPT 174
Cdd:pfam00005 77 RENLRLGLLLK-GLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-224 |
3.24e-43 |
|
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: 146.34 E-value: 3.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 2 SPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRL 81
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 82 AtwrgrNVGVV--FQFFQLLPTLTVVENIMLPMDFCH---------FLPTSKR-----RGRAMELLEKLSIGRYADNLPA 145
Cdd:COG0411 77 A-----RLGIArtFQNPRLFPELTVLENVLVAAHARLgrgllaallRLPRARReereaRERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 146 DLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHERDL-SRHFTRVVELSDGRI 223
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLvMGLADRIVVLDFGRV 231
|
.
gi 1084922189 224 L 224
Cdd:COG0411 232 I 232
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-224 |
3.60e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 147.54 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTL---VNVMtgIDtPTRGSVAAVGKNIEKFGEDRLatw 84
Cdd:COG1125 4 FENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTlrmINRL--IE-PTSGRILIDGEDIRDLDPVEL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RgRNVGVVFQFFQLLPTLTVVENIML-PMdfchfL---PTSKRRGRAMELLEK--LSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:COG1125 75 R-RRIGYVIQQIGLFPHMTVAENIATvPR-----LlgwDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 159 RALANDPPIIVADEPTGNLD--SRTS--DEVIELFAGLaveGKAVAMVTHerDLSRHF---TRVVELSDGRIL 224
Cdd:COG1125 149 RALAADPPILLMDEPFGALDpiTREQlqDELLRLQREL---GKTIVFVTH--DIDEALklgDRIAVMREGRIV 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-221 |
4.01e-42 |
|
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: 142.60 E-value: 4.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLatwrgrnvgVVFQFFQLLPTLTV 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 105 VENIMLPMD-FCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSD 183
Cdd:TIGR01184 72 RENIALAVDrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1084922189 184 EVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDG 221
Cdd:TIGR01184 152 NLQEELMQIWEEhRVTVLMVTHDVDEALLLSdRVVMLTNG 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-226 |
1.06e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 148.76 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwr 85
Cdd:COG4987 334 LELEDVSFRY--PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTlTVVENIMLpmdfchflptskrrGR-------AMELLEKLSIGRYADNLP-----------ADL 147
Cdd:COG4987 409 -RRIAVVPQRPHLFDT-TLRENLRL--------------ARpdatdeeLWAALERVGLGDWLAALPdgldtwlgeggRRL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 148 SGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-223 |
1.53e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 142.03 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNI------- 73
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 74 ---EKFGEDRLATWRGRnVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI-GRYADNLPADLSG 149
Cdd:PRK10619 77 gqlKVADKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVsSHVIFLHQGKI 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-223 |
7.32e-41 |
|
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: 148.06 E-value: 7.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrLATWR 85
Cdd:COG2274 474 IELENVSFRY--PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTlTVVENIML-----PMDfchflptskrrgRAMELLEKLSIGRYADNLP-----------ADLSG 149
Cdd:COG2274 549 -RQIGVVLQDVFLFSG-TIRENITLgdpdaTDE------------EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSG 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-226 |
3.05e-40 |
|
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: 136.03 E-value: 3.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgR 87
Cdd:cd03214 2 VENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQffqllptltvvenimlpmdfchflptskrrgrameLLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03214 74 KIAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDL-SRHFTRVVELSDGRILSQ 226
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLaARYADRVILLKDGRIVAQ 179
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
3.52e-40 |
|
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: 144.90 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 2 SPSLLCLRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRL 81
Cdd:COG4988 333 GPPSIELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL---DP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 82 ATWRgRNVGVVFQFFQLLPTlTVVENIMLpmdfchflptskrrGRA-------MELLEKLSIGRYADNLPAD-------- 146
Cdd:COG4988 407 ASWR-RQIAWVPQNPYLFAG-TIRENLRL--------------GRPdasdeelEAALEAAGLDEFVAALPDGldtplgeg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 147 ---LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:COG4988 471 grgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDGRI 549
|
...
gi 1084922189 224 LSQ 226
Cdd:COG4988 550 VEQ 552
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-222 |
4.96e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.06 E-value: 4.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 7 CLRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRLATWRg 86
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL---PLEELR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 87 RNVGVVFQffqllptltvvenimlpmdfchflptskrrgramelleklsigryadnlpadLSGGQQQRAAIARALANDPP 166
Cdd:cd00267 73 RRIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 167 IIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE-RDLSRHFTRVVELSDGR 222
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDGK 157
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-223 |
6.81e-40 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 136.93 E-value: 6.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 10 HVSKSYdtpTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgRNV 89
Cdd:PRK10908 6 HVSKAY---LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 90 GVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRgRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIV 169
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRR-RVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 170 ADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDL-SRHFTRVVELSDGRI 223
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLiSRRSYRMLTLSDGHL 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-223 |
8.65e-40 |
|
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: 137.09 E-value: 8.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedrlATWRGRN 88
Cdd:cd03296 6 RNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD------VPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQFFQLLPTLTVVENIMLPMDFCH---FLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVKPrseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRI 223
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVAdRVVVMNKGRI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-223 |
8.86e-40 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 135.85 E-value: 8.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 10 HVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaavgknieKFGEDRLATW-RGRN 88
Cdd:cd03226 4 NISFSYK---KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI--------LLNGKPIKAKeRRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVV-----FQFFqllpTLTVVENIMLPMDfchflPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:cd03226 73 IGYVmqdvdYQLF----TDSVREELLLGLK-----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERD-LSRHFTRVVELSDGRI 223
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAI 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
25-228 |
7.89e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.88 E-value: 7.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAaVGkNIEKFGEDRLATWRG------RNVGVVFQFFQL 98
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIR-VG-DITIDTARSLSQQKGlirqlrQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 LPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:PRK11264 97 FPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 179 SRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFT-RVVELSDGRILSQSE 228
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGP 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-223 |
9.13e-39 |
|
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: 133.53 E-value: 9.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAavgkniekFGEDRLATWRG- 86
Cdd:cd03301 3 LENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIY--------IGGRDVTDLPPk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 87 -RNVGVVFQFFQLLPTLTVVENIMLPMDFCHFlPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:cd03301 71 dRDIAMVFQNYALYPHMTVYDNIAFGLKLRKV-PKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 166 PIIVADEPTGNLDSR----TSDEVIELFAGLaveGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:cd03301 150 KVFLMDEPLSNLDAKlrvqMRAELKRLQQRL---GTTTIYVTHDQVEAMTMaDRIAVMNDGQI 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-204 |
2.18e-38 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 139.01 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIeKFGEDR 80
Cdd:COG3845 1 MMPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LAtwRGRNVGVVFQFFQLLPTLTVVENIMLPMD--FCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:COG3845 76 DA--IALGIGMVHQHFMLVPNLTVAENIVLGLEptKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1084922189 159 RALANDPPIIVADEPTGNLdsrTSDEVIELFA---GLAVEGKAVAMVTH 204
Cdd:COG3845 154 KALYRGARILILDEPTAVL---TPQEADELFEilrRLAAEGKSIIFITH 199
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-226 |
2.38e-38 |
|
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: 134.09 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGknIEKFGEDRLATWRgR 87
Cdd:TIGR04520 3 VENVSFSY--PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQF--FQLLPTlTV-------VENIMlpmdfchfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:TIGR04520 78 KVGMVFQNpdNQFVGA-TVeddvafgLENLG--------VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-204 |
8.36e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.46 E-value: 8.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 2 SPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkFGEDRL 81
Cdd:COG1129 1 AEPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 82 ATWRGrnVGVVFQFFQLLPTLTVVENIML---PMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:COG1129 76 AQAAG--IAIIHQELNLVPNLSVAENIFLgrePRRG-GLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1084922189 159 RALANDPPIIVADEPTGNLdsrTSDEVIELFA---GLAVEGKAVAMVTH 204
Cdd:COG1129 153 RALSRDARVLILDEPTASL---TEREVERLFRiirRLKAQGVAIIYISH 198
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-207 |
1.06e-37 |
|
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: 134.39 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgedRLATWR 85
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDIT-----RLPPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTLTVVENIMLPMdFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:TIGR03265 76 -RDYGIVFQSYALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084922189 166 PIIVADEPTGNLDSRTSD----EVIELFAGLAVegkAVAMVTHERD 207
Cdd:TIGR03265 154 GLLLLDEPLSALDARVREhlrtEIRQLQRRLGV---TTIMVTHDQE 196
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-220 |
3.91e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.55 E-value: 3.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTGQFL-------ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNI 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 74 EKFGEDRLATWRgRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEK--LS---IGRYadnlPAD 146
Cdd:COG4608 83 TGLSGRELRPLR-RRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELvgLRpehADRY----PHE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDLS--RHFT---------R 214
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISH--DLSvvRHISdrvavmylgK 235
|
....*.
gi 1084922189 215 VVELSD 220
Cdd:COG4608 236 IVEIAP 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-230 |
6.13e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.58 E-value: 6.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSYdtPTGQFLA-------LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKF 76
Cdd:PRK10419 2 TLLNVSGLSHHY--AHGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 77 GEDRLATWRgRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIG-RYADNLPADLSGGQQQ 153
Cdd:PRK10419 80 NRAQRKAFR-RDIQMVFQdsISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 154 RAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHF-TRVVELSDGRILSQSEVS 230
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVG 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-224 |
6.98e-37 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 129.22 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI-----DTPTRGSVAAVGKNIEKFGEDRLa 82
Cdd:cd03260 3 LRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 tWRGRNVGVVFQFFQLLPtLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRY-ADNLPA-DLSGGQQQRAAIARA 160
Cdd:cd03260 78 -ELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEvKDRLHAlGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEgKAVAMVTHerDL---SRHFTRVVELSDGRIL 224
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTH--NMqqaARVADRTAFLLNGRLV 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-230 |
3.51e-36 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 128.38 E-value: 3.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSYDT-----PTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGE 78
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 79 DRLATWRgRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI-GRYADNLPADLSGGQQQRA 155
Cdd:TIGR02769 81 KQRRAFR-RDVQLVFQdsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRILSQSEVS 230
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCqRVAVMDKGQIVEECDVA 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-226 |
4.98e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 133.37 E-value: 4.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRLATWR 85
Cdd:COG1132 340 IEFENVSFSYP---GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL---TLESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLpTLTVVENIMLpmdfchflptskrrGRA-------MELLEKLSIGRYADNLP-----------ADL 147
Cdd:COG1132 414 -RQIGVVPQDTFLF-SGTIRENIRY--------------GRPdatdeevEEAAKAAQAHEFIEALPdgydtvvgergVNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 148 SGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHeRdLS--RHFTRVVELSDGRILS 225
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAH-R-LStiRNADRILVLDDGRIVE 554
|
.
gi 1084922189 226 Q 226
Cdd:COG1132 555 Q 555
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-223 |
5.84e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.45 E-value: 5.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 latwrgRNVGVVFQFFQLLPTLTVVENIM--LPMDFChflPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:PRK09452 86 ------RHVNTVFQSYALFPHMTVFENVAfgLRMQKT---PAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEV-IELFAGLAVEGKAVAMVTH--ERDLSRHfTRVVELSDGRI 223
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMqNELKALQRKLGITFVFVTHdqEEALTMS-DRIVVMRDGRI 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-223 |
6.51e-36 |
|
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: 126.68 E-value: 6.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatwrgRNVGVVFQFFQLLPTLTV 104
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK------RDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 105 VENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDE 184
Cdd:cd03299 89 YKNIAYGLKK-RKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1084922189 185 VIELFAGLAVE-GKAVAMVTHerDLSRHFT---RVVELSDGRI 223
Cdd:cd03299 168 LREELKKIRKEfGVTVLHVTH--DFEEAWAladKVAIMLNGKL 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-223 |
1.31e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.05 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 10 HVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgedRLATwRGRNV 89
Cdd:PRK10851 7 NIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-----RLHA-RDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 90 GVVFQFFQLLPTLTVVENIMLPMDFchfLPTSKR------RGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTV---LPRRERpnaaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAM-VTHERDLSRHFT-RVVELSDGRI 223
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVfVTHDQEEAMEVAdRVVVMSQGNI 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-224 |
1.93e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 127.51 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYD--TPTgQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKN---------IEKF 76
Cdd:PRK13651 5 VKNIVKIFNkkLPT-ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkeKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 77 GED---RLATWRG--------RNVGVVFQF--FQLLPTlTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGR-YAD 141
Cdd:PRK13651 84 LEKlviQKTRFKKikkikeirRRVGVVFQFaeYQLFEQ-TIEKDIIFgPVSMG--VSKEEAKKRAAKYIELVGLDEsYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 142 NLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFT-RVVELSD 220
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTkRTIFFKD 240
|
....
gi 1084922189 221 GRIL 224
Cdd:PRK13651 241 GKII 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-230 |
2.52e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.25 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDTPTGQFlaltdiDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatwr 85
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTLTVVENIMLPMDfchflP----TSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARAL 161
Cdd:COG3840 71 -RPVSMLFQENNLFPHLTVAQNIGLGLR-----PglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRILSQSEVS 230
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIAdRVLLVADGRIAADGPTA 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-224 |
2.58e-35 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 124.92 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgeDRLAtwR 85
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT---DRKA--A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GRNVGVVFQFFQLLPTLTVVENIMLpmdFCHF--LPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRF---YARLkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLaVEGKAVAMVTHERDLSRHF-TRVVELSDGRIL 224
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALcDRIAIMSDGKLR 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-223 |
8.61e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 124.40 E-value: 8.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGED-RLatw 84
Cdd:PRK11247 13 LLLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDtRL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 rgrnvgvVFQFFQLLPTLTVVENIMLPMdfchflpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAND 164
Cdd:PRK11247 86 -------MFQDARLLPWKKVIDNVGLGL-------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDLSRHFT---RVVELSDGRI 223
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTH--DVSEAVAmadRVLLIEEGKI 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-226 |
4.48e-34 |
|
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: 122.50 E-value: 4.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 3 PSLLCLRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVgkniekFGEDR-- 80
Cdd:COG1119 1 DPLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRL------FGERRgg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 --LATWRgRNVGVVFQFFQL-LPTLTVVEN---------IMLPMDfchflPTSKRRGRAMELLEKLSIGRYADNLPADLS 148
Cdd:COG1119 71 edVWELR-KRIGLVSPALQLrFPRDETVLDvvlsgffdsIGLYRE-----PTDEQRERARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 149 GGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEG-KAVAMVTH-ERDLSRHFTRVVELSDGRILSQ 226
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhVEEIPPGITHVLLLKDGRVVAA 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-223 |
7.38e-34 |
|
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: 119.63 E-value: 7.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 14 SYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLatwrGRNVGVVF 93
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL----GDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 94 QFFQLLPTlTVVENImlpmdfchflptskrrgramelleklsigryadnlpadLSGGQQQRAAIARALANDPPIIVADEP 173
Cdd:cd03246 83 QDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1084922189 174 TGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
29-227 |
8.56e-34 |
|
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: 120.74 E-value: 8.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 29 DLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgedRLATWRgRNVGVVFQFFQLLPTLTVVENI 108
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT-----GLAPYQ-RPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 109 MLPMDFCHFLpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIEL 188
Cdd:TIGR01277 92 GLGLHPGLKL-NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1084922189 189 FAGLAVEGK-AVAMVTHE-RDLSRHFTRVVELSDGRILSQS 227
Cdd:TIGR01277 171 VKQLCSERQrTLLMVTHHlSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-226 |
1.03e-33 |
|
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: 120.29 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatwrgRNVGVVFQFFQLLPTLTVVE 106
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 107 NIMLPMDFCHFLpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVI 186
Cdd:cd03298 90 NVGLGLSPGLKL-TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1084922189 187 ELFAGLAVE-GKAVAMVTHERDLSRH-FTRVVELSDGRILSQ 226
Cdd:cd03298 169 DLVLDLHAEtKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQ 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
2.29e-33 |
|
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: 125.57 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKS----TLVNVMTGIDTPTRGSVAAVGKNIEKF 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 77 GEDRLATWRGRNVGVVFQ--FFQLLPTLTVVENIMLPMdFCHF-LPTSKRRGRAMELLEKLSI-------GRYadnlPAD 146
Cdd:COG4172 82 SERELRRIRGNRIAMIFQepMTSLNPLHTIGKQIAEVL-RLHRgLSGAAARARALELLERVGIpdperrlDAY----PHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHerDLS--RHFT-RVVELSDGR 222
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITH--DLGvvRRFAdRVAVMRQGE 234
|
....*..
