|
Name |
Accession |
Description |
Interval |
E-value |
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
24-264 |
4.37e-61 |
|
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: 202.30 E-value: 4.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 24 QKKQRTIANDIPKILEITINNLSIGYD--KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKK 101
Cdd:COG4988 321 AAPAGTAPLPAAGPPSIELEDVSFSYPggRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 102 LR-FDanfRHDWLKRAIYLGSEPYLFSGSIIDNLLFAS-KYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPG 179
Cdd:COG4988 401 LSdLD---PASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 180 QRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYES 258
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVeQGTHEE 557
|
....*.
gi 2306450510 259 LLKNSP 264
Cdd:COG4988 558 LLAKNG 563
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
39-273 |
7.23e-50 |
|
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: 175.02 E-value: 7.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdaNFRHDWLKR 115
Cdd:COG2274 473 DIELENVSFRYPgdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLR---QIDPASLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AI-YLGSEPYLFSGSIIDNL-LFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAAD 193
Cdd:COG2274 550 QIgVVLQDVFLFSGTIRENItLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 194 KNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKNSPSFKNLINQ 272
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVeDGTHEELLARKGLYAELVQQ 709
|
.
gi 2306450510 273 Q 273
Cdd:COG2274 710 Q 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
35-269 |
2.20e-46 |
|
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: 163.40 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 35 PKILEITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdANFRHD 111
Cdd:COG4987 329 PGGPSLELEDVSFRYPgagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR--DLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 WLKRAIYLGSEPYLFSGSIIDNLLFASKY-DRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAV 190
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 191 AADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKNSPSFKNL 269
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVeQGTHEELLAQNGRYRQL 566
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
39-274 |
1.36e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 161.49 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGY--DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKtLVA-----QQkslaGEISFSDKKLRfdaNFRHD 111
Cdd:COG1132 339 EIEFENVSFSYpgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVN-LLLrfydpTS----GRILIDGVDIR---DLTLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 WLKRAI-YLGSEPYLFSGSIIDNLLFASK-YDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRA 189
Cdd:COG1132 411 SLRRQIgVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 190 VAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAF-----ITEkkavIGPYESLLKNSP 264
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVlddgrIVE----QGTHEELLARGG 566
|
250
....*....|
gi 2306450510 265 SFKNLINQQF 274
Cdd:COG1132 567 LYARLYRLQF 576
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
37-243 |
7.07e-42 |
|
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: 150.90 E-value: 7.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 37 ILEITINNLSIGYD--KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfDANfRHDWLK 114
Cdd:TIGR02857 319 ASSLEFSGVSVAYPgrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-DAD-ADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 115 RAIYLGSEPYLFSGSIIDNLLFASKY-DRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAAD 193
Cdd:TIGR02857 397 QIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2306450510 194 KNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQI 243
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
40-273 |
1.10e-38 |
|
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: 135.74 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY----DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfDANFRhdWLKR 115
Cdd:cd03249 1 IEFKNVSFRYpsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIR-DLNLR--WLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AI-YLGSEPYLFSGSIIDNLLFaSKYDR--KELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAA 192
Cdd:cd03249 78 QIgLVSQEPVLFDGTIAENIRY-GKPDAtdEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKNSPSFKNLIN 271
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVeQGTHDELMAQKGVYAKLVK 236
|
..
gi 2306450510 272 QQ 273
Cdd:cd03249 237 AQ 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
39-261 |
3.38e-38 |
|
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: 134.28 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD--KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTL-----VAQQKSLAGEISFSDKKlrfdanfRHD 111
Cdd:cd03254 2 EIEFENVNFSYDekKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLmrfydPQKGQILIDGIDIRDIS-------RKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 WLKRAIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDK-FGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAV 190
Cdd:cd03254 75 LRSMIGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKeAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2306450510 191 AADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLK 261
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIeEGTHDELLA 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
40-269 |
2.67e-36 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 129.27 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDK---PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdaNFRHDWLKRA 116
Cdd:cd03251 1 VEFKNVTFRYPGdgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR---DYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYLGS-EPYLFSGSIIDNLLFA-SKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADK 194
Cdd:cd03251 78 IGLVSqDVFLFNDTVAENIAYGrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 195 NFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKNSPSFKNL 269
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVeRGTHEELLAQGGVYAKL 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
40-273 |
2.87e-36 |
|
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: 129.53 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPLITQ-LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHDWLKRA 116
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDnISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL---ALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 I-YLGSEPYLFSGSIIDNLLFASK-YDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADK 194
Cdd:cd03252 78 VgVVLQENVLFNRSIRDNIALADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 195 NFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIaFITEKKAVI--GPYESLLKNSPSFKNLINQ 272
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRI-IVMEKGRIVeqGSHDELLAENGLYAYLYQL 236
|
.
gi 2306450510 273 Q 273
Cdd:cd03252 237 Q 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
40-250 |
1.16e-35 |
|
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: 125.57 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdaNFRHDWLKRA 116
Cdd:cd03228 1 IEFKNVSFSYPgrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLR---DLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 I-YLGSEPYLFSGSIIDNLLfaskydrkelikifdkfglcsfvsslpdqydsqvgengkwlSPGQRQQIAFGRAVAADKN 195
Cdd:cd03228 78 IaYVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2306450510 196 FYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKK 250
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
39-243 |
2.17e-32 |
|
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: 118.85 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdaNFRHDWLKR 115
Cdd:cd03245 2 RIEFRNVSFSYPnqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR---QLDPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AI-YLGSEPYLFSGSIIDNLLFASKY-DRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAAD 193
Cdd:cd03245 79 NIgYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2306450510 194 KNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQI 243
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRI 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
36-273 |
2.70e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 122.26 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 36 KILEITINNLSI-GYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTL---VAQQKSL--AG-EISFSDKKlrfdan 107
Cdd:PRK11174 346 DPVTIEAEDLEIlSPDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgfLPYQGSLkiNGiELRELDPE------ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 108 frhDWLKRAIYLGSEPYLFSGSIIDNLLFA-SKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAF 186
Cdd:PRK11174 420 ---SWRKHLSWVGQNPQLPHGTLRDNVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLAL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 187 GRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIaFITEKKAVI--GPYESLLKNSP 264
Cdd:PRK11174 497 ARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI-WVMQDGQIVqqGDYAELSQAGG 575
|
....*....
gi 2306450510 265 SFKNLINQQ 273
Cdd:PRK11174 576 LFATLLAHR 584
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
40-244 |
4.47e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.91 E-value: 4.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVaqqkSL----AGEISFSDKKL-RFDAnfrHDWL 113
Cdd:COG4619 1 LELEGLSFRVGgKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA----DLdpptSGEIYLDGKPLsAMPP---PEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIYLGSEPYLFSGSIIDNLLFAS-----KYDRKELIKIFDKFGLCsfvsslPDQYDSQVGEngkwLSPGQRQQIAFGR 188
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFqlrerKFDRERALELLERLGLP------PDILDKPVER----LSGGERQRLALIR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2306450510 189 AVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHkieDLKQSDQIA 244
Cdd:COG4619 144 ALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSH---DPEQIERVA 198
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
35-250 |
7.01e-31 |
|
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: 114.88 E-value: 7.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 35 PKILE--ITINNLSIGY----DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANF 108
Cdd:cd03248 5 PDHLKgiVKFQNVTFAYptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 109 RHDWLKRAIYL-GSEPYLFSGSIIDNLLFASKYDRKELIK-IFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAF 186
Cdd:cd03248 82 EHKYLHSKVSLvGQEPVLFARSLQDNIAYGLQSCSFECVKeAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 187 GRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKK 250
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
40-273 |
8.90e-31 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 121.00 E-value: 8.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDK---PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHDWLKRA 116
Cdd:TIGR01846 456 ITFENIRFRYAPdspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL---AIADPAWLRRQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 I-YLGSEPYLFSGSIIDNLLFAS-KYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADK 194
Cdd:TIGR01846 533 MgVVLQENVLFSRSIRDNIALCNpGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 195 NFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIafITEKKAVI---GPYESLLKNSPSFKNLIN 271
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRI--IVLEKGQIaesGRHEELLALQGLYARLWQ 690
|
..
gi 2306450510 272 QQ 273
Cdd:TIGR01846 691 QQ 692
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-270 |
2.71e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 119.83 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 11 IFAQIDDKNSFSSQKKQRtiandiPKILE--ITINNLSIGY----DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTL 84
Cdd:TIGR00958 454 VFEYLDRKPNIPLTGTLA------PLNLEglIEFQDVSFSYpnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 85 VAQQKSLAGEISFSDKKLRfdaNFRHDWLKRAIYL-GSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLC-SFVSSLP 162
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLV---QYDHHYLHRQVALvGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAhDFIMEFP 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 163 DQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRlaKEKIVLIITHKIEDLKQSDQ 242
Cdd:TIGR00958 605 NGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQ 682
|
250 260
....*....|....*....|....*....
gi 2306450510 243 IAFITEKKAV-IGPYESLLKNSPSFKNLI 270
Cdd:TIGR00958 683 ILVLKKGSVVeMGTHKQLMEDQGCYKHLV 711
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
39-274 |
3.17e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 118.97 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdaNFRHDWLKR 115
Cdd:PRK11176 341 DIEFRNVTFTYpgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR---DYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AIYLGSEP-YLFSGSIIDNLLFAS--KYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAA 192
Cdd:PRK11176 418 QVALVSQNvHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKNSPSFKNLIN 271
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVeRGTHAELLAQNGVYAQLHK 577
|
...
gi 2306450510 272 QQF 274
Cdd:PRK11176 578 MQF 580
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
40-273 |
4.97e-30 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 113.09 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD--KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdaNFRHDWLKRAI 117
Cdd:cd03253 1 IEFENVTFAYDpgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR---EVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 -YLGSEPYLFSGSIIDNLLF----ASKydrKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAA 192
Cdd:cd03253 78 gVVPQDTVLFNDTIGYNIRYgrpdATD---EEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKNSPSFKNLIN 271
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVeRGTHEELLAKGGLYAEMWK 234
|
..
gi 2306450510 272 QQ 273
Cdd:cd03253 235 AQ 236
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-271 |
4.04e-29 |
|
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: 116.38 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 19 NSFSSQKKQRTIANDIPKILEITINNLSIGYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFS 98
Cdd:TIGR01193 455 DSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 99 DKKLrfdANFRHDWLKRAI-YLGSEPYLFSGSIIDNLLFASK--YDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKW 175
Cdd:TIGR01193 535 GFSL---KDIDRHTLRQFInYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 176 LSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLaKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IG 254
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIeQG 690
|
250
....*....|....*..
gi 2306450510 255 PYESLLKNSPSFKNLIN 271
Cdd:TIGR01193 691 SHDELLDRNGFYASLIH 707
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
40-232 |
4.38e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 115.54 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHDWLKRAI 117
Cdd:TIGR02868 335 LELRDLSAGYpgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV---SSLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 -YLGSEPYLFSGSIIDNLLFASK-YDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKN 195
Cdd:TIGR02868 412 sVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 2306450510 196 FYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITH 232
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
39-243 |
1.67e-28 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 108.73 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSD---KKLRfdanfRHDW 112
Cdd:cd03244 2 DIEFKNVSLRYRpnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiSKIG-----LHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 113 LKRAIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAA 192
Cdd:cd03244 77 RSRISIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQI 243
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRI 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
40-246 |
1.26e-27 |
|
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: 105.63 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD------KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSdkklrfdanfrhdwl 113
Cdd:cd03250 1 ISVEDASFTWDsgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAAD 193
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2306450510 194 KNFYIFDEVTSNIDHENAGIILRA--MKRLAKEKIVLIITHKIEDLKQSDQIAFI 246
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVL 200
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
40-250 |
2.92e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 103.40 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDkklrFDANFRHDWLKRAI- 117
Cdd:COG4555 2 IEVENLSKKYgKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG----EDVRKEPREARRQIg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPYLFSG-SIIDNLLFA------SKYDRKELI-KIFDKFGLcsfvsslPDQYDSQVGEngkwLSPGQRQQIAFGRA 189
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYFaelyglFDEELKKRIeELIELLGL-------EEFLDRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2306450510 190 VAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIEDL-KQSDQIAFITEKK 250
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVeALCDRVVILHKGK 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
38-273 |
3.30e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.60 E-value: 3.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 38 LEITINNLSIGYDK---PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLV----AQQkslaGEISFSDKKLrfdANFRH 110
Cdd:PRK11160 337 VSLTLNNVSFTYPDqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrawdPQQ----GEILLNGQPI---ADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 111 DWLKRAIYLGSE-PYLFSGSIIDNLLFAS-KYDRKELIKIFDKFGLCSFVSSlPDQYDSQVGENGKWLSPGQRQQIAFGR 188
Cdd:PRK11160 410 AALRQAISVVSQrVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 189 AVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAVI-GPYESLLKNSPSFK 267
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEqGTHQELLAQQGRYY 568
|
....*.