gi 1084922189 223 ILSQSEV 229
Cdd:COG4172 235 IVEQGPT 241
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-205 |
2.66e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.57 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYD-TPtgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlat 83
Cdd:PRK11248 1 MLQISHLYADYGgKP-----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 84 wrgrnvGVVFQFFQLLPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:PRK11248 73 ------GVVFQNEGLLPWRNVQDNVAFGLQLAG-VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHE 205
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHD 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-223 |
3.26e-33 |
|
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: 125.18 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 3 PSLLCLRHVSKSYDTPTG-------QFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIdTPTRGSVAAVGKNIEK 75
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 76 FGEDRLATWRgRNVGVVFQ--FFQLLPTLTVVENIMLPMDFcHFLPTSK--RRGRAMELLEKL-----SIGRYadnlPAD 146
Cdd:COG4172 352 LSRRALRPLR-RRMQVVFQdpFGSLSPRMTVGQIIAEGLRV-HGPGLSAaeRRARVAEALEEVgldpaARHRY----PHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDLS--RHFT-RVVELSDGR 222
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISH--DLAvvRALAhRVMVMKDGK 503
|
.
gi 1084922189 223 I 223
Cdd:COG4172 504 V 504
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-227 |
5.40e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.65 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 11 VSKSYD--TPTgQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR-LATWRGR 87
Cdd:PRK13646 8 VSYTYQkgTPY-EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 nVGVVFQF--FQLLPTLTVVENIMLPMDFChfLPTSKRRGRAMELLEKLSIGRYADNL-PADLSGGQQQRAAIARALAND 164
Cdd:PRK13646 87 -IGMVFQFpeSQLFEDTVEREIIFGPKNFK--MNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHE-RDLSRHFTRVVELSDGRILSQS 227
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDmNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-227 |
5.40e-33 |
|
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: 118.55 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRaGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVG-------KNIEkfgedrLATWRgRNVGVVFQFFQLL 99
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKIN------LPPQQ-RKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PTLTVVENIMLPMDFCHflpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:cd03297 88 PHLNVRENLAFGLKRKR---NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 180 RTSDEVI-ELFAGLAVEGKAVAMVTHerDLSRHFT---RVVELSDGRILSQS 227
Cdd:cd03297 165 ALRLQLLpELKQIKKNLNIPVIFVTH--DLSEAEYladRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-226 |
9.32e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.12 E-value: 9.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYD--TPTGQfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVA------AVGKNiekfgED 79
Cdd:PRK13634 5 FQKVEHRYQykTPFER-RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigerviTAGKK-----NK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 80 RLATWRgRNVGVVFQF--FQLLPTlTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGR-YADNLPADLSGGQQQRA 155
Cdd:PRK13634 79 KLKPLR-KKVGIVFQFpeHQLFEE-TVEKDICFgPMNFG--VSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHE-RDLSRHFTRVVELSDGRILSQ 226
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSmEDAARYADQIVVMHKGTVFLQ 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-223 |
1.27e-32 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.99 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkFGEDRLATWR 85
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-FASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GrnVGVVFQffqllptltvvenimlpmdfchflptskrrgramelleklsigryadnlpadLSGGQQQRAAIARALANDP 165
Cdd:cd03216 76 G--IAMVYQ----------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH-ERDLSRHFTRVVELSDGRI 223
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHrLDEVFEIADRVTVLRDGRV 160
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-204 |
2.24e-32 |
|
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: 122.85 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwr 85
Cdd:TIGR02868 335 LELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTlTVVENIMLPmdfchflptskrRGRA-----MELLEKLSIGRYADNLP-----------ADLSG 149
Cdd:TIGR02868 409 -RRVSVCAQDAHLFDT-TVRENLRLA------------RPDAtdeelWAALERVGLADWLRALPdgldtvlgeggARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIE-LFAGLavEGKAVAMVTH 204
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEdLLAAL--SGRTVVLITH 528
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-224 |
4.20e-32 |
|
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: 119.14 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 40 IVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatwrgRNVGVVFQFFQLLPTLTVVENIMLPMDFcHFLP 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL------RHINMVFQSYALFPHMTVEENVAFGLKM-RKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 120 TSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEV-IELFAGLAVEGKA 198
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGIT 153
|
170 180
....*....|....*....|....*....
gi 1084922189 199 VAMVTHerDLSRHFT---RVVELSDGRIL 224
Cdd:TIGR01187 154 FVFVTH--DQEEAMTmsdRIAIMRKGKIA 180
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-224 |
2.03e-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: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 23 LALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTP---TRGSVAAVGKNIEKfgedrlATWRgRNVGVVFQFFQLL 99
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP------DQFQ-KCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PTLTVVENI----MLPMDFChfLPTSKRRGR-AMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPT 174
Cdd:cd03234 94 PGLTVRETLtytaILRLPRK--SSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 175 GNLDSRTSDEVIELFAGLAVEGKAVAMVTHE--RDLSRHFTRVVELSDGRIL 224
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEIV 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-226 |
2.42e-31 |
|
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: 117.89 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVG-------KNIekfgedRLATWRgRNVGVVFQFFQLL 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGI------FLPPHR-RRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PTLTVVENIMLPMDFChflPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:COG4148 90 PHLSVRGNLLYGRKRA---PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1084922189 180 RTSDEVIELFAGLAVEGK-AVAMVTHERD-LSRHFTRVVELSDGRILSQ 226
Cdd:COG4148 167 ARKAEILPYLERLRDELDiPILYVSHSLDeVARLADHVVLLEQGRVVAS 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-224 |
3.21e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.08 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIE-KFGEDRLATWRgRNVGVVFQF--FQLLPT 101
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKKLR-KKVSLVFQFpeAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 lTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGR-YADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:PRK13641 102 -TVLKDVEFgPKNFG--FSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084922189 180 RTSDEVIELFAGLAVEGKAVAMVTHER-DLSRHFTRVVELSDGRIL 224
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLI 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-207 |
8.33e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.86 E-value: 8.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDtptGQFlALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgedRLATW 84
Cdd:PRK11607 19 LLEIRNLTKSFD---GQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RgRNVGVVFQFFQLLPTLTVVENIM--LPMDFchfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALA 162
Cdd:PRK11607 90 Q-RPINMMFQSYALFPHMTVEQNIAfgLKQDK---LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1084922189 163 NDPPIIVADEPTGNLDSRTSD----EVIELfagLAVEGKAVAMVTHERD 207
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDrmqlEVVDI---LERVGVTCVMVTHDQE 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
24-223 |
1.10e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfGEDRLATWRGRnVGVVFQF--FQLLPT 101
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKK-VGLVFQYpeYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 lTVVENIMlpmdfchFLPT---------SKRRGRAMELLeKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADE 172
Cdd:PRK13637 100 -TIEKDIA-------FGPInlglseeeiENRVKRAMNIV-GLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 173 PTGNLDSRTSDEVIELFAGLAVEGK-AVAMVTHE-RDLSRHFTRVVELSDGRI 223
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSmEDVAKLADRIIVMNKGKC 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-220 |
1.98e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 114.68 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTGQFL------ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIE 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 75 KFGEDRLATWRgRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI-----GRYadnlPADL 147
Cdd:PRK11308 81 KADPEAQKLLR-QKIQIVFQnpYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrpehyDRY----PHMF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 148 SGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDLS--RH---------FTRV 215
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISH--DLSvvEHiadevmvmyLGRC 233
|
....*
gi 1084922189 216 VELSD 220
Cdd:PRK11308 234 VEKGT 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-226 |
2.84e-30 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 111.93 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRLATWRgRN 88
Cdd:cd03254 6 ENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI---SRKSLR-SM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQFFQLLPTlTVVENIMLpmdfchFLPTSKRRgRAMELLEKLSIGRYADNLP-----------ADLSGGQQQRAAI 157
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRL------GRPNATDE-EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 158 ARALANDPPIIVADEPTGNLDSRTsDEVIElfAGLAV--EGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTET-EKLIQ--EALEKlmKGRTSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
8-223 |
3.43e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.53 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgR 87
Cdd:cd03245 5 FRNVSFSY--PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTlTVVENIMLpmdfchFLPTSKRRgRAMELLEKLSIGRYADNLP-----------ADLSGGQQQRAA 156
Cdd:cd03245 79 NIGYVPQDVTLFYG-TLRDNITL------GAPLADDE-RILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 157 IARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
9-205 |
6.71e-30 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 111.62 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTL---VNVMTGIDTPTR--GSVAAVGKNIEKFGEDrLAT 83
Cdd:TIGR00972 5 ENLNLFY----GEKEALKNINLDIPKNQVTALIGPSGCGKSTLlrsLNRMNDLVPGVRieGKVLFDGQDIYDKKID-VVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 84 WRgRNVGVVFQFFQLLPtLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI-GRYADNL---PADLSGGQQQRAAIAR 159
Cdd:TIGR00972 80 LR-RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALwDEVKDRLhdsALGLSGGQQQRLCIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084922189 160 ALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHE 205
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHN 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-226 |
8.46e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 8.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 14 SYDTPTGQfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIeKFGEDRLATWRgRNVGVVF 93
Cdd:PRK13639 8 KYSYPDGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 94 QF--FQLLPTlTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVA 170
Cdd:PRK13639 85 QNpdDQLFAP-TVEEDVAFgPLNLG--LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 171 DEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDL-SRHFTRVVELSDGRILSQ 226
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLvPVYADKVYVMSDGKIIKE 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-227 |
1.23e-29 |
|
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: 113.28 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGRNVGVVFQFFQLLPTLTVVE 106
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 107 NIMLPMDFCHflpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVI 186
Cdd:TIGR02142 95 NLRYGMKRAR---PSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1084922189 187 ELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRILSQS 227
Cdd:TIGR02142 172 PYLERLHAEfGIPILYVSHSLQEVLRLAdRVVVLEDGRVAAAG 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-207 |
1.53e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.49 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDtptGQFLaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTP---TRGSVAAVGKNIekfgeDRLA 82
Cdd:COG4136 2 LSLENLTITLG---GRPL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-----TALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 TWRgRNVGVVFQFFQLLPTLTVVENIM--LPMDfchfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARA 160
Cdd:COG4136 73 AEQ-RRIGILFQDDLLFPHLSVGENLAfaLPPT----IGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEVIEL-FAGLAVEGKAVAMVTHERD 207
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEE 195
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-224 |
1.60e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.59 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 19 TGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGRNVGVVFQFFQL 98
Cdd:PRK10070 38 TGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 LPTLTVVENIMLPMDFCHfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAG-INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 179 ----SRTSDEVIELfagLAVEGKAVAMVTHERDLS-RHFTRVVELSDGRIL 224
Cdd:PRK10070 197 plirTEMQDELVKL---QAKHQRTIVFISHDLDEAmRIGDRIAIMQNGEVV 244
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-218 |
1.69e-29 |
|
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: 115.08 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDrlaTWRGRnVGVVFQFFQLLPTlT 103
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---SWRDQ-IAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 VVENIML--PMDFCHFLPTSKRRGRAMELLEKLSIG--RYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:TIGR02857 412 IAENIRLarPDASDAEIREALERAGLDEFVAALPQGldTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190
....*....|....*....|....*....|....*....
gi 1084922189 180 RTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVEL 218
Cdd:TIGR02857 492 ETEAEVLEALRALA-QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-224 |
1.78e-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: 108.79 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 11 VSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTG--IDTPTRGSVAAVGKNIEKFgedrlaTWRGRn 88
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKR------SFRKI- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQFFQLLPTLTVVENIMLpmdfchflpTSKRRGramelleklsigryadnlpadLSGGQQQRAAIARALANDPPII 168
Cdd:cd03213 84 IGYVPQDDILHPTLTVRETLMF---------AAKLRG---------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 169 VADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE--RDLSRHFTRVVELSDGRIL 224
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpsSEIFELFDKLLLLSQGRVI 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-223 |
1.81e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.06 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 29 DLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatwrgRNVGVVFQFFQLLPTLTVVENI 108
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 109 MLPMDfchflP----TSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDE 184
Cdd:PRK10771 93 GLGLN-----PglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1084922189 185 VIELFAGLAVEGK-AVAMVTHE-RDLSRHFTRVVELSDGRI 223
Cdd:PRK10771 168 MLTLVSQVCQERQlTLLMVSHSlEDAARIAPRSLVVADGRI 208
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-226 |
2.11e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.85 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgeDRLATWRGr 87
Cdd:PRK13632 10 VENVSFSY--PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEIRK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQ-----FFqllpTLTV-------VENIMLPmdfchflpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRA 155
Cdd:PRK13632 84 KIGIIFQnpdnqFI----GATVeddiafgLENKKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEG-KAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQ 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
24-224 |
2.87e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.10 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI---DTPTRGSVAAVGKNIEKFGedRLA--TWRGR-NVGVVFQFFQ 97
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREG--RLArdIRKSRaNTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 98 LLPTLTVVENIML------PM---DFCHFLPTSKRRgrAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPII 168
Cdd:PRK09984 97 LVNRLSVLENVLIgalgstPFwrtCFSWFTREQKQR--ALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 169 VADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHERDLS-RHFTRVVELSDGRIL 224
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYAlRYCERIVALRQGHVF 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-226 |
3.11e-29 |
|
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: 107.78 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATwr 85
Cdd:cd03247 1 LSINNVSFSY--PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 grnVGVVFQFFQLLPTltvvenimlpmdfchflptskrrgramelleklSIGryaDNLPADLSGGQQQRAAIARALANDP 165
Cdd:cd03247 77 ---ISVLNQRPYLFDT---------------------------------TLR---NNLGRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-224 |
3.46e-29 |
|
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: 108.43 E-value: 3.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGdFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEdrlaTWR 85
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GRnVGVVFQFFQLLPTLTVVENImlpmDFCHFL---PTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALA 162
Cdd:cd03264 72 RR-IGYLPQEFGVYPNFTVREFL----DYIAWLkgiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 163 NDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHE-RDLSRHFTRVVELSDGRIL 224
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-218 |
3.98e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.09 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGkniekfgedrlatwrGRNVGVVFQFFQLLPTL- 102
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 103 -TVVENIML---PMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:NF040873 72 lTVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1084922189 179 SRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVEL 218
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
24-222 |
5.64e-29 |
|
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: 108.68 E-value: 5.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSV----AAVGKNIEKFGEDRLATWRGRNVGVVFQFFQLL 99
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhDGGWVDLAQASPREILALRRRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 P---TLTVVENIMLPMDFchflPTSKRRGRAMELLEKLSIG-RYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTG 175
Cdd:COG4778 106 PrvsALDVVAEPLLERGV----DREEARARARELLARLNLPeRLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1084922189 176 NLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGR 222
Cdd:COG4778 182 SLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVaDRVVDVTPFS 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-231 |
7.66e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 7.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEdrlaTWRGRNVGVVFQ-----FFql 98
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE----KWVRSKVGLVFQdpddqVF-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 lpTLTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNL 177
Cdd:PRK13647 94 --SSTVWDDVAFgPVNMG--LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 178 DSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFT-RVVELSDGRILSQSEVSV 231
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWAdQVIVLKEGRVLAEGDKSL 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
8-224 |
1.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.06 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTG-QFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRG 86
Cdd:PRK13649 5 LQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 87 RNVGVVFQF--FQLLPTlTVVENIML-PMDFchflPTSKRRGRAMELlEKLSIGRYADNL----PADLSGGQQQRAAIAR 159
Cdd:PRK13649 85 KKVGLVFQFpeSQLFEE-TVLKDVAFgPQNF----GVSQEEAEALAR-EKLALVGISESLfeknPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 160 ALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH-ERDLSRHFTRVVELSDGRIL 224
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANYADFVYVLEKGKLV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-223 |
1.23e-28 |
|
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: 107.52 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATwR 85
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR-A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GrnVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLsiGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:cd03224 76 G--IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRL--KERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIaDRAYVLERGRV 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
24-225 |
1.35e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 109.05 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGRNVGVVFQF--FQLLPT 101
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpeSQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 lTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGR-YADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:PRK13643 101 -TVLKDVAFgPQNFG--IPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1084922189 180 RTSDEVIELFAGLAVEGKAVAMVTH-ERDLSRHFTRVVELSDGRILS 225
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-230 |
1.82e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.80 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgEDR 80
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRGrnVGVVFQFFQLLPTLTVVENImlpmdFCHFLPTSK-----------RRGRAMELLEKLSIGRYADNLPADLSG 149
Cdd:PRK09700 76 LAAQLG--IGIIYQELSVIDELTVLENL-----YIGRHLTKKvcgvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLdsrTSDEVIELFA---GLAVEGKAVAMVTHE-RDLSRHFTRVVELSDGRILS 225
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLimnQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSSVC 225
|
....*
gi 1084922189 226 QSEVS 230
Cdd:PRK09700 226 SGMVS 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
2.40e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.18 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGK--NIEKFGE 78
Cdd:PRK13635 1 MKEEIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 79 DRlatwrgRNVGVVFQF--FQLLPTlTV-------VENIMLPMDfchflptsKRRGRAMELLEKLSIGRYADNLPADLSG 149
Cdd:PRK13635 79 VR------RQVGMVFQNpdNQFVGA-TVqddvafgLENIGVPRE--------EMVERVDQALRQVGMEDFLNREPHRLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKA-VAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-224 |
2.48e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.17 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPT-GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSV----------------- 66
Cdd:PRK13631 21 ILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 67 -AAVGKNIEKFGEDRlatwrgRNVGVVFQF--FQLLPTlTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGR-YAD 141
Cdd:PRK13631 101 tNPYSKKIKNFKELR------RRVSMVFQFpeYQLFKD-TIEKDIMFgPVALG--VKKSEAKKLAKFYLNKMGLDDsYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 142 NLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDlsrhftRVVELSDG 221
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME------HVLEVADE 245
|
...