gi 2306450510 268 NLINQQ 273
Cdd:PRK11160 569 QLKQRL 574
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
40-232 |
1.08e-23 |
|
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: 95.24 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDanfRHDWLKRAIY 118
Cdd:COG4133 3 LEAENLSCRRgERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA---REDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LGSEPYLFSG-SIIDNLLFASKY-----DRKELIKIFDKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQQIAFGRAVAA 192
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAALyglraDREAIDEALEAVGLAGLA-------DLPVRQ----LSAGQKRRVALARLLLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKR-LAKEKIVLIITH 232
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
40-260 |
1.25e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 97.10 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHDWLKRAI 117
Cdd:PRK10790 341 IDIDNVSFAYrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPL---SSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YL-GSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNF 196
Cdd:PRK10790 418 AMvQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2306450510 197 YIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLL 260
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVeQGTHQQLL 562
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
40-260 |
2.97e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.46 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLR--------------F 104
Cdd:COG1121 7 IELENLTVSYGgRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRrarrrigyvpqraeV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 105 DANF--------------RHDWLKRaiylgsepylfsgsiidnllfASKYDRKELIKIFDKFGLCSFVsslpdqyDSQVG 170
Cdd:COG1121 87 DWDFpitvrdvvlmgrygRRGLFRR---------------------PSRADREAVDEALERVGLEDLA-------DRPIG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 171 EngkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITHKIEDLKQ-SDQIAFITE 248
Cdd:COG1121 139 E----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKtILVVTHDLGAVREyFDRVLLLNR 214
|
250
....*....|..
gi 2306450510 249 KKAVIGPYESLL 260
Cdd:COG1121 215 GLVAHGPPEEVL 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
40-250 |
4.22e-22 |
|
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: 90.45 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDkklrFDANFRHDWLKRA 116
Cdd:cd03247 1 LSINNVSFSYpeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG----VPVSDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 I-YLGSEPYLFSGSIIDNLlfaskydrkelikifdkfglcsfvsslpdqydsqvgenGKWLSPGQRQQIAFGRAVAADKN 195
Cdd:cd03247 77 IsVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2306450510 196 FYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKK 250
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGK 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
41-250 |
4.35e-22 |
|
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: 90.00 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 41 TINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdANFRHDWLKRAIYL 119
Cdd:cd00267 1 EIENLSFRYgGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--KLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 120 GSepylfsgsiidnllfaskydrkelikifdkfglcsfvsslpdqydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIF 199
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2306450510 200 DEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIEDLKQ-SDQIAFITEKK 250
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
42-237 |
1.92e-21 |
|
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: 89.45 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 42 INNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdANFRHDWLKRAIY 118
Cdd:cd03225 2 LKNLSFSYPdgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LGSEP--YLFSGSIIDNLLFA------SKYDRKELIK-IFDKFGLcsfvSSLPDQYDSQvgengkwLSPGQRQQIAFGRA 189
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGlenlglPEEEIEERVEeALELVGL----EGLRDRSPFT-------LSGGQKQRVAIAGV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2306450510 190 VAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITHKIEDL 237
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLL 197
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
40-251 |
2.09e-21 |
|
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: 88.43 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEIsfsdkklRFDANFRHDWLKRA 116
Cdd:cd03246 1 LEVENVSFRYpgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-------RLDGADISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 I-----YLGSEPYLFSGSIIDNLLfaskydrkelikifdkfglcsfvsslpdqydsqvgengkwlSPGQRQQIAFGRAVA 191
Cdd:cd03246 74 LgdhvgYLPQDDELFSGSIAENIL-----------------------------------------SGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 192 ADKNFYIFDEVTSNIDHENAGIILRAMKRL-AKEKIVLIITHKIEDLKQSDQIAFITEKKA 251
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
40-244 |
3.30e-21 |
|
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: 89.49 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDKPLITQ-----LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDANFRHDWL 113
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkalddVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIYLGSEPY-----LFS--GSIIDNLLFASKYDRKELIKIFDKFGLCSF--VSSLPDQYDSQvgengkwLSPGQRQQI 184
Cdd:cd03257 82 KEIQMVFQDPMsslnpRMTigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglPEEVLNRYPHE-------LSGGQRQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2306450510 185 AFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHKIEDLKQ-SDQIA 244
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVA 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
37-243 |
6.80e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 92.08 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 37 ILEITINNLSI-GYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSD---KKLRFDanfrhDW 112
Cdd:PRK10789 313 ELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiplTKLQLD-----SW 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 113 LKRAIYLGSEPYLFSGSIIDNLLF----ASKYDRKE---LIKIFDKfglcsfVSSLPDQYDSQVGENGKWLSPGQRQQIA 185
Cdd:PRK10789 388 RSRLAVVSQTPFLFSDTVANNIALgrpdATQQEIEHvarLASVHDD------ILRLPQGYDTEVGERGVMLSGGQKQRIS 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2306450510 186 FGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQI 243
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEI 519
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
40-270 |
2.09e-20 |
|
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: 91.16 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISfsdkklrfdanfrhdwLKRA 116
Cdd:TIGR00957 637 ITVHNATFTWardLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH----------------MKGS 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 I-YLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKN 195
Cdd:TIGR00957 701 VaYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 196 FYIFDEVTSNIDHENAGIILRAM---KRLAKEKIVLIITHKIEDLKQSDQIAFITEKK-AVIGPYESLLKNSPSFKNLI 270
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKiSEMGSYQELLQRDGAFAEFL 859
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-270 |
2.61e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.81 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 35 PKILEITINNLSIGYD----KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVaqqkslaGEISFSDkklrfDANFrh 110
Cdd:PLN03232 610 PGAPAISIKNGYFSWDsktsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GELSHAE-----TSSV-- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 111 DWLKRAIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAV 190
Cdd:PLN03232 676 VIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 191 AADKNFYIFDEVTSNID-HENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEkkAVI---GPYESLLKNSPSF 266
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDaHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSE--GMIkeeGTFAELSKSGSLF 833
|
....
gi 2306450510 267 KNLI 270
Cdd:PLN03232 834 KKLM 837
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
40-232 |
3.16e-20 |
|
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: 87.17 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-----DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL--RFDANFRHD- 111
Cdd:COG1124 2 LEVRNLSVSYgqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtrRRRKAFRRRv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 --------------W-LKRAIylgSEPYLFSGsiIDNllfaskyDRKELIKIFDKFGL-CSFVSSLPDQydsqvgengkw 175
Cdd:COG1124 82 qmvfqdpyaslhprHtVDRIL---AEPLRIHG--LPD-------REERIAELLEQVGLpPSFLDRYPHQ----------- 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 176 LSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITH 232
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSH 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
40-262 |
3.45e-20 |
|
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: 89.96 E-value: 3.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKT---LVAQQKSLAGEISFSDKKLRfdANFRHDWL 113
Cdd:COG1123 5 LEVRDLSVRYpggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAlmgLLPHGGRISGEVLLDGRDLL--ELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIYLGSEPY--LFSGSIIDNLLFA------SKYDRKEL-IKIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQI 184
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAEAlenlglSRAEARARvLELLEAVGLERRLDRYPHQ-----------LSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 185 AFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDLKQ-SDQIAFITEKKAV-IGPYESLL 260
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEiADRVVVMDDGRIVeDGPPEEIL 231
|
..
gi 2306450510 261 KN 262
Cdd:COG1123 232 AA 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-283 |
3.94e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.47 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 34 IPKILEITINNLSIGYDK----PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFR 109
Cdd:PTZ00265 377 LKDIKKIQFKNVRFHYDTrkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 110 HdWLKRAIYLGSEPYLFSGSIIDNLLFA-------------------SKYDRK--------------------------- 143
Cdd:PTZ00265 457 W-WRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgnDSQENKnkrnscrakcagdlndmsnttdsneli 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 144 ------------ELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENA 211
Cdd:PTZ00265 536 emrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 212 GIILRAMKRLA--KEKIVLIITHKIEDLKQSDQIAFITEKKAVIGPYESLLKNSPSFKNLINQQflllKGNKQD 283
Cdd:PTZ00265 616 YLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNN----KNNKDD 685
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
57-204 |
4.61e-20 |
|
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: 84.24 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDAnfRHDWLKRAIYLGSEPYLFSGSII-DNLL 135
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE--RKSLRKEIGYVFQDPQLFPRLTVrENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 136 FA-------SKYDRKELIKIFDKFGlcsfvssLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTS 204
Cdd:pfam00005 82 LGlllkglsKREKDARAEEALEKLG-------LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
39-243 |
7.19e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.11 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD--KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTL-----VAQqkslaGEISFSDKKLRfdaNFRHD 111
Cdd:COG5265 357 EVRFENVSFGYDpeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydVTS-----GRILIDGQDIR---DVTQA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 WLKRAIylG---SEPYLFSGSIIDNLLF----ASKYDRKELIK---IFDkfglcsFVSSLPDQYDSQVGENGKWLSPGQR 181
Cdd:COG5265 429 SLRAAI--GivpQDTVLFNDTIAYNIAYgrpdASEEEVEAAARaaqIHD------FIESLPDGYDTRVGERGLKLSGGEK 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2306450510 182 QQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQI 243
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEI 562
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
40-246 |
9.60e-20 |
|
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: 85.31 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTL-----VAQQKSLAGEISFSDKKLrFDANFRHDWL 113
Cdd:cd03260 1 IELRDLNVYYgDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDI-YDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIylG---SEPYLFSGSIIDNLLFASK---YDRKELIKIFDKFGLCSfvSSLPDQYDSQVGENGkwLSPGQRQQIAFG 187
Cdd:cd03260 80 RRRV--GmvfQKPNPFPGSIYDNVAYGLRlhgIKLKEELDERVEEALRK--AALWDEVKDRLHALG--LSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2306450510 188 RAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHkieDLKQ----SDQIAFI 246
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH---NMQQaarvADRTAFL 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
40-246 |
2.68e-19 |
|
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: 82.83 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDanfRHDWLKRAIY 118
Cdd:cd03230 1 IEVRNLSKRYgKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKE---PEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LGSEPYLFSG-SIIDNLLfaskydrkelikifdkfglcsfvsslpdqydsqvgengkwLSPGQRQQIAFGRAVAADKNFY 197
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 198 IFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIEDLKQ-SDQIAFI 246
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVAIL 168
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
43-270 |
3.29e-19 |
|
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: 87.66 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 43 NNLSIgYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVaqqkslaGEISFSDKKLRFDAnfrhdwlkRAIYLGSE 122
Cdd:TIGR01271 432 SNFSL-YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-------GELEPSEGKIKHSG--------RISFSPQT 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 123 PYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEV 202
Cdd:TIGR01271 496 SWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 203 TSNID-HENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAVI-GPYESLLKNSPSFKNLI 270
Cdd:TIGR01271 576 FTHLDvVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFyGTFSELQAKRPDFSSLL 645
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
40-246 |
1.02e-18 |
|
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: 81.46 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfDANFRHDWLKRAI- 117
Cdd:cd03229 1 LELKNVSKRYgQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT-DLEDELPPLRRRIg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPYLFSG-SIIDNLLFAskydrkelikifdkfglcsfvsslpdqydsqvgengkwLSPGQRQQIAFGRAVAADKNF 196
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2306450510 197 YIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDLKQ-SDQIAFI 246
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVL 174
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
38-243 |
1.33e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.99 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 38 LEITINNLSIGYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHDWLKR-- 115
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKN 195
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 196 FYIFDEVTSNID-HENAGIILRAMKRLAKE--KIVLIITHKIEDLKQSDQI 243
Cdd:cd03290 161 IVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWI 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
40-262 |
2.15e-18 |
|
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: 81.61 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfDANFRhDWLKRAI 117
Cdd:COG1122 1 IELENLSFSYpgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT-KKNLR-ELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEP--YLFSGSIIDNLLFA---SKYDRKELIK----IFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGR 188
Cdd:COG1122 79 LVFQNPddQLFAPTVEEDVAFGpenLGLPREEIRErveeALELVGLEHLADRPPHE-----------LSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2306450510 189 AVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITHKIEDL-KQSDQIAFITEKKAVI-GPYESLLKN 262
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKtVIIVTHDLDLVaELADRVIVLDDGRIVAdGTPREVFSD 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-284 |
3.79e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD--KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfDANFRHdwLKRA 116
Cdd:PRK13657 334 AVEFDDVSFSYDnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTRAS--LRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 I-YLGSEPYLFSGSIIDNLLFAsKYD--RKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAAD 193
Cdd:PRK13657 411 IaVVFQDAGLFNRSIEDNIRVG-RPDatDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 194 KNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFItEKKAVI--GPYESLLKNSPSFKNLIN 271
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVF-DNGRVVesGSFDELVARGGRFAALLR 568
|
250
....*....|...