gi 1084922189 222 RIL 224
Cdd:PRK13631 246 VIV 248
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
25-226 |
3.95e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.12 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGrnvgVVFQFFQLLPTLTV 104
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA----VLPQHSSLAFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 105 VENIML---PmdfcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALA-------NDPPIIVADEPT 174
Cdd:COG4559 93 EEVVALgraP----HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 175 GNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFT-RVVELSDGRILSQ 226
Cdd:COG4559 169 SALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYAdRILLLHQGRLVAQ 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-223 |
3.97e-28 |
|
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: 111.38 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 14 SYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLatwrGRNVGVVF 93
Cdd:COG4618 337 TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL----GRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 94 QFFQLLPTlTVVENI-MLPMdfchflPTSK------RRGRAMELLEKLSIGrYADNLPAD---LSGGQQQRAAIARALAN 163
Cdd:COG4618 413 QDVELFDG-TIAENIaRFGD------ADPEkvvaaaKLAGVHEMILRLPDG-YDTRIGEGgarLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-224 |
1.36e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 104.22 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatwrgR 87
Cdd:cd03268 3 TNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMLpmdfcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPI 167
Cdd:cd03268 73 RIGALIEAPGFYPNLTARENLRL-----LARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE-RDLSRHFTRVVELSDGRIL 224
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-223 |
1.40e-27 |
|
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: 104.76 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 10 HVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedRLATWRgRNV 89
Cdd:cd03265 5 NLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVR-RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 90 GVVFQFFQLLPTLTVVENiMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIV 169
Cdd:cd03265 76 GIVFQDLSVDDELTGWEN-LYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 170 ADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHERDLSRHFT-RVVELSDGRI 223
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCdRVAIIDHGRI 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-223 |
1.64e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 109.75 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 32 LRAGDFLAIVGKSGSGKSTLVNVMTGIDTP---TRGSVAAVGKNIEKfgedrlatWRGRNV-GVVFQFFQLLPTLTVVEN 107
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA--------KEMRAIsAYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 108 IM----LPMDfcHFLPTSKRRGRAMELLEKLSIGRYAD------NLPADLSGGQQQRAAIARALANDPPIIVADEPTGNL 177
Cdd:TIGR00955 120 LMfqahLRMP--RRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1084922189 178 DSRTSDEVIELFAGLAVEGKAVAMVTHE--RDLSRHFTRVVELSDGRI 223
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRV 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-179 |
2.81e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.04 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaavgknieKFGEDRL--ATWR 85
Cdd:PRK11000 6 LRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL--------FIGEKRMndVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GRNVGVVFQFFQLLPTLTVVENimlpMDFCHFLPTSK---RRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALA 162
Cdd:PRK11000 74 ERGVGMVFQSYALYPHLSVAEN----MSFGLKLAGAKkeeINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170
....*....|....*..
gi 1084922189 163 NDPPIIVADEPTGNLDS 179
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDA 166
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-226 |
2.99e-27 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 104.23 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtPTGQFlALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrLATWRgR 87
Cdd:cd03251 3 FKNVTFRYP-GDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTlTVVENIMLpmdfchflptsKRRGRAMELLEKLSIGRYA----DNLP-----------ADLSGGQQ 152
Cdd:cd03251 77 QIGLVSQDVFLFND-TVAENIAY-----------GRPGATREEVEEAARAANAhefiMELPegydtvigergVKLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 153 QRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-228 |
5.07e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 5.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 14 SYDTPTGQfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgeDRLATWRgRNVGVVF 93
Cdd:PRK13644 8 SYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF--SKLQGIR-KLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 94 QFFQL-LPTLTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVAD 171
Cdd:PRK13644 84 QNPETqFVGRTVEEDLAFgPENLC--LPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 172 EPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQSE 228
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-204 |
5.61e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.27 E-value: 5.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfGEDR 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP--SRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRgrnVGVVFQFFQLLPTLTVVENIMLpmdFCHF--LPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:PRK13537 77 HARQR---VGVVPQFDNLDPDFTVRENLLV---FGRYfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH 204
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-224 |
7.04e-27 |
|
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: 107.82 E-value: 7.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 14 SYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLatwrGRNVGVVF 93
Cdd:TIGR01842 323 TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETF----GKHIGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 94 QFFQLLPTlTVVENImlpmdfCHF--LPTSK------RRGRAMELLEKLSIGRYADNLP--ADLSGGQQQRAAIARALAN 163
Cdd:TIGR01842 399 QDVELFPG-TVAENI------ARFgeNADPEkiieaaKLAGVHELILRLPDGYDTVIGPggATLSGGQRQRIALARALYG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRIL 224
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-223 |
9.16e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 9.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTG-QFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatwRG 86
Cdd:COG1101 4 LKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK----RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 87 RNVGVVFQFFQL--LPTLTVVENIMLPMDFCHFLP-----TSKRRGRAMELLEKLSIG---RYADNLpADLSGGQQQRAA 156
Cdd:COG1101 80 KYIGRVFQDPMMgtAPSMTIEENLALAYRRGKRRGlrrglTKKRRELFRELLATLGLGlenRLDTKV-GLLSGGQRQALS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 157 IARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVA-MVTHE-RDLSRHFTRVVELSDGRI 223
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTlMVTHNmEQALDYGNRLIMMHEGRI 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-224 |
1.01e-26 |
|
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: 102.45 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgEDRLATw 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEAR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 rgRNVGVVFQFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAND 164
Cdd:cd03266 78 --RRLGFVSDSTGLYDRLTARENLEYFAGL-YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERD-LSRHFTRVVELSDGRIL 224
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVV 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-223 |
1.10e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 23 LALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEdrlaTWRGRN-VGVVFQF--FQLL 99
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN----LWDIRNkAGMVFQNpdNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PTLtVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:PRK13633 100 ATI-VEEDVAFgPENLG--IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084922189 179 SRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:PRK13633 177 PSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-220 |
1.39e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 106.53 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 2 SPSLLCLRHVSKSYdtPTGQflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIeKFGEDRL 81
Cdd:PRK11288 1 SSPYLSFDGIGKTF--PGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 82 ATWRGrnVGVVFQFFQLLPTLTVVENIML---PMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:PRK11288 76 ALAAG--VAIIYQELHLVPEMTVAENLYLgqlPHKG-GIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDlsrhftRVVELSD 220
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME------EIFALCD 208
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
8-226 |
2.07e-26 |
|
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: 106.87 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgeDRlATWRgR 87
Cdd:TIGR03375 466 FRNVSFAY--PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI--DP-ADLR-R 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLpTLTVVENIMLPMDFchflpTSKRRgrAMELLEKLSIGRYADNLP-----------ADLSGGQQQRAA 156
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIALGAPY-----ADDEE--ILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVA 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 157 IARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLaVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW-LAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-224 |
1.30e-25 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 104.11 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtptgQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDT--PTRGSV----------------AAV 69
Cdd:TIGR03269 3 VKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 70 GKNIEKFGE-------------DRLATWRGRNVGVVFQ-FFQLLPTLTVVENIMLPMDFCHFlPTSKRRGRAMELLEKLS 135
Cdd:TIGR03269 79 GEPCPVCGGtlepeevdfwnlsDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGY-EGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 136 IGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGlAVEGKAVAMVtherdLSRHFTRV 215
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE-AVKASGISMV-----LTSHWPEV 231
|
250
....*....|
gi 1084922189 216 VE-LSDGRIL 224
Cdd:TIGR03269 232 IEdLSDKAIW 241
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-226 |
1.34e-25 |
|
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: 99.87 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSY--DTPtgqfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrlATWR 85
Cdd:cd03252 3 FEHVRFRYkpDGP----VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD----PAWL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GRNVGVVFQFfQLLPTLTVVENIMLP---MDFCHFLPTSKRRGrAMELLEKLSIGrYADNLP---ADLSGGQQQRAAIAR 159
Cdd:cd03252 75 RRQVGVVLQE-NVLFNRSIRDNIALAdpgMSMERVIEAAKLAG-AHDFISELPEG-YDTIVGeqgAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 160 ALANDPPIIVADEPTGNLDSRtSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-226 |
1.60e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 103.75 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLatw 84
Cdd:PRK11160 338 SLTLNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RgRNVGVVFQFFQLLPTlTVVENIMLPMDfchflptSKRRGRAMELLEKLSIGRYADNLPA----------DLSGGQQQR 154
Cdd:PRK11160 413 R-QAISVVSQRVHLFSA-TLRDNLLLAAP-------NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 155 AAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-226 |
1.80e-25 |
|
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: 98.89 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR---LA 82
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigyLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 TWRGrnvgvvfqffqLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALA 162
Cdd:cd03269 77 EERG-----------LYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 163 NDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRILSQ 226
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLY 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-204 |
2.05e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfGEDR 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRgrnVGVVFQFFQLLPTLTVVENIMLpmdFCHFLPTSKRRGRAM--ELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:PRK13536 111 LARAR---IGVVPQFDNLDLEFTVRENLLV---FGRYFGMSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH 204
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-204 |
2.21e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.60 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI-----DTPTRGSVAAVGKNIEKFGEDRLAtwrgRNVGVVFQ 94
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELR----RRVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 95 FFQLLPTLTVVENIMLPMDFCHFLPTSKR-RGRAMELLEKLSIGRYADN---LPA-DLSGGQQQRAAIARALANDPPIIV 169
Cdd:PRK14247 90 IPNPIPNLSIFENVALGLKLNRLVKSKKElQERVRWALEKAQLWDEVKDrldAPAgKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1084922189 170 ADEPTGNLDSRTSDEVIELFAGLAVEgKAVAMVTH 204
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-174 |
2.58e-25 |
|
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: 99.14 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedRLATWR 85
Cdd:TIGR03410 1 LEVSNLNVYY----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK----LPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GRN-VGVVFQFFQLLPTLTVVENIMLPMDfchflpTSKRRGRAM--ELLEKLSIGRYADNLPA-DLSGGQQQRAAIARAL 161
Cdd:TIGR03410 73 ARAgIAYVPQGREIFPRLTVEENLLTGLA------ALPRRSRKIpdEIYELFPVLKEMLGRRGgDLSGGQQQQLAIARAL 146
|
170
....*....|...
gi 1084922189 162 ANDPPIIVADEPT 174
Cdd:TIGR03410 147 VTRPKLLLLDEPT 159
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-225 |
4.51e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.70 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDTPTG-QFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVA----AVGKNIEKFGE-D 79
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyAIPANLKKIKEvK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 80 RLAtwrgRNVGVVFQF--FQLLPTlTVVENIML-PMDfchfLPTSKRRG--RAMELLEKLSIGR-YADNLPADLSGGQQQ 153
Cdd:PRK13645 87 RLR----KEIGLVFQFpeYQLFQE-TIEKDIAFgPVN----LGENKQEAykKVPELLKLVQLPEdYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 154 RAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERD-LSRHFTRVVELSDGRILS 225
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDqVLRIADEVIVMHEGKVIS 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
25-226 |
5.94e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.55 E-value: 5.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgrnvgvvfQFFQLLPT-LT 103
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-----------RRLALLPQhHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 VVENIML---------PmdfchFLP-----TSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIV 169
Cdd:PRK11231 87 TPEGITVrelvaygrsP-----WLSlwgrlSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 170 ADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHerDL---SRHFTRVVELSDGRILSQ 226
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH--DLnqaSRYCDHLVVLANGHVMAQ 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-224 |
6.29e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 96.73 E-value: 6.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFG-------------EDRLAtwRGrnvg 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSprdairagiayvpEDRKR--EG---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 91 vvfqffqLLPTLTVVENIMLPmdfchflptskrrgramelleklsigryadnlpADLSGGQQQRAAIARALANDPPIIVA 170
Cdd:cd03215 89 -------LVLDLSVAENIALS---------------------------------SLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 171 DEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDlsrhftRVVELSDgRIL 224
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELD------ELLGLCD-RIL 175
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-226 |
9.33e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 9.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgR 87
Cdd:COG4604 4 IKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIMlpmdFCHFlPTSKRR---------GRAMELLEKLSI-GRYADNLpadlSGGQQQRAAI 157
Cdd:COG4604 76 RLAILRQENHINSRLTVRELVA----FGRF-PYSKGRltaedreiiDEAIAYLDLEDLaDRYLDEL----SGGQRQRAFI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 158 ARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDL---SRHFTRVVELSDGRILSQ 226
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLH--DInfaSCYADHIVAMKDGRVVAQ 217
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
25-224 |
1.13e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 100.30 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgeDRLATWRGRNVGVVFQFFQL---LPT 101
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE----ALSARAASRRVASVPQDTSLsfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 LTVVENIMLPmDFCHFLPTSKRRGRAME-LLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSR 180
Cdd:PRK09536 95 RQVVEMGRTP-HRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1084922189 181 TSDEVIELFAGLAVEGKAVAMVTHERDL-SRHFTRVVELSDGRIL 224
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRVR 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-226 |
2.35e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATW 84
Cdd:PRK13548 2 MLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RgrnvGVVFQFFQLLPTLTVVENIML---PmdfchfLPTSKRRGRA--MELLEKLSIGRYADNLPADLSGGQQQRAAIAR 159
Cdd:PRK13548 78 R----AVLPQHSSLSFPFTVEEVVAMgraP------HGLSRAEDDAlvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 160 ALA------NDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRILSQ 226
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYAdRIVLLHQGRLVAD 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-202 |
2.97e-24 |
|
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: 96.20 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 3 PSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIekfgeDRLA 82
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-----TGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 TWR-----------GRNVgvvfqfFqllPTLTVVENIMLPMdfchFLPTSKRRGRA-----MELLEKLsiGRYADNLPAD 146
Cdd:COG0410 72 PHRiarlgigyvpeGRRI------F---PSLTVEENLLLGA----YARRDRAEVRAdlervYELFPRL--KERRRQRAGT 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMV 202
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLV 192
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-226 |
3.91e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGK-----NIEK 75
Cdd:PRK11701 2 MDQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 76 FGE-DRLATWRGRnVGVVFQFFQ--LLPTLTVVENI---MLPMDFCHFlptSKRRGRAMELLEKLSIGR-YADNLPADLS 148
Cdd:PRK11701 78 LSEaERRRLLRTE-WGFVHQHPRdgLRMQVSAGGNIgerLMAVGARHY---GDIRATAGDWLERVEIDAaRIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 149 GGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSR---HftRVVELSDGRIL 224
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARllaH--RLLVMKQGRVV 231
|
..