gi 2306450510 272 QQFLLLKGNKQDA 284
Cdd:PRK13657 569 AQGMLQEDERRKQ 581
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
122-243 |
5.84e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.93 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 122 EPYLFSGSIIDNLLFASKYDRKELIKIFDKFG-LCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFD 200
Cdd:PTZ00265 1304 EPMLFNMSIYENIKFGKEDATREDVKRACKFAaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLD 1383
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2306450510 201 EVTSNIDHENAGIILRAMKRLAK--EKIVLIITHKIEDLKQSDQI 243
Cdd:PTZ00265 1384 EATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKI 1428
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
40-246 |
7.47e-18 |
|
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: 79.88 E-value: 7.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANfrhDWLKRAIY 118
Cdd:cd03262 1 IEIKNLHKSFgDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK---NINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LG---SEPYLFSG-SIIDNLLFA----SKYDRKELIKI----FDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAF 186
Cdd:cd03262 78 VGmvfQQFNLFPHlTVLENITLApikvKGMSKAEAEERalelLEKVGLADKADAYPAQ-----------LSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2306450510 187 GRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITHKIEDLKQ-SDQIAFI 246
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREvADRVIFM 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-270 |
1.01e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 35 PKILEITINNLSIGYD----KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVaqqkslaGEISfsdkkLRFDANF-- 108
Cdd:PLN03130 610 PGLPAISIKNGYFSWDskaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML-------GELP-----PRSDASVvi 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 109 RhdwlKRAIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGR 188
Cdd:PLN03130 678 R----GTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMAR 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 189 AVAADKNFYIFDEVTSNID-HENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEkkAVI---GPYESLLKNSP 264
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDaHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHE--GMIkeeGTYEELSNNGP 831
|
....*.
gi 2306450510 265 SFKNLI 270
Cdd:PLN03130 832 LFQKLM 837
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
39-232 |
1.07e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSI--GYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTlvaqqksLAGEISFSDKKLRFDAnfrhdwLKRA 116
Cdd:COG4178 362 ALALEDLTLrtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA-------IAGLWPYGSGRIARPA------GARV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYLGSEPYLFSGSIIDNLLF---ASKYDRKELIKIFDKFGLCSFVSSLPDQYD-SQVgengkwLSPGQRQQIAFGRAVAA 192
Cdd:COG4178 429 LFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLAERLDEEADwDQV------LSLGEQQRLAFARLLLH 502
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITH 232
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
40-246 |
1.24e-17 |
|
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: 79.46 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDK-----PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDANFRHDWL 113
Cdd:cd03255 1 IELKNLSKTYGGggekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAI-------YLgsEPYLfsgSIIDNLLFA-------SKYDRKELIKIFDKFGLCSFVSSLPDQydsqvgengkwLSPG 179
Cdd:cd03255 81 RRHIgfvfqsfNL--LPDL---TALENVELPlllagvpKKERRERAEELLERVGLGDRLNHYPSE-----------LSGG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 180 QRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDLKQSDQIAFI 246
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAEYADRIIEL 213
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
35-273 |
1.98e-17 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 82.30 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 35 PKILEITINNLSIGYDKPL---ITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEI-----SFSDKKLrfda 106
Cdd:TIGR00957 1280 PPRGRVEFRNYCLRYREDLdlvLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIiidglNIAKIGL---- 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 107 nfrHDWLKRAIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAF 186
Cdd:TIGR00957 1356 ---HDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 187 GRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKqsDQIAFITEKKAVIGPYesllkNSPSf 266
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM--DYTRVIVLDKGEVAEF-----GAPS- 1504
|
....*..
gi 2306450510 267 kNLINQQ 273
Cdd:TIGR00957 1505 -NLLQQR 1510
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
43-270 |
4.44e-17 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 79.13 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 43 NNLSIgYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDkklrfdanfrhdwlkRAIYLGSE 122
Cdd:cd03291 43 SNLCL-VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG---------------RISFSSQF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 123 PYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEV 202
Cdd:cd03291 107 SWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 203 TSNID-HENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAVI-GPYESLLKNSPSFKNLI 270
Cdd:cd03291 187 FGYLDvFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFyGTFSELQSLRPDFSSKL 256
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
42-235 |
4.49e-17 |
|
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: 77.57 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 42 INNLSIGYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLR--------------FDA 106
Cdd:cd03235 2 VEDLTVSYGgHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEkerkrigyvpqrrsIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 107 NFRHDwLKRAIYLGSEPYLFSGSIIdnllfaSKYDRKELIKIFDKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQQIAF 186
Cdd:cd03235 82 DFPIS-VRDVVLMGLYGHKGLFRRL------SKADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRVLL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2306450510 187 GRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIE 235
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLG 193
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
40-261 |
4.61e-17 |
|
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: 78.31 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISF--------SDKKLRfdaNFRh 110
Cdd:cd03261 1 IELRGLTKSFgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedisglSEAELY---RLR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 111 dwlKRAIYLGSEPYLFSG-SIIDNLLF---------ASKYDRKELIKIfDKFGLCSFVSSLPDQydsqvgengkwLSPGQ 180
Cdd:cd03261 77 ---RRMGMLFQSGALFDSlTVFENVAFplrehtrlsEEEIREIVLEKL-EAVGLRGAEDLYPAE-----------LSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 181 RQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKI--VLIITHKIEDLKQ-SDQIAFITEKKAVI-GPY 256
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGltSIMVTHDLDTAFAiADRIAVLYDGKIVAeGTP 221
|
....*
gi 2306450510 257 ESLLK 261
Cdd:cd03261 222 EELRA 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-261 |
6.88e-17 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 80.72 E-value: 6.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVaQQKSLAGEISFSDkkLRFDANFRHDWLKR 115
Cdd:TIGR01271 1217 QMDVQGLTAKYTeagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDG--VSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKN 195
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 196 FYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKavIGPYESLLK 261
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSS--VKQYDSIQK 1437
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
39-248 |
8.74e-17 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 78.03 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSD---KKLRFdanfrHDW 112
Cdd:cd03288 19 EIKIHDLCVRYEnnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidiSKLPL-----HTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 113 LKRAIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAA 192
Cdd:cd03288 94 RSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITE 248
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSR 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
41-252 |
8.87e-17 |
|
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: 76.32 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 41 TINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdanfrhdwlkraiyl 119
Cdd:cd03214 1 EVENLSVGYgGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 120 gsepylfsgsiidnllfaSKYDRKELIKIF-------DKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQQIAFGRAVAA 192
Cdd:cd03214 64 ------------------ASLSPKELARKIayvpqalELLGLAHLA-------DRPFNE----LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHkieDLKQ----SDQIAFITEKKAV 252
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARErgKTVVMVLH---DLNLaaryADRVILLKDGRIV 177
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
57-246 |
3.08e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.85 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISF--------SDKKLrfdANFRHDwlkraiYLG---SEPYL 125
Cdd:COG1136 27 VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdgqdisslSEREL---ARLRRR------HIGfvfQFFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 126 FSG-SIIDNLLFASKY-------DRKELIKIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFY 197
Cdd:COG1136 98 LPElTALENVALPLLLagvsrkeRRERARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 198 IFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDLKQSDQIAFI 246
Cdd:COG1136 167 LADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRL 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
39-271 |
3.89e-16 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 76.43 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYDK---PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVaQQKSLAGEISFSDkkLRFDANFRHDWLKR 115
Cdd:cd03289 2 QMTVKDLTAKYTEggnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDG--VSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKN 195
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 196 FYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKavIGPYES---LLKNSPSFKNLIN 271
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENK--VRQYDSiqkLLNEKSHFKQAIS 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
40-252 |
4.53e-16 |
|
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: 74.86 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKklrfdanfrhDWLKRAIY 118
Cdd:cd03259 1 LELKGLSKTYgSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR----------DVTGVPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LGSEPYLFSG-------SIIDNLLFA---SKYDRKELIK----IFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQI 184
Cdd:cd03259 71 RRNIGMVFQDyalfphlTVAENIAFGlklRGVPKAEIRArvreLLELVGLEGLLNRYPHE-----------LSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 185 AFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIED-LKQSDQIAFITEKKAV 252
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEaLALADRIAVMNEGRIV 210
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
60-265 |
5.67e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 60 SLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHDWLKRAIYLGSEPYLFSG-SIIDNLLF-- 136
Cdd:PRK09493 23 NIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHlTALENVMFgp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 137 -----ASKYDRKELIK-IFDKFGLcsfvSSLPDQYDSQvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHEN 210
Cdd:PRK09493 103 lrvrgASKEEAEKQAReLLAKVGL----AERAHHYPSE-------LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2306450510 211 AGIILRAMKRLAKEKIVLII-THKIEDLKQ-SDQIAFITEKK-AVIGPYESLLKNSPS 265
Cdd:PRK09493 172 RHEVLKVMQDLAEEGMTMVIvTHEIGFAEKvASRLIFIDKGRiAEDGDPQVLIKNPPS 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
35-243 |
2.05e-15 |
|
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: 73.22 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 35 PKILEITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHD 111
Cdd:cd03369 2 PEHGEIEVENLSVRYApdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 WLKRAI-YLGSEPYLFSGSIIDNLLFASKYDRKELIKIFdkfglcsfvsslpdqydsQVGENGKWLSPGQRQQIAFGRAV 190
Cdd:cd03369 79 DLRSSLtIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGAL------------------RVSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2306450510 191 AADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQSDQI 243
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKI 193
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
39-273 |
2.34e-15 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 75.76 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGY--DKPLITQ-LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDanfrhdwlK 114
Cdd:TIGR03797 451 AIEVDRVTFRYrpDGPLILDdVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLaGLD--------V 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 115 RAI--YLG---SEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRA 189
Cdd:TIGR03797 523 QAVrrQLGvvlQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 190 VAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVliITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKNSPSFKN 268
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIV--IAHRLSTIRNADRIYVLDAGRVVqQGTYDELMAREGLFAQ 680
|
....*
gi 2306450510 269 LINQQ 273
Cdd:TIGR03797 681 LARRQ 685
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
40-232 |
3.17e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDK---KLRfdanfrhdwlK 114
Cdd:COG2884 2 IRFENVSKRYpgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLK----------R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 115 RAIylgsePY--------------LFSGSIIDNLLFA-------SKYDRKELIKIFDKFGLCSFVSSLPDQydsqvgeng 173
Cdd:COG2884 72 REI-----PYlrrrigvvfqdfrlLPDRTVYENVALPlrvtgksRKEIRRRVREVLDLVGLSDKAKALPHE--------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 174 kwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITH 232
Cdd:COG2884 138 --LSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTtVLIATH 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
40-262 |
3.23e-15 |
|
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: 75.32 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY------DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDANFRHDW 112
Cdd:COG1123 261 LEVRNLSKRYpvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 113 LKRAIYLGSEPY--LFS----GSII----DNLLFASKYDRKELIK-IFDKFGLC-SFVSSLPDQydsqvgengkwLSPGQ 180
Cdd:COG1123 341 RRRVQMVFQDPYssLNPrmtvGDIIaeplRLHGLLSRAERRERVAeLLERVGLPpDLADRYPHE-----------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 181 RQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDLKQ-SDQIAFITEKKAV-IGPY 256
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElgLTYLFISHDLAVVRYiADRVAVMYDGRIVeDGPT 489
|
....*.