gi 1084922189 225 SQ 226
Cdd:PRK11701 232 ES 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-223 |
4.76e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.10 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGK-----NIEKFG--- 77
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpeDRRRIGylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 78 EDRlatwrgrnvGvvfqffqLLPTLTVVENIM----LpmdfcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQ 153
Cdd:COG4152 78 EER---------G-------LYPKMKVGEQLVylarL-----KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 154 RAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDL-SRHFTRVVELSDGRI 223
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELvEELCDRIVIINKGRK 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
4.76e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.92 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLcLRHVSKSY------------------DTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPT 62
Cdd:COG1134 1 MSSMIE-VENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 63 RGSVaavgkniekfgedrlaTWRGR-----NVGVVFQffqllPTLTVVENIMLpmdfchflptskrRGRAM-----ELLE 132
Cdd:COG1134 80 SGRV----------------EVNGRvsallELGAGFH-----PELTGRENIYL-------------NGRLLglsrkEIDE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 133 KLS-------IGRYADnLPA-DLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH 204
Cdd:COG1134 126 KFDeivefaeLGDFID-QPVkTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSH 204
|
250 260
....*....|....*....|
gi 1084922189 205 ERD-LSRHFTRVVELSDGRI 223
Cdd:COG1134 205 SMGaVRRLCDRAIWLEKGRL 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-204 |
5.89e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.87 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLV---NVMtgID-TP---TRGSVAAVGKNIEKFGEDrLATWRgRNVGVV 92
Cdd:COG1117 22 GDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRM--NDlIPgarVEGEILLDGEDIYDPDVD-VVELR-RRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 93 FQffqlLPT---LTVVENIMLPMDFCHFlptsKRRGRAMELLEKlSIGRYA------DNL--PA-DLSGGQQQRAAIARA 160
Cdd:COG1117 98 FQ----KPNpfpKSIYDNVAYGLRLHGI----KSKSELDEIVEE-SLRKAAlwdevkDRLkkSAlGLSGGQQQRLCIARA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTH 204
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIVTH 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-223 |
1.05e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTgqfLaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAaVGKNIEkfgedrlatwrgr 87
Cdd:COG0488 1 LENLSKSFGGRP---L-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-IPKGLR------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 nVGVVFQFFQLLPTLTVVENIM---------------LPMDFCHFLPTSKRRG----------------RAMELLEKLSI 136
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLdgdaelraleaeleeLEAKLAEPDEDLERLAelqeefealggweaeaRAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 137 G-RYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTsdevIELFAG-LAVEGKAVAMVTHerDlsRHF-- 212
Cdd:COG0488 142 PeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEfLKNYPGTVLVVSH--D--RYFld 213
|
250
....*....|....
gi 1084922189 213 ---TRVVELSDGRI 223
Cdd:COG0488 214 rvaTRILELDRGKL 227
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-226 |
1.20e-23 |
|
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: 95.28 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 3 PSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLA 82
Cdd:TIGR02323 1 KPLLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 TWRGRNV-----GVVFQFFQ--LLPTLTVVENI---MLPMDFCHFlptSKRRGRAMELLEKLSIGR-YADNLPADLSGGQ 151
Cdd:TIGR02323 77 EAERRRLmrtewGFVHQNPRdgLRMRVSAGANIgerLMAIGARHY---GNIRATAQDWLEEVEIDPtRIDDLPRAFSGGM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 152 QQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRILSQ 226
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAqRLLVMQQGRVVES 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-179 |
1.59e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.71 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedr 80
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 lATWRGRNVGVVFQFFQLLPTLTVVENI-----MLPmdfchfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRA 155
Cdd:PRK11432 73 -RSIQQRDICMVFQSYALFPHMSLGENVgyglkMLG------VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRV 145
|
170 180
....*....|....*....|....
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDS 179
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDA 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-230 |
1.65e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIE----------KFG---EDRlatwrgRNVG 90
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdairaGIAyvpEDR------KGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 91 vvfqffqLLPTLTVVENIMLPM--DFCH--FLPTSKRRGRAMELLEKLSIgRYAD-NLPA-DLSGGQQQRAAIARALAND 164
Cdd:COG1129 341 -------LVLDLSIRENITLASldRLSRggLLDRRRERALAEEYIKRLRI-KTPSpEQPVgNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERD----LSrhfTRVVELSDGRI---LSQSEVS 230
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPellgLS---DRILVMREGRIvgeLDREEAT 482
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-227 |
1.77e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR 80
Cdd:PRK13640 1 MKDNIVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRGRnVGVVFQF--FQLLPTlTVVENIMLPMDfCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIA 158
Cdd:PRK13640 79 VWDIREK-VGIVFQNpdNQFVGA-TVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFTRVVELSDGRILSQS 227
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-226 |
4.12e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.22 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 17 TPTGQFLAlTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIdTPTRGSVAAVGknIEkFGEDRLATWRgRNVGVVFQFF 96
Cdd:PRK11174 359 SPDGKTLA-GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKING--IE-LRELDPESWR-KHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 97 QLLPTlTVVENIMLpmdfchflptskrrGRA-------MELLEKLSIGRYADNLP-----------ADLSGGQQQRAAIA 158
Cdd:PRK11174 433 QLPHG-TLRDNVLL--------------GNPdasdeqlQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIElfaGL--AVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLDAHSEQLVMQ---ALnaASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-230 |
5.44e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 96.61 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPsLLCLRHVSKSYdtPTGQflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIeKFGEDR 80
Cdd:PRK10762 1 MQA-LLQLKGIDKAF--PGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRGrnVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPT---SKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAI 157
Cdd:PRK10762 75 SSQEAG--IGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 158 ARALANDPPIIVADEPTgnlDSRTSDEVIELFA---GLAVEGKAVAMVTHErdLSRHFT---RVVELSDGRILSQSEVS 230
Cdd:PRK10762 153 AKVLSFESKVIIMDEPT---DALTDTETESLFRvirELKSQGRGIVYISHR--LKEIFEicdDVTVFRDGQFIAEREVA 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-224 |
7.88e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.13 E-value: 7.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgrNVGVV--FQFFQ 97
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-----RMGVVrtFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 98 LLPTLTVVENIM------LPMDFCHFL---PTSKRR-----GRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:PRK11300 91 LFREMTVIENLLvaqhqqLKTGLFSGLlktPAFRRAesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLsrhftrVVELSDgRIL 224
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKL------VMGISD-RIY 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-224 |
9.74e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.00 E-value: 9.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRlatWRG--RNVGVVFQ--FFQLL 99
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDE---WRAvrSDIQMIFQdpLASLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PTLTVVENIMLPMDFCH-FLPTS--KRRGRAME----LLEKLsIGRYadnlPADLSGGQQQRAAIARALANDPPIIVADE 172
Cdd:PRK15079 113 PRMTIGEIIAEPLRTYHpKLSRQevKDRVKAMMlkvgLLPNL-INRY----PHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 173 PTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHerDLSrhftrVVE-LSDgRIL 224
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREmGLSLIFIAH--DLA-----VVKhISD-RVL 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-222 |
9.76e-23 |
|
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: 91.38 E-value: 9.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDT-PTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKniekfgedrlatw 84
Cdd:cd03250 1 ISVEDASFTWDSgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 rgrnVGVVFQFFQLLPTlTVVENIM--LPMDfchflptSKRRGRAME---LLEKLSIgryadnLPA-D----------LS 148
Cdd:cd03250 68 ----IAYVSQEPWIQNG-TIRENILfgKPFD-------EERYEKVIKacaLEPDLEI------LPDgDlteigekginLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 149 GGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIE-LFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGR 222
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-226 |
1.37e-22 |
|
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: 91.83 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDT-PTGQflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRLATWRg 86
Cdd:cd03249 3 FKNVSFRYPSrPDVP--ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 87 RNVGVVFQFFQLLPTlTVVENIMlpmdFCHFLPTSKRrgrAMELLEKLSIGRYADNLP-----------ADLSGGQQQRA 155
Cdd:cd03249 77 SQIGLVSQEPVLFDG-TIAENIR----YGKPDATDEE---VEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRtSDEVIELFAGLAVEGKAVAMVTHErdLS--RHFTRVVELSDGRILSQ 226
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKGRTTIVIAHR--LStiRNADLIAVLQNGQVVEQ 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-178 |
1.68e-22 |
|
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: 91.45 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwr 85
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GRNVGVVFQFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170
....*....|...
gi 1084922189 166 PIIVADEPTGNLD 178
Cdd:cd03218 153 KFLLLDEPFAGVD 165
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.69e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSY--DTPtgqfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAvgkNIEKFGE 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYqsDAS----FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 79 DRLATWRgRNVGVVFQ-----FFQLLPTLTV---VENimlpmdfcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGG 150
Cdd:PRK13648 76 DNFEKLR-KHIGIVFQnpdnqFVGSIVKYDVafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 151 QQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEgKAVAM--VTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSE-HNITIisITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-223 |
1.88e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.71 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 23 LALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFG-------------EDRLATwrgrnv 89
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSprerrrlgvayipEDRLGR------ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 90 GVVfqffqllPTLTVVENIML----PMDFCH--FLPTSKRRGRAMELLEKLSIgRYAD-NLPAD-LSGGQQQRAAIARAL 161
Cdd:COG3845 346 GLV-------PDMSVAENLILgryrRPPFSRggFLDRKAIRAFAEELIEEFDV-RTPGpDTPARsLSGGNQQKVILAREL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERD----LSrhfTRVVELSDGRI 223
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDeilaLS---DRIAVMYEGRI 480
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-226 |
3.50e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 94.40 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRLATWRgRN 88
Cdd:TIGR02203 334 RNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLR-RQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQFFQLLPTlTVVENIMLpmdfchflptSKRRGRAMELLEKLSIGRYA----DNLP-----------ADLSGGQQQ 153
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAY----------GRTEQADRAEIERALAAAYAqdfvDKLPlgldtpigengVLLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 154 RAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLaVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADRIVVMDDGRIVER 548
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-173 |
3.67e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGRnVGVVFQFFQLL 99
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALF 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 100 PTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEP 173
Cdd:PRK11831 97 TDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
4.42e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTGqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkFGEDR 80
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATWRgRNVGVVFQF--FQLLpTLTVVENIML-PMDFChfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAI 157
Cdd:PRK13636 77 LMKLR-ESVGMVFQDpdNQLF-SASVYQDVSFgAVNLK--LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 158 ARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDL-SRHFTRVVELSDGRILSQSEVS 230
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPK 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-223 |
4.88e-22 |
|
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: 90.28 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTGQ------------------FLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAV 69
Cdd:cd03220 3 LENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 70 GKNIEKFGedrlatwrgrnVGVVFQffqllPTLTVVENIMLpmdFCHFLPTSKRRGRAM--ELLEKLSIGRYADnLP-AD 146
Cdd:cd03220 83 GRVSSLLG-----------LGGGFN-----PELTGRENIYL---NGRLLGLSRKEIDEKidEIIEFSELGDFID-LPvKT 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:cd03220 143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLcDRALVLEKGKI 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
9-223 |
6.25e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.49 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrLATWRgRN 88
Cdd:PRK13657 338 DDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQfFQLLPTLTVVENIML--PMDFCHFLPTSKRRGRAMELLEKlSIGRYADNL---PADLSGGQQQRAAIARALAN 163
Cdd:PRK13657 411 IAVVFQ-DAGLFNRSIEDNIRVgrPDATDEEMRAAAERAQAHDFIER-KPDGYDTVVgerGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLaVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-223 |
6.26e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaAVGKNIEkfgedrlatwrgr 87
Cdd:COG0488 318 LEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVK------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 nVGVVFQFFQLL-PTLTVVENImlpmdfCHFLPTsKRRGRAMELLEK-LSIGRYADNLPADLSGGQQQRAAIARALANDP 165
Cdd:COG0488 380 -IGYFDQHQEELdPDKTVLDEL------RDGAPG-GTEQEVRGYLGRfLFSGDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 166 PIIVADEPTGNLD--SRTS-DEVIELFAGlavegkAVAMVTHERD-LSRHFTRVVELSDGRI 223
Cdd:COG0488 452 NVLLLDEPTNHLDieTLEAlEEALDDFPG------TVLLVSHDRYfLDRVATRILEFEDGGV 507
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-180 |
1.17e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.44 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGK---NIEKfgedrlatw 84
Cdd:PRK11650 6 LQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEP--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RGRNVGVVFQFFQLLPTLTVVENIMLPMdfchflptsKRRGRAMELLEK--------LSIGRYADNLPADLSGGQQQRAA 156
Cdd:PRK11650 74 ADRDIAMVFQNYALYPHMSVRENMAYGL---------KIRGMPKAEIEErvaeaariLELEPLLDRKPRELSGGQRQRVA 144
|
170 180
....*....|....*....|....
gi 1084922189 157 IARALANDPPIIVADEPTGNLDSR 180
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAK 168
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-205 |
1.28e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 91.12 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIdTPTRGSVAAvgkniekfgeDRLaTW 84
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTA----------DRF-RW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 R----------------GRNVGVVFQFFQ--LLPTLTVVENIM--LPMDF--CHFLPTSK-RRGRAMELLEKLSI---GR 138
Cdd:COG4170 71 NgidllklsprerrkiiGREIAMIFQEPSscLDPSAKIGDQLIeaIPSWTfkGKWWQRFKwRKKRAIELLHRVGIkdhKD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 139 YADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLA-VEGKAVAMVTHE 205
Cdd:COG4170 151 IMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHD 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-219 |
1.54e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.00 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVsksyDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDrlaTW 84
Cdd:PRK10247 7 LLQLQNV----GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RgRNVGVVFQffqlLPTL---TVVENIMLPM-------DFCHFLPTSKRRGRAMELLEKlSIgryadnlpADLSGGQQQR 154
Cdd:PRK10247 80 R-QQVSYCAQ----TPTLfgdTVYDNLIFPWqirnqqpDPAIFLDDLERFALPDTILTK-NI--------AELSGGEKQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 155 AAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFTRVVELS 219
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-226 |
1.58e-21 |
|
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: 89.21 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTptgQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLatwRgR 87
Cdd:cd03253 3 FENVTFAYDP---GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL---R-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTlTVVENImlpmdfchflptskRRGR-------AMELLEKLSIGRYADNLP-----------ADLSG 149
Cdd:cd03253 76 AIGVVPQDTVLFND-TIGYNI--------------RYGRpdatdeeVIEAAKAAQIHDKIMRFPdgydtivgergLKLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-204 |
1.92e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI-----DTPTRGSVAAVGKNIekFGEDRLATWRGRNVGVVFQ 94
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 95 FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAME-LLEKLSI-----GRYADnLPADLSGGQQQRAAIARALANDPPII 168
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALwdevkDRLND-YPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1084922189 169 VADEPTGNLDSRTSDEVIELFAGLAVEgKAVAMVTH 204
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTH 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-224 |
1.93e-21 |
|
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: 92.17 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSY-DTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAA-VGK---NIEKFGEDRla 82
Cdd:TIGR03269 282 VRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDewvDMTKPGPDG-- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 twRGRN---VGVVFQFFQLLPTLTVVEN------IMLPMDFCHF--LPTSKRRG----RAMELLEKLsigryadnlPADL 147
Cdd:TIGR03269 360 --RGRAkryIGILHQEYDLYPHRTVLDNlteaigLELPDELARMkaVITLKMVGfdeeKAEEILDKY---------PDEL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 148 SGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRIL 224
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCdRAALMRDGKIV 507
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-205 |
2.50e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.17 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI---DTPTRGSVAAVGKNIEKFG 77
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 78 EDRLATWRGRNVGVVFQ--FFQLLPTLTVVENIMlpmdfcHFLPTSKRRGRAMELLE--------KLSIGRYADNL-PAD 146
Cdd:PRK09473 88 EKELNKLRAEQISMIFQdpMTSLNPYMRVGEQLM------EVLMLHKGMSKAEAFEEsvrmldavKMPEARKRMKMyPHE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHE 205
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHD 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-179 |
3.09e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.62 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRLATWRgRN 88
Cdd:PRK11176 345 RNVTFTY--PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLR-NQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQFFQLLPTlTVVENIMLPM-DFC--HFLPTSKRRGRAMELLEKLS------IGRYAdnlpADLSGGQQQRAAIAR 159
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARtEQYsrEQIEEAARMAYAMDFINKMDngldtvIGENG----VLLSGGQRQRIAIAR 493
|
170 180
....*....|....*....|
gi 1084922189 160 ALANDPPIIVADEPTGNLDS 179
Cdd:PRK11176 494 ALLRDSPILILDEATSALDT 513
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
28-218 |
4.24e-21 |
|
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: 87.03 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 28 IDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIekfgeDRLATWRGRNVGVVFQFFQLLPTLTVVEN 107
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 108 IMLpmdFCHFLPTSKRRgrAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIE 187
Cdd:TIGR01189 94 LHF---WAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170 180 190
....*....|....*....|....*....|.
gi 1084922189 188 LFAGLAVEGKAVAMVTHErDLSRHFTRVVEL 218
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTHQ-DLGLVEARELRL 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-228 |
4.31e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 91.34 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgeDRlatwrgrnvGVVFQFFQLLP--- 100
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DR---------HTLRQFINYLPqep 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 101 ---TLTVVENIMLpmdfchflpTSKRRGRAMELLEKLSIGRYAD---NLP-----------ADLSGGQQQRAAIARALAN 163
Cdd:TIGR01193 558 yifSGSILENLLL---------GAKENVSQDEIWAACEIAEIKDdieNMPlgyqtelseegSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFagLAVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQSE 228
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS 691
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-227 |
1.10e-20 |
|
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: 87.00 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTG-----------------QFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaAVG 70
Cdd:cd03267 3 VSNLSKSYRVYSKepgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-RVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 71 KNIEKFGEDRLAtwrgRNVGVVF-QFFQLLPTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSG 149
Cdd:cd03267 82 GLVPWKRRKKFL----RRIGVVFgQKTQLWWDLPVIDSFYLLAAI-YDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVT-HE-RDLSRHFTRVVELSDGRILSQS 227
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTsHYmKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-223 |
1.17e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 86.76 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYDTPTGQfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgRN 88
Cdd:cd03248 15 QNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH----SK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQffqlLPTL---TVVENIMLPMDFCHF--LPTSKRRGRAMELLEKLSIGRY--ADNLPADLSGGQQQRAAIARAL 161
Cdd:cd03248 90 VSLVGQ----EPVLfarSLQDNIAYGLQSCSFecVKEAAQKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 162 ANDPPIIVADEPTGNLDSRtSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:cd03248 166 IRNPQVLILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-224 |
1.65e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.53 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRgRNVGVVFQ--FFQLLPT 101
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQdpYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 LTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI-GRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSR 180
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084922189 181 TSDEVIELFAGLAVE-GKAVAMVTHERD-LSRHFTRVVELSDGRIL 224
Cdd:PRK10261 498 IRGQIINLLLDLQRDfGIAYLFISHDMAvVERISHRVAVMYLGQIV 543
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-222 |
3.92e-20 |
|
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: 82.88 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDtptGQFLaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAaVGKNIEkfgedrlatwr 85
Cdd:cd03221 1 IELENLSKTYG---GKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-WGSTVK----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 grnvgvvfqffqllptltvvenimlpmdFCHFlptskrrgramelleklsigryadnlpADLSGGQQQRAAIARALANDP 165
Cdd:cd03221 65 ----------------------------IGYF---------------------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLavEGkAVAMVTHERDLSRHF-TRVVELSDGR 222
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEY--PG-TVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-204 |
4.05e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRG-RNVgvvfqffqLLPTLT 103
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhRNA--------MKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 VVENImlpmDF-CHFLPTskRRGRAMELLEKLSIGRYADnLPA-DLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRT 181
Cdd:PRK13539 90 VAENL----EFwAAFLGG--EELDIAAALEAVGLAPLAH-LPFgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|...
gi 1084922189 182 SDEVIELFAGLAVEGKAVAMVTH 204
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATH 185
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-205 |
5.58e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 86.72 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKS-TLVNVMTGIDTPTRGSVAAV---GKNIEKFGED 79
Cdd:PRK11022 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRVMAEKLefnGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 80 RLATWRGRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYA---DNLPADLSGGQQQR 154
Cdd:PRK11022 82 ERRNLVGAEVAMIFQdpMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 155 AAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLA-VEGKAVAMVTHE 205
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHD 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-227 |
5.60e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.94 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTGQFlALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGkniEKFGEDRLATWRgR 87
Cdd:PRK13650 7 VKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWDIR-H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQ-----FFqllpTLTVVENIMLPMDfCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALA 162
Cdd:PRK13650 82 KIGMVFQnpdnqFV----GATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 163 NDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFTRVVELSDGRILSQS 227
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQVESTS 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-219 |
1.23e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.31 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 26 TDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLA--TWRGRNVGVVfqffqllPTLT 103
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdlLYLGHQPGIK-------TELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 VVENimlpMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSD 183
Cdd:PRK13538 91 ALEN----LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1084922189 184 EVIELFAGLAVEGKAVAMVTHeRDLSRHFTRVVELS 219
Cdd:PRK13538 167 RLEALLAQHAEQGGMVILTTH-QDLPVASDKVRKLR 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-226 |
1.32e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgRNVGVVFQFFQLL 99
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PTLTVVENIMLPMDFCHFLPTSKRR------GRAMellEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEP 173
Cdd:PRK10253 94 GDITVQELVARGRYPHQPLFTRWRKedeeavTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 174 TGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLS-RHFTRVVELSDGRILSQ 226
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQAcRYASHLIALREGKIVAQ 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-178 |
1.39e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVG-------KNI----EKfgedrlatwrgRNVGVVFQF 95
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGIclppEK-----------RRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 96 FQLLPTLTVVENIMLPMdfchflpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTG 175
Cdd:PRK11144 85 ARLFPHYKVRGNLRYGM-------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
...
gi 1084922189 176 NLD 178
Cdd:PRK11144 158 SLD 160
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-173 |
1.41e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 3 PSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRla 82
Cdd:COG1137 1 MMTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 twRGRnVGV--------VFQffqllpTLTVVENIMLPMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQR 154
Cdd:COG1137 75 --RAR-LGIgylpqeasIFR------KLTVEDNILAVLEL-RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170
....*....|....*....
gi 1084922189 155 AAIARALANDPPIIVADEP 173
Cdd:COG1137 145 VEIARALATNPKFILLDEP 163
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-192 |
1.42e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 19 TGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTlvnvmTGID----TPTRGSVAAVGKNIEKFGEDRLATWRgRNVGVVFQ 94
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLAllrlINSQGEIWFDGQPLHNLNRRQLLPVR-HRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 95 --FFQLLPTLTVVENIMLPMDFCH-FLPTSKRRGRAMELLEKLSIG-----RYadnlPADLSGGQQQRAAIARALANDPP 166
Cdd:PRK15134 370 dpNSSLNPRLNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGLDpetrhRY----PAEFSGGQRQRIAIARALILKPS 445
|
170 180
....*....|....*....|....*.
gi 1084922189 167 IIVADEPTGNLDSRTSDEVIELFAGL 192
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSL 471
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-229 |
3.47e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.21 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTP----TRGSVAAVGKNIEkfgedrLATWRGRNVGVVFQ----FFQL 98
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA------PCALRGRKIATIMQnprsAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 LPTLTVvenimlpmdfcHFLPTSKRRGRA------MELLEKLSIG---RYADNLPADLSGGQQQRAAIARALANDPPIIV 169
Cdd:PRK10418 95 LHTMHT-----------HARETCLALGKPaddatlTAALEAVGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 170 ADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHERD-LSRHFTRVVELSDGRILSQSEV 229
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGvVARLADDVAVMSHGRIVEQGDV 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-211 |
3.61e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.30 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSYDTPTGQFL-----ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkFGE 78
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 79 DRlatWRGRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGR-YADNLPADLSGGQQQRA 155
Cdd:PRK15112 82 YS---YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHERDLSRH 211
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKH 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-221 |
4.61e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSksYDTPTGQFLaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAavgkniekfgedrlatwR 85
Cdd:COG4178 363 LALEDLT--LRTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-----------------R 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GRNVGVVFqffqL-----LPTLTVVENIMLPMDfchflPTSKRRGRAMELLEKLSIGRYADNL--PAD----LSGGQQQR 154
Cdd:COG4178 423 PAGARVLF----LpqrpyLPLGTLREALLYPAT-----AEAFSDAELREALEAVGLGHLAERLdeEADwdqvLSLGEQQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 155 AAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGlAVEGKAVAMVTHERDLSRHFTRVVELSDG 221
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-204 |
7.20e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.39 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 28 IDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkFGEDRLAT---WRGRNVGVVfqffqllPTLTV 104
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-FQRDSIARgllYLGHAPGIK-------TTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 105 VENImlpmdfcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDE 184
Cdd:cd03231 91 LENL-------RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 1084922189 185 VIELFAGLAVEGKAVAMVTH 204
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
38-229 |
1.09e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 38 LAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgeDRLATWRgRNVGVVFQFF--QLLPTlTVVENIML-PMDF 114
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVR-KFVGLVFQNPddQIFSP-TVEQDIAFgPINL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 115 ChfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAV 194
Cdd:PRK13652 108 G--LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 1084922189 195 E-GKAVAMVTHERDLSRHFTRVVELSD-GRILSQSEV 229
Cdd:PRK13652 186 TyGMTVIFSTHQLDLVPEMADYIYVMDkGRIVAYGTV 222
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-208 |
1.46e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 3 PSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSvaavgknIEKFGEDRla 82
Cdd:PRK09544 2 TSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 twrgrnVGVVFQFFQLLPTLTV-VENIMLpmdfchfLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARAL 161
Cdd:PRK09544 69 ------IGYVPQKLYLDTTLPLtVNRFLR-------LRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDL 208
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHL 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-204 |
1.54e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.63 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI----DTPTR--GSVAAVGKNIEKFGEDRLAtwrgRNVGVVFQFFQL 98
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiyDSKIKvdGKVLYFGKDIFQIDAIKLR----KEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 LPTLTVVENIMLPMDfCHFLPTSKRRGRAME-LLEKLSIGRYAD---NLPAD-LSGGQQQRAAIARALANDPPIIVADEP 173
Cdd:PRK14246 102 FPHLSIYDNIAYPLK-SHGIKEKREIKKIVEeCLRKVGLWKEVYdrlNSPASqLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190
....*....|....*....|....*....|.
gi 1084922189 174 TGNLDSRTSDEVIELFAGLAVEgKAVAMVTH 204
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSH 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-220 |
1.80e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIdTPT---RGSVAAVGKNIeKFG 77
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVK----ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEEL-QAS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 78 EDRLATWRGrnVGVVFQFFQLLPTLTVVENIML---PMDFcHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQR 154
Cdd:PRK13549 75 NIRDTERAG--IAIIHQELALVKELSVLENIFLgneITPG-GIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 155 AAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDlsrhftRVVELSD 220
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLN------EVKAISD 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-207 |
2.00e-18 |
|
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: 83.34 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI--DTPTRGSVAAVGKNIEKFGedrLA 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASN---IR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 TWRGRNVGVVFQFFQLLPTLTVVENIMLPMDFCH---FLPTSKRRGRAMELLEKLSIGRYADNLP-ADLSGGQQQRAAIA 158
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLGNEITLpggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1084922189 159 RALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERD 207
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLN 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-204 |
3.13e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrLATWRGRNVGVVFQFFQLLPTLTVVE 106
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 107 NIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVI 186
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
|
170
....*....|....*...
gi 1084922189 187 ELFAGLAVEGKAVAMVTH 204
Cdd:PRK10895 178 RIIEHLRDSGLGVLITDH 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-227 |
4.01e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.45 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKS-TLVNVMTGIDTP----TRGSVAAVGKNIEK 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 76 FGEDRLATWRGRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI----GRYADnLPADLSG 149
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQepMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaaKRLTD-YPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 150 GQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHERDLSRHFT-RVVELSDGRILSQS 227
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLAdRVAVMQNGRCVEQN 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-221 |
1.91e-17 |
|
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: 77.28 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 3 PSLLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGidtptRGSVAAVGKNIEKFGEDRLA 82
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-----RKTAGVITGEILINGRPLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 TWRgRNVGVVFQFFQLLPTLTVVENIMLpmdfchflpTSKRRGramelleklsigryadnlpadLSGGQQQRAAIARALA 162
Cdd:cd03232 76 NFQ-RSTGYVEQQDVHSPNLTVREALRF---------SALLRG---------------------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 163 NDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE--RDLSRHFTRVVELSDG 221
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-204 |
2.03e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTL---VNVMTGI--DTPTRGSVAAVGKNIEK 75
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsINRMNDLnpEVTITGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 76 FGEDRLATwrGRNVGVVFQFFQLLPtLTVVENIMLPMDfchfLPTSKRRGRAMELLEKLSIG---------RYADNLPAd 146
Cdd:PRK14239 77 PRTDTVDL--RKEIGMVFQQPNPFP-MSIYENVVYGLR----LKGIKDKQVLDEAVEKSLKGasiwdevkdRLHDSALG- 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTH 204
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK-DDYTMLLVTR 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-223 |
2.39e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 3 PSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgedRLA 82
Cdd:PRK15439 9 PPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-----RLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 83 TWRGRNVGV--VFQFFQLLPTLTVVENIMLPmdfchfLPTSKRRGRAME-LLEKLSIGRYADNLPADLSGGQQQRAAIAR 159
Cdd:PRK15439 80 PAKAHQLGIylVPQEPLLFPNLSVKENILFG------LPKRQASMQKMKqLLAALGCQLDLDSSAGSLEVADRQIVEILR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 160 ALANDPPIIVADEPTGNLdsrTSDEVIELFA---GLAVEGKAVAMVTHE----RDLSrhfTRVVELSDGRI 223
Cdd:PRK15439 154 GLMRDSRILILDEPTASL---TPAETERLFSrirELLAQGVGIVFISHKlpeiRQLA---DRISVMRDGTI 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-204 |
8.78e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.74 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLV---NVMTGIDTPTR--GSVAAVGKNIEKFGEDRLATwrGRNVGVVFQ 94
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFRveGKVTFHGKNLYAPDVDPVEV--RRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 95 FFQLLPTlTVVENIMLPMDFCHFlptskrRGRAMELLEKlSIGRYA------DNLPAD---LSGGQQQRAAIARALANDP 165
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARINGY------KGDMDELVER-SLRQAAlwdevkDKLKQSglsLSGGQQQRLCIARAIAVQP 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1084922189 166 PIIVADEPTGNLDSRTSDEVIELFAGLaVEGKAVAMVTH 204
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTH 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-223 |
9.94e-17 |
|
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: 78.90 E-value: 9.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDtPTGQfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedRLATWR 85
Cdd:TIGR01257 929 VCVKNLVKIFE-PSGR-PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVR 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTLTVVEnimlpmdfcHFLPTSKRRGRAME--------LLEKLSIGRYADNLPADLSGGQQQRAAI 157
Cdd:TIGR01257 1003 -QSLGMCPQHNILFHHLTVAE---------HILFYAQLKGRSWEeaqlemeaMLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 158 ARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAvEGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLgDRIAIISQGRL 1138
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-204 |
1.31e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWRGRNVGVVFQFfqllPTLt 103
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSF----PVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 vVENIMLPMDFCHF----LPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:PRK15056 97 -VEDVVMMGRYGHMgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*
gi 1084922189 180 RTSDEVIELFAGLAVEGKAVAMVTH 204
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTH 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-206 |
2.54e-16 |
|
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: 77.28 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtPTGQFLaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTptrgsvaavgkniEKFGEDRLATwrGR 87
Cdd:TIGR03719 7 MNRVSKVV--PPKKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-------------DFNGEARPQP--GI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIM---------------LPMDFC----HFLPTSKRRGRAMELLE---------KLSIGRY 139
Cdd:TIGR03719 69 KVGYLPQEPQLDPTKTVRENVEegvaeikdaldrfneISAKYAepdaDFDKLAAEQAELQEIIDaadawdldsQLEIAMD 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 140 ADNLP------ADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSD---EVIELFAGlavegkAVAMVTHER 206
Cdd:TIGR03719 149 ALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwleRHLQEYPG------TVVAVTHDR 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-223 |
4.10e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.07 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLV---NVMTGIDTPTR--GSVAAVGKNI--EKFGEDR 80
Cdd:PRK14258 10 VNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclNRMNELESEVRveGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LAtwrgRNVGVVFQFFQLLPtLTVVENIMLPMDFCHFLPTSKRRG------RAMELLEKLSIGRYADNLpaDLSGGQQQR 154
Cdd:PRK14258 86 LR----RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDivesalKDADLWDEIKHKIHKSAL--DLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 155 AAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGK-AVAMVTHE-RDLSR--HFTRVVELSDGRI 223
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNlHQVSRlsDFTAFFKGNENRI 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-180 |
8.65e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.91 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYDTPTGQfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgRN 88
Cdd:TIGR00958 482 QDVSFSYPNRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH----RQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQFFQLLpTLTVVENIMLPMDFChflPTSKRRGRAMELLEKLSIGRYADNLPAD-------LSGGQQQRAAIARAL 161
Cdd:TIGR00958 557 VALVGQEPVLF-SGSVRENIAYGLTDT---PDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARAL 632
|
170
....*....|....*....