gi 2306450510 257 ESLLKN 262
Cdd:COG1123 490 EEVFAN 495
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
44-248 |
4.67e-15 |
|
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: 72.33 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 44 NLSIGYDKPLitqLSWSLKI-----GHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrFDANFRHDW--LKRA 116
Cdd:cd03297 1 MLCVDIEKRL---PDFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL-FDSRKKINLppQQRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 I-YLGSEPYLFSG-SIIDNLLFASKYDRKELIKIF-----DKFGLcsfvSSLPDQYDSQvgengkwLSPGQRQQIAFGRA 189
Cdd:cd03297 77 IgLVFQQYALFPHlNVRENLAFGLKRKRNREDRISvdellDLLGL----DHLLNRYPAQ-------LSGGEKQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2306450510 190 VAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KI-VLIITHKIEDL-KQSDQIAFITE 248
Cdd:cd03297 146 LAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIpVIFVTHDLSEAeYLADRIVVMED 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
57-275 |
9.01e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 72.31 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLR-----------FDANFRHDWLKRAIYLGSEPYL 125
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 126 FSG-SIIDNLLFA-------SKYDRKE-LIKIFDKFGLCsfvsslpdqyDSQVGENGKWLSPGQRQQIAFGRAVAADKNF 196
Cdd:PRK10619 104 WSHmTVLENVMEApiqvlglSKQEARErAVKYLAKVGID----------ERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 197 YIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIEDLKQ-SDQIAFIteKKAVI---GPYESLLKNSPSFKnliN 271
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFL--HQGKIeeeGAPEQLFGNPQSPR---L 248
|
....
gi 2306450510 272 QQFL 275
Cdd:PRK10619 249 QQFL 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
52-275 |
1.02e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 52 PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHDWLKRAI-YLGSEPYLFSGSI 130
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV---AKFGLTDLRRVLsIIPQSPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 131 IDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHEN 210
Cdd:PLN03232 1327 RFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2306450510 211 AGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV--IGPYESLLKNSPSFKNLI------NQQFL 275
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLeyDSPQELLSRDTSAFFRMVhstgpaNAQYL 1479
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
40-246 |
1.21e-14 |
|
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: 71.61 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHDWLKRAI- 117
Cdd:COG1120 2 LEAENLSVGYGgRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL---ASLSRRELARRIa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPYL-FSGSIIDNLLFA-----------SKYDRKELIKIFDKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQQIA 185
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgrpSAEDREAVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2306450510 186 FGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHkieDLKQ----SDQIAFI 246
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLH---DLNLaaryADRLVLL 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
40-262 |
1.26e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.95 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDaNFRHDWLKRA 116
Cdd:PRK13632 8 IKVENVSFSYPnseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE-NLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYLGSEPYLFSGSII-DNLLFA---SKYDRKELIKIFD----KFGLCSFVSSLPdqydsqvgengKWLSPGQRQQIAFGR 188
Cdd:PRK13632 87 IIFQNPDNQFIGATVeDDIAFGlenKKVPPKKMKDIIDdlakKVGMEDYLDKEP-----------QNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2306450510 189 AVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKN 262
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkKTLISITHDMDEAILADKVIVFSEGKLIaQGKPKEILNN 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
50-232 |
1.23e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 50 DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDanfrhDWLKRAIYLGS----EPYL 125
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP-----DVAEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 126 fsgSIIDNLLFASKYDRKELIKI---FDKFGLcSFVSSLPDQYdsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEV 202
Cdd:PRK13539 89 ---TVAENLEFWAAFLGGEELDIaaaLEAVGL-APLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 2306450510 203 TSNIDHENAGIILRAMK-RLAKEKIVLIITH 232
Cdd:PRK13539 155 TAALDAAAVALFAELIRaHLAQGGIVIAATH 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
51-243 |
1.98e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.19 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 51 KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEIsfsdkklrfdanfrhdWLKRAI-YLGSEPYLFSGS 129
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV----------------WAERSIaYVPQQAWIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 130 IIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHE 209
Cdd:PTZ00243 737 VRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190
....*....|....*....|....*....|....*.
gi 2306450510 210 NAGIILRA--MKRLAKEKIVLiITHKIEDLKQSDQI 243
Cdd:PTZ00243 817 VGERVVEEcfLGALAGKTRVL-ATHQVHVVPRADYV 851
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
60-243 |
2.55e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.66 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 60 SLKI--GHLYALSGQSGSGKSTLAKTLV-AQQKSlAGEISFSDKKLRFdANFRHdwlkrAIYLG-----SEPYLFSG-SI 130
Cdd:COG1129 24 SLELrpGEVHALLGENGAGKSTLMKILSgVYQPD-SGEILLDGEPVRF-RSPRD-----AQAAGiaiihQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 131 IDNLLF------ASKYDRKELIK----IFDKFGLcsfvsSL-PDQydsQVGEngkwLSPGQRQQIAFGRAVAADKNFYIF 199
Cdd:COG1129 97 AENIFLgreprrGGLIDWRAMRRrareLLARLGL-----DIdPDT---PVGD----LSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2306450510 200 DEVTSNIDHENAGIILRAMKRLAKEKI-VLIITHKIEDLKQ-SDQI 243
Cdd:COG1129 165 DEPTASLTEREVERLFRIIRRLKAQGVaIIYISHRLDEVFEiADRV 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
40-269 |
2.79e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSD------KKLRfdaNFRHd 111
Cdd:PRK13644 2 IRLENVSYSYpdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQ---GIRK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 wLKRAIYLGSEPYLFSGSIIDNLLFASKydrkelikifdkfGLCSFVSSLPDQYDSQVGENG---------KWLSPGQRQ 182
Cdd:PRK13644 78 -LVGIVFQNPETQFVGRTVEEDLAFGPE-------------NLCLPPIEIRKRVDRALAEIGlekyrhrspKTLSGGQGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 183 QIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRL-AKEKIVLIITHKIEDLKQSDQIAFITEKKAVI-GPYESLL 260
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLeGEPENVL 223
|
....*....
gi 2306450510 261 KNsPSFKNL 269
Cdd:PRK13644 224 SD-VSLQTL 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
60-243 |
1.39e-12 |
|
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: 64.37 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 60 SLKI--GHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDAnfRHDWLKRAIYLgsepylfsgsiidnllfa 137
Cdd:cd03216 20 SLSVrrGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS--PRDARRAGIAM------------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 138 skydrkelikIFdkfglcsfvsslpdqydsQvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRA 217
Cdd:cd03216 80 ----------VY------------------Q-------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170 180
....*....|....*....|....*...
gi 2306450510 218 MKRLAKEKI-VLIITHKIEDLKQ-SDQI 243
Cdd:cd03216 125 IRRLRAQGVaVIFISHRLDEVFEiADRV 152
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
40-275 |
1.67e-12 |
|
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: 65.39 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDANFRHDWLKRai 117
Cdd:COG1127 6 IEVRNLTKSFgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItGLSEKELYELRRR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 yLGsepYLF-SG------SIIDNLLFA----SKYDRKELIKI----FDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQ 182
Cdd:COG1127 84 -IG---MLFqGGalfdslTVFENVAFPlrehTDLSEAEIRELvlekLELVGLPGAADKMPSE-----------LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 183 QIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KI-VLIITHKIEDLKQ-SDQIAFITEKKAV-IGPYES 258
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLtSVVVTHDLDSAFAiADRVAVLADGKIIaEGTPEE 228
|
250
....*....|....*..
gi 2306450510 259 LLKNSPSFknlInQQFL 275
Cdd:COG1127 229 LLASDDPW---V-RQFL 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-254 |
1.86e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 37 ILEITINNLSIGYDKPLITQ-LSWSLKIGHLYALSGQSGSGKSTLAKTLvAQQKSLAGEISFSDKKLRFDANFRH----- 110
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEgVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYErrvnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 111 DWLKRAIYL-GSEPYLFSGSIIDNLLFASKydrkeLIKIFDKFGLCSFVSS------LPDQYDSQVGENGKWLSPGQRQQ 183
Cdd:PRK14258 84 NRLRRQVSMvHPKPNLFPMSVYDNVAYGVK-----IVGWRPKLEIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 184 IAFGRAVAADKNFYIFDEVTSNIDHENAGII--LRAMKRLAKEKIVLIITHKIEDLKQ-SDQIAFITEKKAVIG 254
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVesLIQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGNENRIG 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
57-232 |
2.21e-12 |
|
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: 64.74 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHD---WLKRAIYLGSEPY--LFSGSII 131
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV---SDLRGRaipYLRRKIGVVFQDFrlLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 132 DNLLFA-------SKYDRKELIKIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTS 204
Cdd:cd03292 97 ENVAFAlevtgvpPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|....*....
gi 2306450510 205 NIDHENAGIILRAMKRLAKEKI-VLIITH 232
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAGTtVVVATH 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
38-239 |
5.59e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.26 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 38 LEITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHDWLKRA 116
Cdd:PRK11231 1 MTLRTENLTVGYgTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI---SMLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYL-------------------GSEPYL-FSGSIidnllfaSKYDRKELIKIFDKFGLCSFVsslpdqyDSQVGEngkwL 176
Cdd:PRK11231 78 LALlpqhhltpegitvrelvayGRSPWLsLWGRL-------SAEDNARVNQAMEQTRINHLA-------DRRLTD----L 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 177 SPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHkieDLKQ 239
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLH---DLNQ 200
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-262 |
6.16e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.16 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTL-----VAQQKSLAGEISFSDKKLrfdanFRHDW- 112
Cdd:PRK14247 4 IEIRDLKVSFgQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDI-----FKMDVi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 113 -LKRAIYLGSE-----PYLfsgSIIDNLLFASKYDR--KELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQI 184
Cdd:PRK14247 79 eLRRRVQMVFQipnpiPNL---SIFENVALGLKLNRlvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 185 AFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITH-KIEDLKQSDQIAFITEKKAV-IGPYESLLKN 262
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVeWGPTREVFTN 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
40-235 |
7.82e-12 |
|
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: 63.74 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHDWLKRAI 117
Cdd:cd03256 1 IEVENLSKTYpnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 ylgsePYLFSG-------SIIDNLLFA---------------SKYDRKELIKIFDKFGLCSFVSSLPDQydsqvgengkw 175
Cdd:cd03256 81 -----GMIFQQfnlierlSVLENVLSGrlgrrstwrslfglfPKEEKQRALAALERVGLLDKAYQRADQ----------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2306450510 176 LSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHKIE 235
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVD 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
40-243 |
1.10e-11 |
|
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: 63.60 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD---KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANfRHDWLKRA 116
Cdd:TIGR04520 1 IEVENVSFSYPeseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEN-LWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYLGSEPylfsgsiiDNLLFAS-------------KYDRKELIKIFDK----FGLCSFVSSLPDQydsqvgengkwLSPG 179
Cdd:TIGR04520 80 GMVFQNP--------DNQFVGAtveddvafglenlGVPREEMRKRVDEalklVGMEDFRDREPHL-----------LSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 180 QRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDLKQSDQI 243
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEegITVISITHDMEEAVLADRV 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
40-253 |
1.19e-11 |
|
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: 62.68 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDAnfrhdwlKRAI- 117
Cdd:cd03269 1 LEVENVTKRFgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------RNRIg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPYLFSG-SIIDNLL-FAS------KYDRKELIKIFDKFGlcsfvssLPDQYDSQVGEngkwLSPGQRQQIAFGRA 189
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVyLAQlkglkkEEARRRIDEWLERLE-------LSEYANKRVEE----LSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 190 VAADKNFYIFDEVTSNIDHENAGIILRAMKRLA-KEKIVLIITHKIEDLKQ-SDQIAFITEKKAVI 253
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
47-243 |
1.29e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 47 IGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfDANFRHDWLKRAIYLGSEP 123
Cdd:PRK10247 13 VGYlagDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI--STLKPEIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 124 YLFSGSIIDNLLFA-----SKYDRKELIKIFDKFGLcsfvsslPDQ-YDSQVGEngkwLSPGQRQQIAFGRAVAADKNFY 197
Cdd:PRK10247 91 TLFGDTVYDNLIFPwqirnQQPDPAIFLDDLERFAL-------PDTiLTKNIAE----LSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2306450510 198 IFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHKIEDLKQSDQI 243
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKV 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
59-256 |
1.58e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 59 WSLKI--GHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANfrhdwlkraiylgsepylfsGSIIDNLlf 136
Cdd:COG2401 49 LNLEIepGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGRE--------------------ASLIDAI-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 137 ASKYDRKELIKIFDKFGLCSFVSslpdqYDSQVGEngkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILR 216
Cdd:COG2401 107 GRKGDFKDAVELLNAVGLSDAVL-----WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2306450510 217 AMKRLAKEK---IVLIITHK--IEDLkQSDQIAFITEKKAVIGPY 256
Cdd:COG2401 178 NLQKLARRAgitLVVATHHYdvIDDL-QPDLLIFVGYGGVPEEKR 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
40-248 |
3.03e-11 |
|
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: 61.44 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDKP-LITQLSWSLKIGhLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKklrfDANFRHDWLKRAI- 117
Cdd:cd03264 1 LQLENLTKRYGKKrALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ----DVLKQPQKLRRRIg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPYLFSG-SIIDNLLF-------ASKYDRKELIKIFDKFGLCsfvsslpDQYDSQVGEngkwLSPGQRQQIAFGRA 189
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkgiPSKEVKARVDEVLELVNLG-------DRAKKKIGS----LSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 190 VAADKNFYIFDEVTSNIDHENAgIILRAM-KRLAKEKIVLIITHKIEDLKQS-DQIAFITE 248
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEER-IRFRNLlSELGEDRIVILSTHIVEDVESLcNQVAVLNK 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
40-262 |
4.52e-11 |
|
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: 61.55 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdanfrhDW----L 113
Cdd:cd03295 1 IEFENVTKRYggGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-------EQdpveL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAI-YLGSEPYLFSG-SIIDN---LLFASKYDR-------KELIKIFDkFGLCSFVSSLPDQydsqvgengkwLSPGQR 181
Cdd:cd03295 74 RRKIgYVIQQIGLFPHmTVEENialVPKLLKWPKekireraDELLALVG-LDPAEFADRYPHE-----------LSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 182 QQIAFGRAVAADKNFYIFDEVTSNIDHenagiILRA-----MKRLAKE--KIVLIITHKI-EDLKQSDQIAFITEKKAV- 252
Cdd:cd03295 142 QRVGVARALAADPPLLLMDEPFGALDP-----ITRDqlqeeFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVq 216
|
250
....*....|
gi 2306450510 253 IGPYESLLKN 262
Cdd:cd03295 217 VGTPDEILRS 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-264 |
5.63e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 44 NLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL--RFDANFRH--DWLKRAIY 118
Cdd:PRK14271 26 NLTLGFaGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggRSIFNYRDvlEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVS-SLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFY 197
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEvGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 198 IFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKI-EDLKQSDQIAFITEKKAV-IGPYESLLkNSP 264
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVeEGPTEQLF-SSP 253
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
58-232 |
9.59e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.86 E-value: 9.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 58 SWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHDWLKRAIYL-------GSEPYLFSGSI 130
Cdd:PRK10419 32 SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMvfqdsisAVNPRKTVREI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 131 ID----NLLFASKYDRKELI-KIFDKFGL-CSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTS 204
Cdd:PRK10419 112 IReplrHLLSLDKAERLARAsEMLRAVDLdDSVLDKRPPQ-----------LSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190
....*....|....*....|....*....|.
gi 2306450510 205 NID-HENAGIIlRAMKRLAKEK--IVLIITH 232
Cdd:PRK10419 181 NLDlVLQAGVI-RLLKKLQQQFgtACLFITH 210
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
53-244 |
1.06e-10 |
|
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: 59.81 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 53 LITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDanfRHDWLKRAIYLGSEPYLFSG-SII 131
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ---RDSIARGLLYLGHAPGIKTTlSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 132 DNLLF-ASKYDRKELIKIFDKFGLCSFvSSLPDQYdsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHEN 210
Cdd:cd03231 92 ENLRFwHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2306450510 211 AGIILRAMK-RLAKEKIVLIITHkiEDLKQSDQIA 244
Cdd:cd03231 161 VARFAEAMAgHCARGGMVVLTTH--QDLGLSEAGA 193
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
40-230 |
1.12e-10 |
|
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: 60.14 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDKPLITQ-LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFR-HDWLKRAI 117
Cdd:cd03224 1 LEVENLNAGYGKSQILFgVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPpHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 -YLGSEPYLFSG-SIIDNLLFASKYDRKELIK-----IFDKFglcsfvSSLPDQYDSQVGEngkwLSPGQRQQIAFGRAV 190
Cdd:cd03224 78 gYVPEGRRIFPElTVEENLLLGAYARRRAKRKarlerVYELF------PRLKERRKQLAGT----LSGGEQQMLAIARAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2306450510 191 AADKNFYIFDEVTsnidhenAGI-------ILRAMKRLAKEKI-VLII 230
Cdd:cd03224 148 MSRPKLLLLDEPS-------EGLapkiveeIFEAIRELRDEGVtILLV 188
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
40-272 |
1.12e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.97 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKT---LVAQQKSLAGEISFSDKKLRFDA--NFRHd 111
Cdd:PRK13640 6 VEFKHVSFTYpdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTvwDIRE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 wlKRAIYLGSEPYLFSGSII-DNLLFA---SKYDRKELIKIFDK----FGLCSFVSSLPdqydsqvgengKWLSPGQRQQ 183
Cdd:PRK13640 85 --KVGIVFQNPDNQFVGATVgDDVAFGlenRAVPRPEMIKIVRDvladVGMLDYIDSEP-----------ANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 184 IAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHKIEDLKQSDQIAFITEKKAV-------IG 254
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLaqgspveIF 231
|
250 260
....*....|....*....|..
gi 2306450510 255 PYESLLKNS----PSFKNLINQ 272
Cdd:PRK13640 232 SKVEMLKEIgldiPFVYKLKNK 253
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
40-235 |
1.37e-10 |
|
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: 59.79 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD-----KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdanfRHDwlK 114
Cdd:cd03293 1 LEVRNVSKTYGggggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPG--P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 115 RAIYLGSEPYLFS-GSIIDNLLFA------SKYDRKELI-KIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAF 186
Cdd:cd03293 74 DRGYVFQQDALLPwLTVLDNVALGlelqgvPKAEARERAeELLELVGLSGFENAYPHQ-----------LSGGMRQRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 187 GRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIE 235
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTHDID 193
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
36-248 |
1.66e-10 |
|
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: 59.10 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 36 KILEITINNLSIGYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLA--GEISFSDKKLRfdanfRHDWL 113
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLD-----KRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIYLGSEPYLFSGSIID-NLLFASKYdrkelikifdkfglcsfvsslpdqydsqvgengKWLSPGQRQQIAFGRAVAA 192
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVReTLMFAAKL---------------------------------RGLSGGERKRVSIALELVS 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITH--KIEDLKQSDQIAFITE 248
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHqpSSEIFELFDKLLLLSQ 187
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
48-241 |
1.99e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.78 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 48 GYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEIsfsdkklrfdanfRHDWLKRAIYL---GSEP 123
Cdd:NF040873 1 GYGgRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRAGGARVAYVpqrSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 124 YLFSGSIIDNL---LFA--------SKYDRKELIKIFDKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQQIAFGRAVAA 192
Cdd:NF040873 68 DSLPLTVRDLVamgRWArrglwrrlTRDDRAAVDDALERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITHKIEDLKQSD 241
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHARGAtVVVVTHDLELVRRAD 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
50-276 |
2.08e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 59.68 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 50 DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDAN-FRHDWLKRAIYLG---SEPYL 125
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDiFQIDAIKLRKEVGmvfQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 126 FSG-SIIDNLLFASKY----DRKELIKIFDKfglCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFD 200
Cdd:PRK14246 102 FPHlSIYDNIAYPLKShgikEKREIKKIVEE---CLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2306450510 201 EVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQ-SDQIAFITEKKAVIGPYESLLKNSPsfKNLINQQFLL 276
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSP--KNELTEKYVI 253
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
57-234 |
2.32e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.12 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHDWLKRAIYLGSEPY--LFSGSIIDNL 134
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHhlLMDRTVYDNV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 135 LF------ASKYD-RKELIKIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNID 207
Cdd:PRK10908 101 AIpliiagASGDDiRRRVSAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180
....*....|....*....|....*...
gi 2306450510 208 HENAGIILRAMKRLAKEKI-VLIITHKI 234
Cdd:PRK10908 170 DALSEGILRLFEEFNRVGVtVLMATHDI 197
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
40-250 |
2.48e-10 |
|
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: 59.06 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHdwlkra 116
Cdd:cd03263 1 LQIRNLTKTYkkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYLGSEPY---LFSG-SIIDNL-LFA-----SKYDRKELI-KIFDKFGlcsfvssLPDQYDSQVGEngkwLSPGQRQQIA 185
Cdd:cd03263 75 QSLGYCPQfdaLFDElTVREHLrFYArlkglPKSEIKEEVeLLLRVLG-------LTDKANKRART----LSGGMKRKLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 186 FGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQ-SDQIAFITEKK 250
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGK 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-243 |
2.72e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.64 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY---DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfDANFrhdWLKRA 116
Cdd:PRK13635 6 IRVEHISFRYpdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS-EETV---WDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 ---IYLGSEPYLFSGSII-DNLLFA---SKYDRKELIK----IFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIA 185
Cdd:PRK13635 82 qvgMVFQNPDNQFVGATVqDDVAFGlenIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 186 FGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHKIEDLKQSDQI 243
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRV 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
38-201 |
3.98e-10 |
|
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: 58.89 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 38 LEITINNLSIGYDK-PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKklrfDANfRHDWLKRA 116
Cdd:cd03296 1 MSIEVRNVSKRFGDfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE----DAT-DVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYLGSEPY-LFSG-SIIDNLLFA----SKYDRKELIKIFDKF-GLCSFV--SSLPDQYDSQvgengkwLSPGQRQQIAFG 187
Cdd:cd03296 76 VGFVFQHYaLFRHmTVFDNVAFGlrvkPRSERPPEAEIRAKVhELLKLVqlDWLADRYPAQ-------LSGGQRQRVALA 148
|
170
....*....|....