gi 1084922189 162 ANDPPIIVADEPTGNLDSR 180
Cdd:TIGR00958 633 VRKPRVLILDEATSALDAE 651
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-192 |
1.76e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.07 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIdTPTRGSVAAvgkniEKFGEDRLATW 84
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTA-----DRMRFDDIDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 R----------GRNVGVVFQFFQ--LLPTLTVVENIMlpmdfcHFLP--TSK---------RRGRAMELLEKLSIGRYAD 141
Cdd:PRK15093 77 RlsprerrklvGHNVSMIFQEPQscLDPSERVGRQLM------QNIPgwTYKgrwwqrfgwRKRRAIELLHRVGIKDHKD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 142 ---NLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGL 192
Cdd:PRK15093 151 amrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRL 204
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-226 |
2.15e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.21 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRG-----SVAAVGKNIekFGEDRLATWRgRNVGVVFQFFQLL 99
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFR-RRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PtLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI-----GRYADNlPADLSGGQQQRAAIARALANDPPIIVADEPT 174
Cdd:PRK14271 114 P-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavkDRLSDS-PFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 175 GNLDSRTSDEVIELFAGLAvEGKAVAMVTHE-RDLSRHFTRVVELSDGRILSQ 226
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLA-DRLTVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-220 |
2.15e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.03 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSksYDTPTGQFLaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGidtptrgsvaavgkniekfgedrLATWR 85
Cdd:cd03223 1 IELENLS--LATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-----------------------LWPWG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 GRNVGvvfqffqlLPTLtvvENIMlpmdfchFLPtskRRGramelleKLSIGRYADNL--PAD--LSGGQQQRAAIARAL 161
Cdd:cd03223 55 SGRIG--------MPEG---EDLL-------FLP---QRP-------YLPLGTLREQLiyPWDdvLSGGEQQRLAFARLL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGlavEGKAVAMVTHERDLSRHFTRVVELSD 220
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKE---LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-224 |
2.25e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 35 GDFLAIVGKSGSGKSTLVNVMTG--IDTPTRGSVAAVGKNIEKFGEDRlatwrgrnVGVVFQFFQLLPTLTVVENIMlpm 112
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQILKR--------TGFVTQDDILYPHLTVRETLV--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 113 dFCHFLptskRRGRAMELLEKLSIgryADNLPADL------------------SGGQQQRAAIARALANDPPIIVADEPT 174
Cdd:PLN03211 163 -FCSLL----RLPKSLTKQEKILV---AESVISELgltkcentiignsfirgiSGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 175 GNLDSRTSDEVIELFAGLAVEGKAVAMVTHE--RDLSRHFTRVVELSDGRIL 224
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCL 286
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-223 |
2.27e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 14 SYDTPTGQfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPT-------RGSVAAVGKniekfgedrlATWrg 86
Cdd:PLN03232 623 SWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAetssvviRGSVAYVPQ----------VSW-- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 87 rnvgvVFQffqllptLTVVENIMLPMDFchflpTSKRRGRAMELL------------EKLSIGRYADNLpadlSGGQQQR 154
Cdd:PLN03232 690 -----IFN-------ATVRENILFGSDF-----ESERYWRAIDVTalqhdldllpgrDLTEIGERGVNI----SGGQKQR 748
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 155 AAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:PLN03232 749 VSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-204 |
4.20e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYdtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedrlatw 84
Cdd:TIGR01257 1937 ILRLNELTKVY--SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT--------- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 rgrNVGVVFQFFQLLPTLTVVENIMLPMDfcHFLPTSKRRGRAMELLEK--------LSIGRYADNLPADLSGGQQQRAA 156
Cdd:TIGR01257 2006 ---NISDVHQNMGYCPQFDAIDDLLTGRE--HLYLYARLRGVPAEEIEKvanwsiqsLGLSLYADRLAGTYSGGNKRKLS 2080
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1084922189 157 IARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH 204
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-178 |
4.42e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.81 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfGEDRLAtwrgRNVGVVF-QFFQLLPTL 102
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFA----RRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 103 TVVENimlpmdfchF--------LPTSKRRGRAMELLEKLSIGRYADNlPA-DLSGGQQQRAAIARALANDPPIIVADEP 173
Cdd:COG4586 112 PAIDS---------FrllkaiyrIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
....*
gi 1084922189 174 TGNLD 178
Cdd:COG4586 182 TIGLD 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
8-174 |
8.87e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLATWR-- 85
Cdd:NF033858 4 LEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 ------GRNvgvvfqffqLLPTLTVVENImlpmDFchF-----LPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQR 154
Cdd:NF033858 80 ympqglGKN---------LYPTLSVFENL----DF--FgrlfgQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQK 144
|
170 180
....*....|....*....|
gi 1084922189 155 AAIARALANDPPIIVADEPT 174
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPT 164
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-202 |
1.03e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 1 MSPSLLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDR 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 LATwrgRNVGVVFQFFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYadNLPADLSGGQQQRAAIARA 160
Cdd:PRK11614 77 IMR---EAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRI--QRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMV 202
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-224 |
1.05e-14 |
|
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: 70.22 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 23 LALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrLATWRgRNVGVVFQffqlLPTL 102
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SRISIIPQ----DPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 103 ---TVVENImlpmDFCHFLPTSKRrgraMELLEKLSIGRYADNLP-----------ADLSGGQQQRAAIARALANDPPII 168
Cdd:cd03244 90 fsgTIRSNL----DPFGEYSDEEL----WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 169 VADEPTGNLDSRTsDEVI-----ELFAglaveGKAVAMVTHERDLSRHFTRVVELSDGRIL 224
Cdd:cd03244 162 VLDEATASVDPET-DALIqktirEAFK-----DCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-181 |
1.07e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTptgQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgR 87
Cdd:PRK10790 343 IDNVSFAYRD---DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR----Q 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTlTVVENIMLPMDFchflptskRRGRAMELLEKLSIGRYADNLPA-----------DLSGGQQQRAA 156
Cdd:PRK10790 416 GVAMVQQDPVVLAD-TFLANVTLGRDI--------SEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLA 486
|
170 180
....*....|....*....|....*
gi 1084922189 157 IARALANDPPIIVADEPTGNLDSRT 181
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGT 511
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-221 |
2.02e-14 |
|
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: 69.67 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 11 VSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgEDRLATWRGRNVG 90
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNES---EPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 91 VVFQFFQ--LLPTLTVVENIMLPMdfchflPTSKRRGRAmeLLEKLSIGRYADNLP-----------ADLSGGQQQRAAI 157
Cdd:cd03290 80 SVAYAAQkpWLLNATVEENITFGS------PFNKQRYKA--VTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084922189 158 ARALANDPPIIVADEPTGNLDSRTSDEVIE--LFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDG 221
Cdd:cd03290 152 ARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-223 |
2.19e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIE--------KFGEDRLATWRgRNVGvvfqFFql 98
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKKGMAYITESR-RDNG----FF-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 lPTLTVVENimlpMDFCHFLPTSKRRGrAMELLEKLSIGRYADNLPAD--------------LSGGQQQRAAIARALAND 164
Cdd:PRK09700 354 -PNFSIAQN----MAISRSLKDGGYKG-AMGLFHEVDEQRTAENQRELlalkchsvnqniteLSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 165 PPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE-RDLSRHFTRVVELSDGRI 223
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-204 |
3.44e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI--------DTPTRGSVAAVgKNIeKFGEDRlatwrgrnvGVVF-- 93
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGEVCRF-KDI-RDSEAL---------GIVIih 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 94 QFFQLLPTLTVVENImlpmdfchFL--PTSKR--------RGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN 163
Cdd:NF040905 85 QELALIPYLSIAENI--------FLgnERAKRgvidwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH 204
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
25-230 |
4.37e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.74 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGkniEKFGEDRLATWRgRNVGVVFQF-FQLLPTLT 103
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLR-RKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 VVENIMLPMDfCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSD 183
Cdd:PRK13642 99 VEDDVAFGME-NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1084922189 184 EVIELFAGLAVEGK-AVAMVTHERDLSRHFTRVVELSDGRILSQSEVS 230
Cdd:PRK13642 178 EIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPS 225
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-181 |
4.74e-14 |
|
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: 70.62 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDtPTGQFLAltDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLatwR 85
Cdd:COG5265 358 VRFENVSFGYD-PERPILK--GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---R 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTlTVVENImlpmdfchflptskRRGRA-------MELLEKLSIGRYADNLPA-----------DL 147
Cdd:COG5265 432 -AAIGIVPQDTVLFND-TIAYNI--------------AYGRPdaseeevEAAARAAQIHDFIESLPDgydtrvgerglKL 495
|
170 180 190
....*....|....*....|....*....|....
gi 1084922189 148 SGGQQQRAAIARALANDPPIIVADEPTGNLDSRT 181
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-172 |
8.32e-14 |
|
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: 69.83 E-value: 8.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTGQ--FlALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfgEDRLATWR 85
Cdd:COG4615 330 LRGVTYRYPGEDGDegF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTLTVVENIMLPMDFCHFLptskrrgRAMELLEKLSI--GRYADNlpaDLSGGQQQRAAIARALAN 163
Cdd:COG4615 406 -QLFSAVFSDFHLFDRLLGLDGEADPARARELL-------ERLELDHKVSVedGRFSTT---DLSQGQRKRLALLVALLE 474
|
....*....
gi 1084922189 164 DPPIIVADE 172
Cdd:COG4615 475 DRPILVFDE 483
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-205 |
1.18e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKS-TLVNVMTGIDTPtrGSVAAVGK-----------N 72
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA--GGLVQCDKmllrrrsrqviE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 73 IEKFGEDRLATWRGRNVGVVFQ--FFQLLPTLTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSI-------GRYadnl 143
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaqtilSRY---- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 144 PADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVE-GKAVAMVTHE 205
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHD 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-174 |
1.25e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.38 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkfGEDrLATwRgRNVGVVFQFFQLL 99
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--AGD-IAT-R-RRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 100 PTLTVVENIMLpmdfcH---F-LPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPT 174
Cdd:NF033858 352 GELTVRQNLEL-----HarlFhLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-226 |
3.01e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.79 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIdTPTRGSVAAVGKNIEKFGEDRLATWRG------RNVGV--VFQFF 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRAylsqqqSPPFAmpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 97 QL-LPTLTVVENImlpmdfchflptskrRGRAMELLEKLSIgryADNLPAD---LSGGQQQRAAIARAL-----ANDPP- 166
Cdd:COG4138 91 ALhQPAGASSEAV---------------EQLLAQLAEALGL---EDKLSRPltqLSGGEWQRVRLAAVLlqvwpTINPEg 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 167 -IIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHerDLS---RHFTRVVELSDGRILSQ 226
Cdd:COG4138 153 qLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSH--DLNhtlRHADRVWLLKQGKLVAS 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-187 |
3.13e-13 |
|
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: 68.40 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKniekfgedrlatwrgrnVGVVFQFFQLLPTlTV 104
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 105 VENIMLPMDFCHFLPTSKRrgRAMELLEKLSIGRYADNLP-----ADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVI--KACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*...
gi 1084922189 180 RTSDEVIE 187
Cdd:TIGR01271 582 VTEKEIFE 589
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-223 |
3.66e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGID--TPTRGSVAAVGKNIEKFG-EDRLAtwRGrnVGVVFQ------- 94
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSpDERAR--AG--IFLAFQypveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 95 --FFQLLptLTVVENIML-PMDFCHFLPTSKRRGRAMELLEKLsIGRYADnlpADLSGGQQQRAAIARALANDPPIIVAD 171
Cdd:COG0396 92 vsVSNFL--RTALNARRGeELSAREFLKLLKEKMKELGLDEDF-LDRYVN---EGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 172 EPtgnlDS-------RTsdeVIELFAGLAVEGKAVAMVTHERDLSRHF--TRVVELSDGRI 223
Cdd:COG0396 166 ET----DSgldidalRI---VAEGVNKLRSPDRGILIITHYQRILDYIkpDFVHVLVDGRI 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-224 |
4.96e-13 |
|
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: 67.54 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSkSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNV--------------MTGIDTPTRGSVAAVG 70
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAlfgaypgkfegnvfINGKPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 71 KNIEKFGEDRlatwrgRNVGVVfqffqllPTLTVVENIMLPM--DFCHF--LPTSKRRGRAMELLEKLSIGRYADNLP-A 145
Cdd:TIGR02633 336 AGIAMVPEDR------KRHGIV-------PILGVGKNITLSVlkSFCFKmrIDAAAELQIIGSAIQRLKVKTASPFLPiG 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 146 DLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHErdlsrhFTRVVELSDgRIL 224
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSE------LAEVLGLSD-RVL 474
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-206 |
1.24e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 23 LALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfgedRLATWRgRNVGVVFQFFQLLPTL 102
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQ-KQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 103 TVVENimlpmdfCHF-LPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRT 181
Cdd:PRK13540 90 TLREN-------CLYdIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....*
gi 1084922189 182 SDEVIELFAGLAVEGKAVAMVTHER 206
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-226 |
1.91e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.30 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 14 SYDtPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPT-------RGSVAAVGKniekfgedrlatwrg 86
Cdd:PLN03130 623 SWD-SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRsdasvviRGTVAYVPQ--------------- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 87 rnVGVVFQffqllptLTVVENIMLPMDFchflpTSKRRGRAMELLeklSIGRYADNLPA-----------DLSGGQQQRA 155
Cdd:PLN03130 687 --VSWIFN-------ATVRDNILFGSPF-----DPERYERAIDVT---ALQHDLDLLPGgdlteigergvNISGGQKQRV 749
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRILSQ 226
Cdd:PLN03130 750 SMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-224 |
2.37e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVN--------------VMTGIDTPTRGSVAAVGKNIEKFGEDRlatwrgRNVGVV 92
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQclfgaypgrwegeiFIDGKPVKIRNPQQAIAQGIAMVPEDR------KRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 93 fqffqllPTLTVVENIMLPM--DFCHF--LPTSKRRGRAMELLEKLSIGRYADNLP-ADLSGGQQQRAAIARALANDPPI 167
Cdd:PRK13549 354 -------PVMGVGKNITLAAldRFTGGsrIDDAAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1084922189 168 IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHErdlsrhFTRVVELSDgRIL 224
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSE------LPEVLGLSD-RVL 476
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-229 |
1.24e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkFGEDRLATWRgRNVGVVFQ------FFQL 98
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALR-QQVATVFQdpeqqiFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 LPTLTV--VENIMLPMDfchflPTSKRRGRAMELLEKlsiGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGN 176
Cdd:PRK13638 95 IDSDIAfsLRNLGVPEA-----EITRRVDEALTLVDA---QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 177 LDSRTSDEVIELFAGLAVEGKAVAMVTHERDLsrhftrVVELSDG-RILSQSEV 229
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL------IYEISDAvYVLRQGQI 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-223 |
1.34e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 26 TDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIeKFGEDRLATwrgrNVGVVF-----QFFQLLP 100
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAI----RAGIMLcpedrKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 101 TLTVVENIMLPmdfC--HFLP------TSKRRGRAMELLEKLSI-GRYADNLPADLSGGQQQRAAIARALANDPPIIVAD 171
Cdd:PRK11288 345 VHSVADNINIS---ArrHHLRagclinNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 172 EPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE-------RDlsrhftRVVELSDGRI 223
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevlgvAD------RIVVMREGRI 474
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-206 |
1.74e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTrgsvaavgkniekFGEDRLATwrGR 87
Cdd:PRK11819 9 MNRVSKVVP---PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEF-------------EGEARPAP--GI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 88 NVGVVFQFFQLLPTLTVVENIML---------------------PMDfcHFLPTSKRRGRAMELLE---------KLSIG 137
Cdd:PRK11819 71 KVGYLPQEPQLDPEKTVRENVEEgvaevkaaldrfneiyaayaePDA--DFDALAAEQGELQEIIDaadawdldsQLEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 138 RYADNLPAD------LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTsdeVIEL------FAGlavegkAVAMVTHE 205
Cdd:PRK11819 149 MDALRCPPWdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLeqflhdYPG------TVVAVTHD 219
|
.