gi 2306450510 188 RAVAADKNFYIFDE 201
Cdd:cd03296 149 RALAVEPKVLLLDE 162
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
44-241 |
4.71e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 44 NLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDanfRHDWLKRAIYLGSE 122
Cdd:PRK13540 6 ELDFDYhDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD---LCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 123 ----PYLfsgSIIDNLLF-----ASKYDRKELIKIFDKFGLCSFVSSLpdqydsqvgengkwLSPGQRQQIAFGRAVAAD 193
Cdd:PRK13540 83 sginPYL---TLRENCLYdihfsPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2306450510 194 KNFYIFDEVTSNIDHENAGIILRAMK-RLAKEKIVLIITHKIEDLKQSD 241
Cdd:PRK13540 146 AKLWLLDEPLVALDELSLLTIITKIQeHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
40-253 |
6.09e-10 |
|
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: 57.61 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKklrfDANFRHDWLKRAIY 118
Cdd:cd03268 1 LKTNDLTKTYgKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK----SYQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LGSEPYLFSG-SIIDNLLFASKY---DRKELIKIFDKFGlcsfvssLPDQYDSQVGEngkwLSPGQRQQIAFGRAVAADK 194
Cdd:cd03268 77 LIEAPGFYPNlTARENLRLLARLlgiRKKRIDEVLDVVG-------LKDSAKKKVKG----FSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2306450510 195 NFYIFDEVTSNIDHEnaGI--ILRAMKRLAKEKI-VLIITHKIEDLKQ-SDQIAFITEKKAVI 253
Cdd:cd03268 146 DLLILDEPTNGLDPD--GIkeLRELILSLRDQGItVLISSHLLSEIQKvADRIGIINKGKLIE 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
35-244 |
9.31e-10 |
|
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: 56.67 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 35 PKILEITinNLSIgydKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANfrHDWLK 114
Cdd:cd03215 2 EPVLEVR--GLSV---KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP--RDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 115 RAIYLGSEpylfsgsiidnllfaskyDRKelikifdKFGLcsfVSSLPdqydsqVGEN---GKWLSPGQRQQIAFGRAVA 191
Cdd:cd03215 75 AGIAYVPE------------------DRK-------REGL---VLDLS------VAENialSSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2306450510 192 ADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIEDLKQ-SDQIA 244
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGlCDRIL 175
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
40-243 |
1.33e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.45 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY--DKPL-ITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfDANFRHDWLKRA 116
Cdd:PRK13648 8 IVFKNVSFQYqsDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT-DDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYLGSEPYLFSGSIIdnllfasKYDRKelikifdkFGLCSFVSSLPD------QYDSQVG------ENGKWLSPGQRQQI 184
Cdd:PRK13648 87 IVFQNPDNQFVGSIV-------KYDVA--------FGLENHAVPYDEmhrrvsEALKQVDmleradYEPNALSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 185 AFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLI--ITHKIEDLKQSDQI 243
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIisITHDLSEAMEADHV 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
40-245 |
2.30e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.71 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTL-----VAQQKSLAGEISFSDKKLRFDANFRHDWL 113
Cdd:PRK14239 6 LQVSDLSVYYnKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIYLGSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFV-SSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAA 192
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKgASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 193 DKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITHKIEDLKQ-SDQIAF 245
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGF 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-262 |
3.32e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.39 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 66 LYALSGQSGSGKSTLAKTL-----VAQQKSLAGEISFSDKKLrFDANFRHDWLKRAI-----YLGSEPYLfsgSIIDNLL 135
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNI-YSPDVDPIEVRREVgmvfqYPNPFPHL---TIYDNVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 136 FASKYD-----RKELIKIFdKFGLCSfvSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHEN 210
Cdd:PRK14267 108 IGVKLNglvksKKELDERV-EWALKK--AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVG 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 211 AGIILRAMKRLAKEKIVLIITHK-IEDLKQSDQIAFITEKKAV-IGPYESLLKN 262
Cdd:PRK14267 185 TAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIeVGPTRKVFEN 238
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
37-262 |
3.59e-09 |
|
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: 56.60 E-value: 3.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 37 ILEItiNNLSIGYDKP-----LITQLSWSLKIGHLYALSGQSGSGKSTLAKT---LVAQQKSLAGEISF--------SDK 100
Cdd:COG0444 1 LLEV--RNLKVYFPTRrgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFdgedllklSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 101 KLRfdaNFRhdwlkraiylGSE-------PY-----LFS-GSII-DNLLFASKYDRKEL----IKIFDKFGL---CSFVS 159
Cdd:COG0444 79 ELR---KIR----------GREiqmifqdPMtslnpVMTvGDQIaEPLRIHGGLSKAEAreraIELLERVGLpdpERRLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 160 SLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDhenAGI---ILRAMKRLAKEKI--VLIITHki 234
Cdd:COG0444 146 RYPHE-----------LSGGMRQRVMIARALALEPKLLIADEPTTALD---VTIqaqILNLLKDLQRELGlaILFITH-- 209
|
250 260 270
....*....|....*....|....*....|....*.
gi 2306450510 235 eDLkqsDQIAFITEKKAV--------IGPYESLLKN 262
Cdd:COG0444 210 -DL---GVVAEIADRVAVmyagriveEGPVEELFEN 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
25-273 |
3.71e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.40 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 25 KKQRTIANDIPKILEITINNLSIGYDKP------LITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFS 98
Cdd:PRK13631 7 KKKLKVPNPLSDDIILRVKNLYCVFDEKqenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 99 DKKLRFDANFRHDW-------------LKRAI---YLGSEPYLFSGSIIDNLLFA------SKYDRKELIKIF-DKFGL- 154
Cdd:PRK13631 87 DIYIGDKKNNHELItnpyskkiknfkeLRRRVsmvFQFPEYQLFKDTIEKDIMFGpvalgvKKSEAKKLAKFYlNKMGLd 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 155 CSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNID----HENAGIILRAMKrlaKEKIVLII 230
Cdd:PRK13631 167 DSYLERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgeHEMMQLILDAKA---NNKTVFVI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 231 THKIED-LKQSDQIAFITEKKAVIG--PYE-----------------------SLLKNSPSFKNLINQQ 273
Cdd:PRK13631 233 THTMEHvLEVADEVIVMDKGKILKTgtPYEiftdqhiinstsiqvprviqvinDLIKKDPKYKKLYQKQ 301
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
36-243 |
4.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 56.25 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 36 KILEItiNNLSIGYDKPL-ITQL---SWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRhd 111
Cdd:PRK13642 3 KILEV--ENLVFKYEKESdVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 wLKRAI---YLGSEPYLFSGSIIDNLLFASKYD---RKELIKIFDKFGLCSfvsslpDQYDSQVGENGKwLSPGQRQQIA 185
Cdd:PRK13642 79 -LRRKIgmvFQNPDNQFVGATVEDDVAFGMENQgipREEMIKRVDEALLAV------NMLDFKTREPAR-LSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 186 FGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLaKEK---IVLIITHKIEDLKQSDQI 243
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRI 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
61-275 |
5.70e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.53 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 61 LKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDkkLRFDANFRHDWLKRAI-----YLGsepYLFSG------- 128
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGD--ITIDTARSLSQQKGLIrqlrqHVG---FVFQNfnlfphr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 129 ----SIIDNLLFASKYDRKELI----KIFDKFGLCSFVSSLPdqydsqvgengKWLSPGQRQQIAFGRAVAADKNFYIFD 200
Cdd:PRK11264 101 tvleNIIEGPVIVKGEPKEEATararELLAKVGLAGKETSYP-----------RRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2306450510 201 EVTSNIDHENAGIILRAMKRLAKEK-IVLIITHKIEDLKQ-SDQIAFITEKKAV-IGPYESLLKNSpsfKNLINQQFL 275
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVeQGPAKALFADP---QQPRTRQFL 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
57-243 |
7.82e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRF-DANFRHDWLkRAIYLGS----EPYLFSGSII 131
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFgDYSYRSQRI-RMIFQDPstslNPRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 132 D-----NLLFASKYDRKELIKIFDKFGLcsfvssLPDqydsQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTSNI 206
Cdd:PRK15112 111 DfplrlNTDLEPEQREKQIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2306450510 207 DHENAGIILRAMKRL-AKEKIVLI-ITHKIEDLKQ-SDQI 243
Cdd:PRK15112 181 DMSMRSQLINLMLELqEKQGISYIyVTQHLGMMKHiSDQV 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
56-235 |
9.60e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 56 QLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFdANFRhDWLKRA---IY--LGSEPYLfsgSI 130
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF-ASTT-AALAAGvaiIYqeLHLVPEM---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 131 IDNLL---FASKY---DRKELIK----IFDKFGLcsfvsslpdqyDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFD 200
Cdd:PRK11288 97 AENLYlgqLPHKGgivNRRLLNYeareQLEHLGV-----------DIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 2306450510 201 EVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIE 235
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRME 201
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
71-243 |
1.33e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 71 GQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdANFRHDWLKRAI-YLGSEPYLFSGSI---IDNLLFASKydrKELI 146
Cdd:PTZ00243 1343 GRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI---GAYGLRELRRQFsMIPQDPVLFDGTVrqnVDPFLEASS---AEVW 1416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 147 KIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRA-VAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK 225
Cdd:PTZ00243 1417 AALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAlLKKGSGFILMDEATANIDPALDRQIQATVMSAFSAY 1496
|
170
....*....|....*...
gi 2306450510 226 IVLIITHKIEDLKQSDQI 243
Cdd:PTZ00243 1497 TVITIAHRLHTVAQYDKI 1514
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
60-234 |
1.52e-08 |
|
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: 54.34 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 60 SLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEIsfsdKKLRFDANFRHDWLKrAIYLGSEPYLFSgSIIDNLLFASK 139
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI----EIELDTVSYKPQYIK-ADYEGTVRDLLS-SITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 140 YdRKELIKIFdkfglcsfvsSLPDQYDSQVGEngkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMK 219
Cdd:cd03237 95 F-KTEIAKPL----------QIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170
....*....|....*..
gi 2306450510 220 RLA--KEKIVLIITHKI 234
Cdd:cd03237 160 RFAenNEKTAFVVEHDI 176
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
40-236 |
2.66e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDAnfrhdwLKRAIY 118
Cdd:PRK11248 2 LQISHLYADYGgKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG------AERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LGSEPYLFSGSIIDNLLF------ASKYDRKELI-KIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVA 191
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFglqlagVEKMQRLEIAhQMLKKVGLEGAEKRYIWQ-----------LSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2306450510 192 ADKNFYIFDEVTSNID----HENAGIILRAMKRLAKEkiVLIITHKIED 236
Cdd:PRK11248 145 ANPQLLLLDEPFGALDaftrEQMQTLLLKLWQETGKQ--VLLITHDIEE 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
40-236 |
2.89e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 54.07 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANfrhdwLKRAiY 118
Cdd:PRK13536 42 IDLAGVSKSYgDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-----LARA-R 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 119 LGSEPYL----FSGSIIDNLLFASKYDRKELIKIFDKF-GLCSFvSSLPDQYDSQVGEngkwLSPGQRQQIAFGRAVAAD 193
Cdd:PRK13536 116 IGVVPQFdnldLEFTVRENLLVFGRYFGMSTREIEAVIpSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALIND 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2306450510 194 KNFYIFDEVTSNIDHENAGII---LRAMkrLAKEKIVLIITHKIED 236
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIwerLRSL--LARGKTILLTTHFMEE 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
60-243 |
4.62e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 60 SLKI--GHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRF----DAN-------FRH----DWLKRA--IYLG 120
Cdd:COG3845 25 SLTVrpGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIrsprDAIalgigmvHQHfmlvPNLTVAenIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 121 SEPylfsgsiidnlLFASKYDRKELIK----IFDKFGLCsfVSslPDQYdsqVGEngkwLSPGQRQQIAFGRAVAADKNF 196
Cdd:COG3845 105 LEP-----------TKGGRLDRKAARArireLSERYGLD--VD--PDAK---VED----LSVGEQQRVEILKALYRGARI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2306450510 197 YIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIEDLKQ-SDQI 243
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAiADRV 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
58-246 |
6.66e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 58 SWSLKIGHLYALSGQSGSGKSTLAKTL--VAQQKSLAGEISFSDKKLRFdANFR----------HDWLK--------RAI 117
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGEELQA-SNIRdteragiaiiHQELAlvkelsvlENI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPYlfSGSIIDnllFASKYDRKEliKIFDKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQQIAFGRAVAADKNFY 197
Cdd:PRK13549 104 FLGNEIT--PGGIMD---YDAMYLRAQ--KLLAQLKLDINP-------ATPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 198 IFDEVTSNIDHENAGIILRAMKRLAKEKIVLI-ITHKIEDLKQ-SDQIAFI 246
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAHGIACIyISHKLNEVKAiSDTICVI 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
54-262 |
8.10e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 54 ITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHDWLKRAI-------YLGSEPYLF 126
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIqfifqdpYASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 127 SG-SIIDNL----LFASKYDRKELIKIFDKFGLcsfvssLPDQydsqvgengKWLSP-----GQRQQIAFGRAVAADKNF 196
Cdd:PRK10261 420 VGdSIMEPLrvhgLLPGKAAAARVAWLLERVGL------LPEH---------AWRYPhefsgGQRQRICIARALALNPKV 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 197 YIFDEVTSNIDHENAGIILRAMKRLAKEKIV--LIITHKIEDLKQ-SDQIAFITEKKAV-IGPYESLLKN 262
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVeIGPRRAVFEN 554
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
68-260 |
1.31e-07 |
|
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: 52.03 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 68 ALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrFDANFRHdWL---KRAI-YLGSEPYLFSG-SIIDNLLFASKYDR 142
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSARGI-FLpphRRRIgYVFQEARLFPHlSVRGNLLYGRKRAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 143 KELIKI-FDK----FGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRA 217
Cdd:COG4148 107 RAERRIsFDEvvelLGIGHLLDRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2306450510 218 MKRLAKE-KI-VLIITHKIEDLKQ-SDQIAFITEKKAV-IGPYESLL 260
Cdd:COG4148 176 LERLRDElDIpILYVSHSLDEVARlADHVVLLEQGRVVaSGPLAEVL 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
41-234 |
1.75e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 41 TINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdanfrHDWLKRAI-- 117
Cdd:PRK10575 13 ALRNVSFRVpGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL-------ESWSSKAFar 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 ---YLGSEPYLFSGSIIDNLLFASKY------------DRKELIKIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQ 182
Cdd:PRK10575 86 kvaYLPQQLPAAEGMTVRELVAIGRYpwhgalgrfgaaDREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 183 QIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHKI 234
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDI 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
38-201 |
1.86e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.62 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 38 LEITINNL--SIGYDKPLiTQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDAN------- 107
Cdd:PRK10851 1 MSIEIANIkkSFGRTQVL-NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsRLHARdrkvgfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 108 FRHDWLKRAIylgsepylfsgSIIDNLLFA-----------SKYDRKELIKIFDKFGLcsfvSSLPDQYDSQvgengkwL 176
Cdd:PRK10851 80 FQHYALFRHM-----------TVFDNIAFGltvlprrerpnAAAIKAKVTQLLEMVQL----AHLADRYPAQ-------L 137
|
170 180
....*....|....*....|....*
gi 2306450510 177 SPGQRQQIAFGRAVAADKNFYIFDE 201
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDE 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
40-100 |
1.98e-07 |
|
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: 49.37 E-value: 1.98e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDK 100
Cdd:cd03221 1 IELENLSKTYgGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST 62
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
40-207 |
2.31e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.60 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSdKKLR---FD---ANFRHDW 112
Cdd:COG0488 316 LELEGLSKSYgDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-ETVKigyFDqhqEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 113 lkraiylgsepylfsgSIIDNLL-FASKYDRKELIKIFDKFGlcsFVsslPDQYDSQVGEngkwLSPGQRQQIAFGRAVA 191
Cdd:COG0488 395 ----------------TVLDELRdGAPGGTEQEVRGYLGRFL---FS---GDDAFKPVGV----LSGGEKARLALAKLLL 448
|
170
....*....|....*.
gi 2306450510 192 ADKNFYIFDEVTSNID 207
Cdd:COG0488 449 SPPNVLLLDEPTNHLD 464
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
57-235 |
2.35e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 51.00 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHDwLKRAI---YLGSEPYLFSGSIIDN 133
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMK-LRESVgmvFQDPDNQLFSASVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 134 LLFAS---KYDRKELIKIFDKFGLCSFVSSLPDQydsqvgeNGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHEN 210
Cdd:PRK13636 104 VSFGAvnlKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180
....*....|....*....|....*..
gi 2306450510 211 AGIILRAMKRLAKEK--IVLIITHKIE 235
Cdd:PRK13636 177 VSEIMKLLVEMQKELglTIIIATHDID 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
40-243 |
3.62e-07 |
|
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: 49.07 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSI--GYDKPLITQLSWSLKIG-HLYaLSGQSGSGKSTLAKTLVAQQKSLAGEISFSdkklrfdanfrhdWLKRA 116
Cdd:cd03223 1 IELENLSLatPDGRVLLKDLSFEIKPGdRLL-ITGPSGTGKSSLFRALAGLWPWGSGRIGMP-------------EGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 117 IYLGSEPYLFSGSIIDNLLFAskydrkelikifdkfglcsfvsslpdqydsqvgengkW---LSPGQRQQIAFGRAVAAD 193
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIYP-------------------------------------WddvLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 194 KNFYIFDEVTSNIDHENAGiilRAMKRLAKEKIVLI-ITHKIEDLKQSDQI 243
Cdd:cd03223 110 PKFVFLDEATSALDEESED---RLYQLLKELGITVIsVGHRPSLWKFHDRV 157
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
71-234 |
4.89e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 71 GQSGSGKSTLAKTLVAQQKSLAGEISFSdkklrfdanfrhdwLKRAI---YLGSEP----YLFSGSIIDNllFASKYDRK 143
Cdd:PRK13409 372 GPNGIGKTTFAKLLAGVLKPDEGEVDPE--------------LKISYkpqYIKPDYdgtvEDLLRSITDD--LGSSYYKS 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 144 ELIKIFdkfglcsfvsSLPDQYDSQVGEngkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLA- 222
Cdd:PRK13409 436 EIIKPL----------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAe 501
|
170
....*....|...
gi 2306450510 223 -KEKIVLIITHKI 234
Cdd:PRK13409 502 eREATALVVDHDI 514
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
40-251 |
5.02e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.49 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDK-PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdanfrhDW-----L 113
Cdd:PRK11614 6 LSFDKVSAHYGKiQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT-------DWqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIYLGSE-PYLFSG-SIIDNL----LFASKYDRKELIK-IFDKFglcsfvsslPDQYDSQVGENGKwLSPGQRQQIAF 186
Cdd:PRK11614 79 REAVAIVPEgRRVFSRmTVEENLamggFFAERDQFQERIKwVYELF---------PRLHERRIQRAGT-MSGGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2306450510 187 GRAVAADKNFYIFDEVTSNIdhenAGIilramkrlakekIVLIITHKIEDLKQSDQIAFITEKKA 251
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGL----API------------IIQQIFDTIEQLREQGMTIFLVEQNA 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
40-248 |
6.26e-07 |
|
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: 49.31 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQ-KSLAGEISFSDKKLRfdanfRHDW--LKR 115
Cdd:COG1119 4 LELRNVTVRRgGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRG-----GEDVweLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AIylGsepyLFSGSIIDNL-------------LFAS-----KYDR------KELIKIFDkfglcsfVSSLPDQ-YDSqvg 170
Cdd:COG1119 79 RI--G----LVSPALQLRFprdetvldvvlsgFFDSiglyrEPTDeqreraRELLELLG-------LAHLADRpFGT--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 171 engkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK---IVLiITHKIEDLkqsdqIAFIT 247
Cdd:COG1119 143 -----LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaptLVL-VTHHVEEI-----PPGIT 211
|
.
gi 2306450510 248 E 248
Cdd:COG1119 212 H 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
60-244 |
7.42e-07 |
|
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: 48.79 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 60 SLKI--GHLYALSGQSGSGKSTLAKTLvaqqkslAGEISFSDKKLRFDANFRHDW--LKRAIYLGSEPY-LFSG-SIIDN 133
Cdd:cd03301 20 NLDIadGEFVVLLGPSGCGKTTTLRMI-------AGLEEPTSGRIYIGGRDVTDLppKDRDIAMVFQNYaLYPHmTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 134 LLFA---SKYDRKELIK----IFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNI 206
Cdd:cd03301 93 IAFGlklRKVPKDEIDErvreVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2306450510 207 DHEnagiiLRA-----MKRLAKE--KIVLIITH-KIEDLKQSDQIA 244
Cdd:cd03301 162 DAK-----LRVqmraeLKRLQQRlgTTTIYVTHdQVEAMTMADRIA 202
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
40-276 |
9.02e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.74 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDAnfRHDWLKRAI- 117
Cdd:PRK10895 4 LTAKNLAKAYKgRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP--LHARARRGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPYLFSG-SIIDNLLfASKYDRKELIK---------IFDKFGLCSFVSSLpdqydsqvgenGKWLSPGQRQQIAFG 187
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLM-AVLQIRDDLSAeqredraneLMEEFHIEHLRDSM-----------GQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 188 RAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITHKIEDLKQSDQIAFITEKKAVI--GPYESLLKNSP 264
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIahGTPTEILQDEH 229
|
250
....*....|..
gi 2306450510 265 SFKNLINQQFLL 276
Cdd:PRK10895 230 VKRVYLGEDFRL 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
52-265 |
9.67e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 52 PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRfdaNF-RHDWLKRAIYLGSEPYLFSGSI 130
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS---KFgLMDLRKVLGIIPQAPVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 131 IDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYDSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHEN 210
Cdd:PLN03130 1330 RFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 211 AGIILRAMKRLAKEKIVLIITHKIEDLKQSDQIAFITEKKAV-IGPYESLLKNSPS 265
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVeFDTPENLLSNEGS 1465
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
49-252 |
1.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.01 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 49 YDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRF---DANFRHDWLKRAI-YLGSEPY 124
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkDKYIRPVRKRIGMvFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 125 LFSGSIIDNLLFASKYDRKELIKIFDK-------FGLCSFVSSL-PDQydsqvgengkwLSPGQRQQIAFGRAVAADKNF 196
Cdd:PRK13646 98 LFEDTVEREIIFGPKNFKMNLDEVKNYahrllmdLGFSRDVMSQsPFQ-----------MSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 197 YIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDL-KQSDQIAFITEKKAV 252
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVaRYADEVIVMKEGSIV 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
40-243 |
1.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.96 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYD----KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDA--NFRHdwl 113
Cdd:PRK13650 5 IEVKNLTFKYKedqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwDIRH--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 114 KRAIYLGSEPYLFSGSII-DNLLFASK---YDRKELIKIFDK----FGLCSFVSSLPDQydsqvgengkwLSPGQRQQIA 185
Cdd:PRK13650 82 KIGMVFQNPDNQFVGATVeDDVAFGLEnkgIPHEEMKERVNEalelVGMQDFKEREPAR-----------LSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 186 FGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHKIEDLKQSDQI 243
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRV 210
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
48-222 |
1.27e-06 |
|
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: 48.01 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 48 GYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLvAQQK---SLAGEISFSDKKLrfDANFRhdwlKRAIYLGSEPY 124
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL-AGRKtagVITGEILINGRPL--DKNFQ----RSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 125 LFSGS-IIDNLLFaSKYDRKelikifdkfglcsfvsslpdqydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVT 203
Cdd:cd03232 90 HSPNLtVREALRF-SALLRG--------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170
....*....|....*....