gi 1084922189 206 R 206
Cdd:PRK11819 220 R 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-187 |
1.83e-11 |
|
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: 62.18 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKniekfgedrlatwrgrnVGVVFQFFQLLPTlTV 104
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 105 VENIMLPMDFCHFlpTSKRRGRAMELLEKLSIGRYADNLP-----ADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:cd03291 115 KENIIFGVSYDEY--RYKSVVKACQLEEDITKFPEKDNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
....*...
gi 1084922189 180 RTSDEVIE 187
Cdd:cd03291 193 FTEKEIFE 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-208 |
1.98e-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: 62.88 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 32 LRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVG---KNIEKFgedrlatwRGRnvgVVFQFFQLLP--TLTVVE 106
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdEVLKRF--------RGT---ELQDYFKKLAngEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 107 NI----MLPMDFC----HFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:COG1245 165 KPqyvdLIPKVFKgtvrELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|
gi 1084922189 179 SRTSDEVIELFAGLAVEGKAVAMVTHerDL 208
Cdd:COG1245 245 IYQRLNVARLIRELAEEGKYVLVVEH--DL 272
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-208 |
2.36e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 21 QFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGI--DTPTRGSVAaVGKNieKFGEDRlatwrgrnvgvvfqffql 98
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVD-VPDN--QFGREA------------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 lptlTVVENIMLPMDFchflptskrrGRAMELLeklSIGRYADN-----LPADLSGGQQQRAAIARALANDPPIIVADEP 173
Cdd:COG2401 101 ----SLIDAIGRKGDF----------KDAVELL---NAVGLSDAvlwlrRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1084922189 174 TGNLDSRTSDEVIELFAGLAVEGKAVAMV-THERDL 208
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGITLVVaTHHYDV 199
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-224 |
2.87e-11 |
|
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: 60.62 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGID--TPTRGSVAAVGKNI-EKFGEDRLAtwRGrnvgvVFQFFQLLPT 101
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDItDLPPEERAR--LG-----IFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 LTVVENImlpmdfcHFLptskrrgramelleklsigRYADnlpADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRT 181
Cdd:cd03217 89 IPGVKNA-------DFL-------------------RYVN---EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1084922189 182 SDEVIELFAGLAVEGKAVAMVTHERDLSRHF--TRVVELSDGRIL 224
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIV 184
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-208 |
3.88e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 32 LRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVG---KNIEKFGEDRLATW----RGRNVGVVF--QFFQLLPTL 102
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVLKRFRGTELQNYfkklYNGEIKVVHkpQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 103 ---TVVEnimlpmdfchFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:PRK13409 176 fkgKVRE----------LLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*....
gi 1084922189 180 RTSDEVIELFAGLAvEGKAVAMVTHerDL 208
Cdd:PRK13409 246 RQRLNVARLIRELA-EGKYVLVVEH--DL 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-223 |
4.26e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.18 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 28 IDLDLRagdfLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNiekfgedRLATWRGRNVGvvfqffqllpTLTVVEN 107
Cdd:PLN03073 532 IDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-------RMAVFSQHHVD----------GLDLSSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 108 IMLPMDFCH-FLPTSKRRGRamelLEKLSI-GRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDsrtSDEV 185
Cdd:PLN03073 591 PLLYMMRCFpGVPEQKLRAH----LGSFGVtGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAV 663
|
170 180 190
....*....|....*....|....*....|....*....
gi 1084922189 186 IELFAGLAVEGKAVAMVTHERDL-SRHFTRVVELSDGRI 223
Cdd:PLN03073 664 EALIQGLVLFQGGVLMVSHDEHLiSGSVDELWVVSEGKV 702
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-225 |
4.39e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 4 SLLCLRHVSKSY-DTPTgqflaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaavgkNIEKfgeD--- 79
Cdd:PRK11147 2 SLISIHGAWLSFsDAPL-----LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-----IYEQ---Dliv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 80 -RLATWRGRNV-GVVFQFF--------QLLPTLTVVENIML--PMDfchflPTSKRRGRAMELLEKL------------- 134
Cdd:PRK11147 69 aRLQQDPPRNVeGTVYDFVaegieeqaEYLKRYHDISHLVEtdPSE-----KNLNELAKLQEQLDHHnlwqlenrinevl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 135 -SIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTsdevIELFAGLAVEGK-AVAMVTHERDLSRHF 212
Cdd:PRK11147 144 aQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQgSIIFISHDRSFIRNM 219
|
250
....*....|....
gi 1084922189 213 -TRVVELSDGRILS 225
Cdd:PRK11147 220 aTRIVDLDRGKLVS 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-228 |
5.07e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 32 LRAGDFLAIVGKSGSGKSTLVNVMTGIdTPTRGSVAAVGKNIEKFGEDRLATWRGR---------NVGvVFQFFQL-LPT 101
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYlsqqqtppfAMP-VFQYLTLhQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 LTVVENIMLPMDF-CHFLptskrrgramELLEKL--SIGRyadnlpadLSGGQQQR---AA----IARALANDPPIIVAD 171
Cdd:PRK03695 97 KTRTEAVASALNEvAEAL----------GLDDKLgrSVNQ--------LSGGEWQRvrlAAvvlqVWPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 172 EPTGNLD---SRTSDEVIELFAGLaveGKAVAMVTHerDLS---RHFTRVVELSDGRILSQSE 228
Cdd:PRK03695 159 EPMNSLDvaqQAALDRLLSELCQQ---GIAVVMSSH--DLNhtlRHADRVWLLKQGKLLASGR 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-221 |
5.12e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVM-----TGIDTptrgsvaavgkniekfGEDRLATWRG------RNVGVVF 93
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVIT----------------GGDRLVNGRPldssfqRSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 94 QFFQLLPTLTVVENimlpMDFCHFL--PTSKRRGRAMELLEK----LSIGRYAD---NLPAD-LSGGQQQRAAIARALAN 163
Cdd:TIGR00956 843 QQDLHLPTSTVRES----LRFSAYLrqPKSVSKSEKMEYVEEviklLEMESYADavvGVPGEgLNVEQRKRLTIGVELVA 918
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 164 DPPIIV-ADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE--RDLSRHFTRVVELSDG 221
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsAILFEEFDRLLLLQKG 979
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-223 |
5.36e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.60 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 22 FLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGsvaavgkNIEKFGEdrlatwrgrnVGVVFQFFQLLPT 101
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-------KVDRNGE----------VSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 LTVVENI---MLPMDFchflptSKRRGRAM--ELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGN 176
Cdd:PRK13546 100 LTGIENIefkMLCMGF------KRKEIKAMtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1084922189 177 LDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHF-TRVVELSDGRI 223
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFcTKIAWIEGGKL 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-209 |
6.58e-11 |
|
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: 60.46 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 33 RAGDFLAIVGKSGSGKSTLVNVMTGIDTPtrgsvaavgkNIEKFGE-----DRLATWRGRNVGVVF-------------- 93
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKP----------NLGKFDDppdwdEILDEFRGSELQNYFtkllegdvkvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 94 QFFQLLPTlTVVENIMLpmdfchFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEP 173
Cdd:cd03236 94 QYVDLIPK-AVKGKVGE------LLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1084922189 174 TGNLDSRTSDEVIELFAGLAVEGKAVAMVTHerDLS 209
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDNYVLVVEH--DLA 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-178 |
8.59e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 28 IDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKfGEdrlatwRGRNVGVVFQFFQLLPTLTVVEN 107
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GD------RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 108 ImlpmdfcHFL-PTSKRRGRAM--ELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:PRK13543 103 L-------HFLcGLHGRRAKQMpgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-229 |
9.08e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDLDLRAGDFLAIVGKSGSG--KSTLVNVMTGIDTPTRGSvaavgkniekfgedRLATWRGRNVGVVFQFFQ 97
Cdd:NF000106 24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPW--------------RF*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 98 LLP-------TLTVVENIMLpmdFCHFLPTSKR--RGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPII 168
Cdd:NF000106 90 HRPvr*grreSFSGRENLYM---IGR*LDLSRKdaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 169 VADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSD-GRILSQSEV 229
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDrGRVIADGKV 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-189 |
1.07e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEkFGEDRLATWRGrnVGVVFQFFQLLPTLT 103
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID-FKSSKEALENG--ISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 VVENIML---PMDfCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLdsr 180
Cdd:PRK10982 90 VMDNMWLgryPTK-GMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL--- 165
|
....*....
gi 1084922189 181 TSDEVIELF 189
Cdd:PRK10982 166 TEKEVNHLF 174
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-228 |
3.98e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIE-KFGEDRLATwrgrnvGVVF-----QFFQLLP 100
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLAN------GIVYisedrKRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 101 TLTVVENimlpMDFCHFLPTSKRRGRAMELLEKLSIGRY----------ADNLPADLSGGQQQRAAIARALANDPPIIVA 170
Cdd:PRK10762 344 GMSVKEN----MSLTALRYFSRAGGSLKHADEQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 171 DEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHErdlsrhFTRVVELSDgRILSQSE 228
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSE------MPEVLGMSD-RILVMHE 470
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-202 |
4.17e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 31 DLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAvgkniekfgedrlatwrgrNVGVVF--QFFQLLPTLTVVEni 108
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-------------------DLKISYkpQYISPDYDGTVEE-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 109 MLPMDFCHFLPTSKRRGramELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIEL 188
Cdd:COG1245 421 FLRSANTDDFGSSYYKT---EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170
....*....|....
gi 1084922189 189 FAGLAVEGKAVAMV 202
Cdd:COG1245 498 IRRFAENRGKTAMV 511
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-202 |
4.82e-10 |
|
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: 57.80 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDF-----LAIVGKSGSGKSTLVNVMTGIDTPTRGsvaavgkNIEKFGEDrlatwrgrnVGVVFQFFQLL 99
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEG-------DIEIELDT---------VSYKPQYIKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 100 PTLTVVENIMLPMDFCHFLPTSKrrgraMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:cd03237 74 YEGTVRDLLSSITKDFYTHPYFK-----TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180
....*....|....*....|...
gi 1084922189 180 RTSDEVIELFAGLAVEGKAVAMV 202
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFV 171
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-186 |
1.00e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.80 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 13 KSYDTPTGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFgedRLATWRGRnVGVV 92
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-LAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 93 FQffqlLPTL---TVVENIMLpmdfchflptsKRRGRAMELLEKlsIGRYAD------NLPAD-----------LSGGQQ 152
Cdd:PRK10789 395 SQ----TPFLfsdTVANNIAL-----------GRPDATQQEIEH--VARLASvhddilRLPQGydtevgergvmLSGGQK 457
|
170 180 190
....*....|....*....|....*....|....
gi 1084922189 153 QRAAIARALANDPPIIVADEPTGNLDSRTSDEVI 186
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQIL 491
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-231 |
1.01e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFG-EDRLATwrgrnvGVVFqffqlLPTLTVV 105
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLAR------GLVY-----LPEDRQS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 106 ENIML--PM--DFC----HFLPTSKRRGRAMELLEKL--SIG---RYADNLPADLSGGQQQRAAIARALANDPPIIVADE 172
Cdd:PRK15439 350 SGLYLdaPLawNVCalthNRRGFWIKPARENAVLERYrrALNikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 173 PTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFT-RVVELSDGRI---LSQSEVSV 231
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMAdRVLVMHQGEIsgaLTGAAINV 492
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-206 |
1.13e-09 |
|
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: 57.64 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 9 RHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaavgknieKFGEdrlaTWRgrn 88
Cdd:TIGR03719 326 ENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI--------EIGE----TVK--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 89 VGVVFQFFQLL-PTLTVVENIMLPMDfchFLPTSKRR--GRAMelleklsIGRY----ADN--LPADLSGGQQQRAAIAR 159
Cdd:TIGR03719 387 LAYVDQSRDALdPNKTVWEEISGGLD---IIKLGKREipSRAY-------VGRFnfkgSDQqkKVGQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1084922189 160 ALANDPPIIVADEPTGNLDS---RTSDEVIELFAGLAVegkavaMVTHER 206
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVetlRALEEALLNFAGCAV------VISHDR 500
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-226 |
1.33e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.72 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgRNVGVVFQFFQLLPTLTV 104
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 105 VENIMLPMDFCH-----FlpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDS 179
Cdd:PRK10575 103 RELVAIGRYPWHgalgrF--GAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1084922189 180 RTSDEVIELFAGLAVE-GKAVAMVTHERDL-SRHFTRVVELSDGRILSQ 226
Cdd:PRK10575 181 AHQVDVLALVHRLSQErGLTVIAVLHDINMaARYCDYLVALRGGEMIAQ 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-223 |
1.60e-09 |
|
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: 57.65 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 23 LALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgrnvgvvFQFfQLLPTL 102
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR----------FKI-TIIPQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 103 TVVENIMLPMDFCHFLPTSKRRgrAMELLEKLSIGRYADNLPA-----------DLSGGQQQRAAIARALANDPPIIVAD 171
Cdd:TIGR00957 1369 PVLFSGSLRMNLDPFSQYSDEE--VWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 172 EPTGNLDSRTsDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:TIGR00957 1447 EATAAVDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-223 |
2.27e-09 |
|
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: 55.50 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLAtwrgRNVGVVFQFfqllPTL- 102
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR----SSLTIIPQD----PTLf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 103 --TVVENIMlPMDfchflptskrRGRAMELLEKLSIGRYADNLpadlSGGQQQRAAIARALANDPPIIVADEPTGNLDSR 180
Cdd:cd03369 95 sgTIRSNLD-PFD----------EYSDEEIYGALRVSEGGLNL----SQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1084922189 181 TS---DEVI-ELFAglaveGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:cd03369 160 TDaliQKTIrEEFT-----NSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-223 |
3.46e-09 |
|
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: 56.49 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 16 DTPTgqflaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGkniekfgedrlatwrgrNVGVVFQF 95
Cdd:TIGR00957 650 LPPT-----LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------------SVAYVPQQ 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 96 fQLLPTLTVVENIML-----------PMDFCHFLPTskrrgraMELL---EKLSIGRYADNLpadlSGGQQQRAAIARAL 161
Cdd:TIGR00957 708 -AWIQNDSLRENILFgkalnekyyqqVLEACALLPD-------LEILpsgDRTEIGEKGVNL----SGGQKQRVSLARAV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 162 ANDPPIIVADEPTGNLDSRTSDEVIELFAGL--AVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-223 |
3.97e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDTPTgqfLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIekfGEDRLATWR 85
Cdd:PRK10522 323 LELRNVTFAYQDNG---FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 86 gRNVGVVFQFFQLLPTLTVVENimlpmdfchFLPTSKRRGRAMELLE---KLSI--GRYADnlpADLSGGQQQRAAIARA 160
Cdd:PRK10522 397 -KLFSAVFTDFHLFDQLLGPEG---------KPANPALVEKWLERLKmahKLELedGRISN---LKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084922189 161 LANDPPIIVADEPTGNLDSRTSDEVI-ELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-231 |
8.30e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 27 DIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaaVGKNIEKFGEDRLATWRGRnVGVVFQFFQL-------- 98
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI--IINDSHNLKDINLKWWRSK-IGVVSQDPLLfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 99 -------LPTLTVVEN-----------------------------IMLPMDFCHFLPTSK-----RRGRAMELLEKLSIG 137
Cdd:PTZ00265 480 ikyslysLKDLEALSNyynedgndsqenknkrnscrakcagdlndMSNTTDSNELIEMRKnyqtiKDSEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 138 RYADNLP-----------ADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGL-AVEGKAVAMVTHE 205
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHR 639
|
250 260
....*....|....*....|....*.
gi 1084922189 206 RDLSRHFTRVVELSDGRILSQSEVSV 231
Cdd:PTZ00265 640 LSTIRYANTIFVLSNRERGSTVDVDI 665
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-221 |
1.24e-08 |
|
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: 52.71 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNvmTGIDTPTRGSVAavgKNIEKFGEDRLAtwrgrnvgvvfqFFQLLPTLT 103
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLI---SFLPKFSRNKLI------------FIDQLQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 VVEnimlpmdfchflptskrrgramelLEKLSIGRYAdnlpADLSGGQQQRAAIARALANDPP--IIVADEPTGNLDSRT 181
Cdd:cd03238 73 DVG------------------------LGYLTLGQKL----STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1084922189 182 SDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDG 221
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-178 |
1.55e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 32 LRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaavgkniekfgedrlatwrGRNVGVVF--QFFQLLPTLTVVENIM 109
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------------DPELKISYkpQYIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 110 -LPMDF-CHFLPTskrrgramELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:PRK13409 423 sITDDLgSSYYKS--------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-226 |
1.57e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGiDTP---------TRGSVAAVGKNIEKFGEDRLATWRGrnvgVVFQF 95
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTgggaprgarVTGDVTLNGEPLAAIDAPRLARLRA----VLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 96 FQLLPTLTVVENIML---PMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALAN--------- 163
Cdd:PRK13547 92 AQPAFAFSAREIVLLgryPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGK-AVAMVTHERDLS-RHFTRVVELSDGRILSQ 226
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlGVLAIVHDPNLAaRHADRIAMLADGAIVAH 236
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-205 |
2.11e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTP--TRGSVAAVG--KNIEKFGedrlatwrgRNVGVVFQFFQLLP 100
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpKKQETFA---------RISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 101 TLTVVENIMlpmdFCHFLPTSKRRGR---------AMELLEKLSIGRYADNLPA--DLSGGQQQRAAIARALANDPPIIV 169
Cdd:PLN03140 967 QVTVRESLI----YSAFLRLPKEVSKeekmmfvdeVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190
....*....|....*....|....*....|....*.
gi 1084922189 170 ADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE 205
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-223 |
4.48e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEK----------FG---EDRLATWRGRNVG 90
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgFAlvtEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 91 VVFQffqllptlTVVENIMLPMDFCHFLPTSKRRGRAMELLEKLSIGRYADNLP-ADLSGGQQQRAAIARALANDPPIIV 169
Cdd:PRK10982 343 IGFN--------SLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1084922189 170 ADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHER-DLSRHFTRVVELSDGRI 223
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLV 469
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-204 |
4.83e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGID--TPTRGSVAAVGKNIEKFG-EDRlatwRGRNVGVVFQFFQLLPT 101
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSpEDR----AGEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 ltvVENIMlpmdfchFLPTS---KRRGRAMELLEKLSIGRYAD------NLPADL---------SGGQQQRAAIARALAN 163
Cdd:PRK09580 93 ---VSNQF-------FLQTAlnaVRSYRGQEPLDRFDFQDLMEekiallKMPEDLltrsvnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1084922189 164 DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTH 204
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-178 |
6.10e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 6.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSY-DTPTgqflaLTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGiDTPT------------RGSvaavGKNIe 74
Cdd:PRK10938 263 LNNGVVSYnDRPI-----LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrRGS----GETI- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 75 kfgedrlatWR-GRNVGVVFQFFQL-LPTLTVVENIMLPMDF----CHFLPTSKRRGRAMELLEKLSI-GRYADNLPADL 147
Cdd:PRK10938 332 ---------WDiKKHIGYVSSSLHLdYRVSTSVRNVILSGFFdsigIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSL 402
|
170 180 190
....*....|....*....|....*....|.
gi 1084922189 148 SGGQQQRAAIARALANDPPIIVADEPTGNLD 178
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-187 |
1.36e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.36e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSrTSDEVIE 187
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIE 1398
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
25-224 |
1.70e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGID--TPTRGSVAAVGKNI-EKFGEDRlatwrgRNVGvVFQFFQLLPT 101
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESIlDLEPEER------AHLG-IFLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 102 LTVVENimlpMDFCHFLPTSKRRGRAMELLEKLSIGRYAD---------------NLPADLSGGQQQRAAIARALANDPP 166
Cdd:CHL00131 96 IPGVSN----ADFLRLAYNSKRKFQGLPELDPLEFLEIINeklklvgmdpsflsrNVNEGFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 167 IIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRH----FTRVveLSDGRIL 224
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYikpdYVHV--MQNGKII 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-224 |
2.03e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 8 LRHVSKSYDTPTgqFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGidtPTRGSVAAVGKNIEKFG---EDRLATW 84
Cdd:TIGR00956 62 FRKLKKFRDTKT--FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGVITYDGitpEEIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 85 RGRnvgVVF--QFFQLLPTLTVVENimlpMDFCHFLPTSKRRGRAMELLEK-------------LSIGR---YADNLPAD 146
Cdd:TIGR00956 137 RGD---VVYnaETDVHFPHLTVGET----LDFAARCKTPQNRPDGVSREEYakhiadvymatygLSHTRntkVGNDFVRG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVT---HERDLSRHFTRVVELSDGRI 223
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAiyqCSQDAYELFDKVIVLYEGYQ 289
|
.
gi 1084922189 224 L 224
Cdd:TIGR00956 290 I 290
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-223 |
4.34e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 6 LCLRHVSKSYDTPTgqflALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSV-----AAVG----KNIEKF 76
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenANIGyyaqDHAYDF 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 77 GEDR-LATWRGrnvgvvfQFFQLLPTLTVVENIMlpmdfchflptskrrGRAmeLLEKLSIGRYADNlpadLSGGQQQRA 155
Cdd:PRK15064 396 ENDLtLFDWMS-------QWRQEGDDEQAVRGTL---------------GRL--LFSQDDIKKSVKV----LSGGEKGRM 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSrtsdEVIE-LFAGLAVEGKAVAMVTHERDL-SRHFTRVVELSDGRI 223
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDM----ESIEsLNMALEKYEGTLIFVSHDREFvSSLATRIIEITPDGV 513
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-223 |
4.36e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaavgkniekfgedrlatWRGRNVGVVFQFFQLLpTLTV 104
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWIM-NATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 105 VENIMLpmdfchFLPTSKRR----GRAMEL---LEKLS------IGRYADNLpadlSGGQQQRAAIARALANDPPIIVAD 171
Cdd:PTZ00243 738 RGNILF------FDEEDAARladaVRVSQLeadLAQLGggleteIGEKGVNL----SGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1084922189 172 EPTGNLDSRTSDEVI-ELFAGlAVEGKAVAMVTHERDLSRHFTRVVELSDGRI 223
Cdd:PTZ00243 808 DPLSALDAHVGERVVeECFLG-ALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-204 |
6.44e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 40 IVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGEDRLaTWRGRNVGVVFQffqllptLTVVENIMLPMDF---CH 116
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIGHNLGLKLE-------MTVFENLKFWSEIynsAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 117 FLPTSKRRGRAMELLEKLSigryadnlpADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEG 196
Cdd:PRK13541 103 TLYAAIHYFKLHDLLDEKC---------YSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSG 173
|
....*...
gi 1084922189 197 KAVAMVTH 204
Cdd:PRK13541 174 GIVLLSSH 181
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-187 |
9.92e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKNIEKFGedrLATWRgRNVGVVFQffqlLPTL-- 102
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQ----APVLfs 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 103 -TVVENimlpMD-FCHF----LPTSKRRGRAMELLEKLSIGRYADNLPA--DLSGGQQQRAAIARALANDPPIIVADEPT 174
Cdd:PLN03130 1327 gTVRFN----LDpFNEHndadLWESLERAHLKDVIRRNSLGLDAEVSEAgeNFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170
....*....|...
gi 1084922189 175 GNLDSRTsDEVIE 187
Cdd:PLN03130 1403 AAVDVRT-DALIQ 1414
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-204 |
1.01e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 24 ALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVAAVGKniekfgedrlATWRGRNVGVVFQffqllptLT 103
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLNGQ-------LT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 VVENIMLPmDFCHFLPTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSD 183
Cdd:PRK13545 102 GIENIELK-GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180
....*....|....*....|.
gi 1084922189 184 EVIELFAGLAVEGKAVAMVTH 204
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISH 201
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
29-202 |
1.02e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 29 DLDLRAGDFLAIVGKSGSGKSTLVNVMTG------------IDTPTRGSVAAVGKNIEkfgedrlATWRGRNVGVvfqff 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGelpllsgerqsqFSHITRLSFEQLQKLVS-------DEWQRNNTDM----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 97 qLLPT-----LTVVENIMLpmdfchflpTSKRRGRAMELLEKLSIGRYADNLPADLSGGQQQRAAIARALANDPPIIVAD 171
Cdd:PRK10938 91 -LSPGeddtgRTTAEIIQD---------EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190
....*....|....*....|....*....|.
gi 1084922189 172 EPTGNLDSRTSDEVIELFAGLAVEGKAVAMV 202
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
25-223 |
6.57e-06 |
|
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: 45.33 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIdTPTRGSVAAV----GKNIEKFGEdrlaTWRGRNVGVVFQFFQLlP 100
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNVSVEGDihynGIPYKEFAE----KYPGEIIYVSEEDVHF-P 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 101 TLTVVENimlpMDFchflptsKRRGRAMELLEKLSigryadnlpadlsGGQQQRAAIARALANDPPIIVADEPTGNLDSR 180
Cdd:cd03233 97 TLTVRET----LDF-------ALRCKGNEFVRGIS-------------GGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1084922189 181 TSDEVIELFAGLAVEGKAVAMVT---HERDLSRHFTRVVELSDGRI 223
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVSlyqASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
20-219 |
7.02e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 45.34 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 20 GQFLALTDIDL-DLRAGDFLAIVGKSGSGKSTLVNVMTgidtptrgsVAAVGKNIEKFGEDRLATWRGRN---VGVVFQF 95
Cdd:cd03279 12 GPFREEQVIDFtGLDNNGLFLICGPTGAGKSTILDAIT---------YALYGKTPRYGRQENLRSVFAPGedtAEVSFTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 96 fQLLPTLTVVENiMLPMDF-----CHFLPtskrRGRAMELLEklsigRYADNLpadlSGGQQQRAAIARALA-------- 162
Cdd:cd03279 83 -QLGGKKYRVER-SRGLDYdqftrIVLLP----QGEFDRFLA-----RPVSTL----SGGETFLASLSLALAlsevlqnr 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 163 NDPPI--IVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELS 219
Cdd:cd03279 148 GGARLeaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
31-208 |
3.04e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 31 DLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTrgsvaavGKNIEkfgedrlatWRGRNVGVVFQFFqllptltvveniml 110
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPN-------GDNDE---------WDGITPVYKPQYI-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 111 pmdfchflptskrrgramelleklsigryadnlpaDLSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFA 190
Cdd:cd03222 71 -----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170
....*....|....*...
gi 1084922189 191 GLAVEGKAVAMVThERDL 208
Cdd:cd03222 116 RLSEEGKKTALVV-EHDL 132
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-221 |
8.87e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.24 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLV---------------------NVMTGIDTPTRGSVAAVGKNI---EKFGedr 80
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIaidQKTT--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 81 latwrGRN----VGVVFQFFQLLPTLTVVENImlpmdfchflptSKRRGRAMEL-LEKLSIGRYAdnlpADLSGGQQQRA 155
Cdd:cd03270 88 -----SRNprstVGTVTEIYDYLRLLFARVGI------------RERLGFLVDVgLGYLTLSRSA----PTLSGGEAQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 156 AIARALAN--DPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDG 221
Cdd:cd03270 147 RLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPG 214
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-215 |
1.05e-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: 41.82 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 39 AIVGKSGSGKSTLVN----VMTGIDTPTRGSVAAVGKNI---EKFGEDRLATW--RGRNVGVVFQFFQLLPTLtvvenim 109
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIregEVRAQVKLAFEnaNGKKYTITRSLAILENVI------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 110 lpmdFCHflptskrRGRAMELLEkLSIGRyadnlpadLSGGQQQ------RAAIARALANDPPIIVADEPTGNLDSRTSD 183
Cdd:cd03240 99 ----FCH-------QGESNWPLL-DMRGR--------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1084922189 184 ----EVIELFAGLAVEgkAVAMVTHERDLSR---HFTRV 215
Cdd:cd03240 159 eslaEIIEERKSQKNF--QLIVITHDEELVDaadHIYRV 195
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
25-53 |
1.75e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.75e-04
10 20
....*....|....*....|....*....
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVN 53
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-208 |
2.28e-04 |
|
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: 40.42 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMtgidtptrgSVAAVGKNieKFGEDRLATWRGRNVG-VVFQFFQLLPTLt 103
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAI---------GLALGGAQ--SATRRRSGVKAGCIVAaVSAELIFTRLQL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 104 vvenimlpmdfchflptskrrgramelleklsigryadnlpadlSGGQQQRAAIARALA----NDPPIIVADEPTGNLDS 179
Cdd:cd03227 79 --------------------------------------------SGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
170 180
....*....|....*....|....*....
gi 1084922189 180 RTSDEVIELFAGLAVEGKAVAMVTHERDL 208
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPEL 143
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-213 |
2.30e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 5 LLCLRHVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVA-AVGKNIEKFGEDRLAT 83
Cdd:PRK10636 312 LLKMEKVSAGY----GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlAKGIKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 84 WRGRNVgvvfqffqllptltvvenimlPMDfcHFLPTSKRrgramELLEKL-----SIGRYADNLP---ADLSGGQQQRA 155
Cdd:PRK10636 388 LRADES---------------------PLQ--HLARLAPQ-----ELEQKLrdylgGFGFQGDKVTeetRRFSGGEKARL 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 156 AIARALANDPPIIVADEPTGNLDSRTSDEVIElfAGLAVEGkAVAMVTHERDLSRHFT 213
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTE--ALIDFEG-ALVVVSHDRHLLRSTT 494
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
25-53 |
2.93e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 2.93e-04
10 20
....*....|....*....|....*....
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVN 53
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-221 |
3.10e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 145 ADLSGGQQQRAAIARALANDPPII--VADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDLSRHFTRVVELSDG 221
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-206 |
7.58e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 10 HVSKSYdtptGQFLALTDIDLDLRAGDFLAIVGKSGSGKSTLVNVMTGIDTPTRGSVaavgknieKFGEdrlaTWRgrnV 89
Cdd:PRK11819 329 NLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI--------KIGE----TVK---L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 90 GVVFQFFQLL-PTLTVVENImlpmdfchflptskrrgraMELLEKLSIGRYADNLPA-----------------DLSGGQ 151
Cdd:PRK11819 390 AYVDQSRDALdPNKTVWEEI-------------------SGGLDIIKVGNREIPSRAyvgrfnfkggdqqkkvgVLSGGE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1084922189 152 QQRAAIARALANDPPIIVADEPTGNLDS---RTSDEVIELFAGLAVegkavaMVTHER 206
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVetlRALEEALLEFPGCAV------VISHDR 502
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
147-205 |
9.80e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 9.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1084922189 147 LSGGQQQRAAIARALANDPPIIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHE 205
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSE 463
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
147-209 |
1.29e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 1.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084922189 147 LSGGQQQ------RAAIARALANDPPIIVADEPTGNLDS-RTSD--EVIELFAGLAVEGKAVAMVTHERDLS 209
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEdRRTNlkDIIEYSLKDSSDIPQVIMISHHRELL 873
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-53 |
2.20e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.36 E-value: 2.20e-03
10 20
....*....|....*....|....*....
gi 1084922189 25 LTDIDLDLRAGDFLAIVGKSGSGKSTLVN 53
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
38-70 |
2.26e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 38.59 E-value: 2.26e-03
10 20 30
....*....|....*....|....*....|...
gi 1084922189 38 LAIVGKSGSGKSTLVNVMTGidtptrGSVAAVG 70
Cdd:COG3596 42 IALVGKTGAGKSSLINALFG------AEVAEVG 68
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
11-53 |
2.46e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084922189 11 VSKSYDTPTGQFLA----------------------------LTDIDLDLRAGDFLAIVGKSGSGKSTLVN 53
Cdd:COG0178 579 ILKNPDSLTGQYLSgrkripvpkkrrkgngkfltikgarennLKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
148-207 |
4.65e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 4.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 148 SGGQQQRAAIARALANDPPIIVADEPTGNLDSRTsdeVIELFAGLAVEGKAVAMVTHERD 207
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHARE 402
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
39-57 |
4.65e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 35.67 E-value: 4.65e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-221 |
7.37e-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: 37.30 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084922189 131 LEKLSIGRYADNLpadlSGGQQQRAAIARALANDPP--IIVADEPTGNLDSRTSDEVIELFAGLAVEGKAVAMVTHERDL 208
Cdd:TIGR00630 477 LDYLSLSRAAGTL----SGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDT 552
|
90
....*....|...
gi 1084922189 209 SRHFTRVVELSDG 221
Cdd:TIGR00630 553 IRAADYVIDIGPG 565
|
|
| |