gi 2306450510 204 SNIDHENAGIILRAMKRLA 222
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKLA 155
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
42-207 |
1.39e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 49.06 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 42 INNLSIGYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFrhdwlKRAIYLG 120
Cdd:PRK11607 22 IRNLTKSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY-----QRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 121 SEPY-LFSGSIID-NLLFASKYDRKELIKIFDKFG-------LCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVA 191
Cdd:PRK11607 97 FQSYaLFPHMTVEqNIAFGLKQDKLPKAEIASRVNemlglvhMQEFAKRKPHQ-----------LSGGQRQRVALARSLA 165
|
170
....*....|....*.
gi 2306450510 192 ADKNFYIFDEVTSNID 207
Cdd:PRK11607 166 KRPKLLLLDEPMGALD 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
71-237 |
1.68e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 71 GQSGSGKSTLAKTLvaqqkslAGEIS----FSDKKLRFDANFRH-------DWLK-------RAI----YLGSEPYLFSG 128
Cdd:PRK13409 106 GPNGIGKTTAVKIL-------SGELIpnlgDYEEEPSWDEVLKRfrgtelqNYFKklyngeiKVVhkpqYVDLIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 129 SIIDnLLfaSKYD-RKELIKIFDKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNID 207
Cdd:PRK13409 179 KVRE-LL--KKVDeRGKLDEVVERLGLENIL-------DRDISE----LSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190
....*....|....*....|....*....|
gi 2306450510 208 HENAGIILRAMKRLAKEKIVLIITHkieDL 237
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEH---DL 271
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
40-257 |
1.78e-06 |
|
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: 48.00 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDKPLITQ-LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDANfrhdwlKRAI 117
Cdd:cd03300 1 IELENVSKFYGGFVALDgVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItNLPPH------KRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPY-LFSG-SIIDNLLFA------SKYDRKELIK-IFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGR 188
Cdd:cd03300 75 NTVFQNYaLFPHlTVFENIAFGlrlkklPKAEIKERVAeALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 189 AVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIED-LKQSDQIAFITEKKAV-IG-PYE 257
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEEaLTMSDRIAVMNKGKIQqIGtPEE 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
69-235 |
2.23e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 47.70 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 69 LSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDAN----------------FR--HDWlkraiylgsePYLfsgSI 130
Cdd:PRK11124 33 LLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkairelrrnvgmvFQqyNLW----------PHL---TV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 131 IDNLLFA-------SKYD-RKELIKIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEV 202
Cdd:PRK11124 100 QQNLIEApcrvlglSKDQaLARAEKLLERLRLKPYADRFPLH-----------LSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190
....*....|....*....|....*....|....
gi 2306450510 203 TSNIDHENAGIILRAMKRLAKEKIV-LIITHKIE 235
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGITqVIVTHEVE 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
39-257 |
2.53e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYDK--PL----ITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfDANFRH-- 110
Cdd:PRK13645 6 DIILDNVSYTYAKktPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI--PANLKKik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 111 --DWLKRAIYL---GSEPYLFSGSIIDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQYdsqVGENGKWLSPGQRQQIA 185
Cdd:PRK13645 84 evKRLRKEIGLvfqFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2306450510 186 FGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIED-LKQSDQIAFITEKKAV-IG-PYE 257
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQvLRIADEVIVMHEGKVIsIGsPFE 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
51-252 |
2.97e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.12 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 51 KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVaqQKSLAGEISFSDKKL---RFDANFRHdwlKRAIYLgSEPYLFS 127
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA--FRSPKGVKGSGSVLLngmPIDAKEMR---AISAYV-QQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 128 GSII--DNLLF---------ASKYDRKELIK-IFDKFGL--CSfvsslpdqyDSQVGENG--KWLSPGQRQQIAFGRAVA 191
Cdd:TIGR00955 112 PTLTvrEHLMFqahlrmprrVTKKEKRERVDeVLQALGLrkCA---------NTRIGVPGrvKGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 192 ADKNFYIFDEVTSNIDHENAGIILRAMKRLA-KEKIVLIITHK--IEDLKQSDQIAFITEKKAV 252
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQpsSELFELFDKIILMAEGRVA 246
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-248 |
2.98e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 18 KNSFSSQKKQ-RTIANDIpkILEItiNNLsIGYDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEIS 96
Cdd:PRK09700 247 QNRFNAMKENvSNLAHET--VFEV--RNV-TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 97 FSDKKLRFDANFrhDWLKRAIYLGSEPYLFSG-----SIIDNL----------------LFASKYDRKELIKIFDKFGL- 154
Cdd:PRK09700 322 LNGKDISPRSPL--DAVKKGMAYITESRRDNGffpnfSIAQNMaisrslkdggykgamgLFHEVDEQRTAENQRELLALk 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 155 CSFVsslpdqyDSQVGEngkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHK 233
Cdd:PRK09700 400 CHSV-------NQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSE 468
|
250
....*....|....*.
gi 2306450510 234 I-EDLKQSDQIAFITE 248
Cdd:PRK09700 469 LpEIITVCDRIAVFCE 484
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-262 |
3.16e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.11 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 24 QKKQRTIANDIPKILEITINNLSIGydkplITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFS--DKK 101
Cdd:PRK10070 19 QRAFKYIEQGLSKEQILEKTGLSLG-----VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 102 LRFDANFRHDWLKR-AIYLGSEPYLFSGSIIDNLLF-------ASKYDRKELIKIFDKFGLCSFVSSLPDQydsqvgeng 173
Cdd:PRK10070 94 KISDAELREVRRKKiAMVFQSFALMPHMTVLDNTAFgmelagiNAEERREKALDALRQVGLENYAHSYPDE--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 174 kwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNID------HENAGIILRAmkrlAKEKIVLIITHKI-EDLKQSDQIAFI 246
Cdd:PRK10070 165 --LSGGMRQRVGLARALAINPDILLMDEAFSALDplirteMQDELVKLQA----KHQRTIVFISHDLdEAMRIGDRIAIM 238
|
250
....*....|....*..
gi 2306450510 247 TEKKAV-IGPYESLLKN 262
Cdd:PRK10070 239 QNGEVVqVGTPDEILNN 255
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
62-232 |
3.20e-06 |
|
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: 47.36 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 62 KIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEIsfsDKKLRFD---ANFR----HDWLKRAI-----------YLGSEP 123
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF---DDPPDWDeilDEFRgselQNYFTKLLegdvkvivkpqYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 124 YLFSGSIIDNLlfASKYDRKELIKIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVT 203
Cdd:cd03236 101 KAVKGKVGELL--KKKDERGKLDELVDQLELRHVLDRNIDQ-----------LSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 2306450510 204 SNID---HENAGIILRamkRLAKE-KIVLIITH 232
Cdd:cd03236 168 SYLDikqRLNAARLIR---ELAEDdNYVLVVEH 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
71-237 |
3.57e-06 |
|
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: 47.86 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 71 GQSGSGKSTLAKTLVAQQKSLAGEIsfsDKKLRFDA---NFR----HDWLKRaIYLGSE------------PYLFSGSII 131
Cdd:COG1245 106 GPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEvlkRFRgtelQDYFKK-LANGEIkvahkpqyvdliPKVFKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 132 DnLLfaSKYD-RKELIKIFDKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNID-HE 209
Cdd:COG1245 182 E-LL--EKVDeRGKLDELAEKLGLENIL-------DRDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQ 247
|
170 180 190
....*....|....*....|....*....|.
gi 2306450510 210 --NAGiilRAMKRLAKE-KIVLIITHkieDL 237
Cdd:COG1245 248 rlNVA---RLIRELAEEgKYVLVVEH---DL 272
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
40-246 |
4.06e-06 |
|
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: 46.59 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDKPLITQ-----LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEIS---FSDKKLRFDANFRHD 111
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavdgVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 112 WL--KRAIYlgsePYLfsgSIIDNLL-FASKYDRK------ELIKIFDKFGLCSFVsslpdqyDSQVGEngkwLSPGQRQ 182
Cdd:cd03266 82 FVsdSTGLY----DRL---TARENLEyFAGLYGLKgdeltaRLEELADRLGMEELL-------DRRVGG----FSTGMRQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 183 QIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIEDLKQ-SDQIAFI 246
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERlCDRVVVL 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
57-235 |
5.02e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSlAGEISFSDKKLrfdanfrHDWLKRAI--------------YLGSE 122
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPL-------HNLNRRQLlpvrhriqvvfqdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 123 PYLFSGSIIDNLL-----FASKYDRKE-LIKIFDKFGLCsfvsslPD---QYDSQvgengkwLSPGQRQQIAFGRAVAAD 193
Cdd:PRK15134 377 PRLNVLQIIEEGLrvhqpTLSAAQREQqVIAVMEEVGLD------PEtrhRYPAE-------FSGGQRQRIAIARALILK 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2306450510 194 KNFYIFDEVTSNIDHENAGIILRAMKRL-AKEKIVLI-ITHKIE 235
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLfISHDLH 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
64-239 |
1.29e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 64 GHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKklrfdaNFRHDWLKRAIYLGSEPYLFSGSIIDNL-----LFAS 138
Cdd:PRK09700 31 GEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI------NYNKLDHKLAAQLGIGIIYQELSVIDELtvlenLYIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 139 KYDRKEL--IKIFDKFGLCSFVSSLPDQYDSQVGENGKW--LSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGII 214
Cdd:PRK09700 105 RHLTKKVcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVanLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL 184
|
170 180
....*....|....*....|....*.
gi 2306450510 215 LRAMKRLAKE-KIVLIITHKIEDLKQ 239
Cdd:PRK09700 185 FLIMNQLRKEgTAIVYISHKLAEIRR 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-260 |
2.07e-05 |
|
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: 45.56 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 20 SFSSQKKQRTI--ANDIPKILEITINNLSIgyDKPLIT---QLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGE 94
Cdd:TIGR03269 263 GVSEVEKECEVevGEPIIKVRNVSKRYISV--DRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 95 ISF--SDK-----KLRFDANFRhdwLKRAI-YLGSEPYLFS-GSIIDNLLFASKYD-------RKELIKI----FDKFGL 154
Cdd:TIGR03269 341 VNVrvGDEwvdmtKPGPDGRGR---AKRYIgILHQEYDLYPhRTVLDNLTEAIGLElpdelarMKAVITLkmvgFDEEKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 155 CSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNID----HENAGIILRAMKRLakEKIVLII 230
Cdd:TIGR03269 418 EEILDKYPDE-----------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEM--EQTFIIV 484
|
250 260 270
....*....|....*....|....*....|..
gi 2306450510 231 THKIE-DLKQSDQIAFITEKKAV-IGPYESLL 260
Cdd:TIGR03269 485 SHDMDfVLDVCDRAALMRDGKIVkIGDPEEIV 516
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
40-252 |
2.30e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGY-----DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKS-----LAGEISFSDKKLRF--DAN 107
Cdd:PRK15134 6 LAIENLSVAFrqqqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHasEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 108 FRHDWLKRAIYLGSEPY--LFSGSIIDNLLFA---------SKYDRKELIKIFDKFGLCSFVSSLPDqYDSQvgengkwL 176
Cdd:PRK15134 86 LRGVRGNKIAMIFQEPMvsLNPLHTLEKQLYEvlslhrgmrREAARGEILNCLDRVGIRQAAKRLTD-YPHQ-------L 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 177 SPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE--KIVLIITHKIEDLKQ-SDQIAFITEKKAV 252
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
52-243 |
2.46e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 52 PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDANFRHdwlKRAIYL-GSEPYLFSG- 128
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKAH---QLGIYLvPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 129 SIIDNLLF---ASKYDRKELIKIFDKFGlCSFvsslpdQYDSQVGEngkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSN 205
Cdd:PRK15439 102 SVKENILFglpKRQASMQKMKQLLAALG-CQL------DLDSSAGS----LEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2306450510 206 ID-HENAGIILRAMKRLAKEKIVLIITHKIEDLKQ-SDQI 243
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRI 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
40-243 |
2.50e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.02 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNLSIGYDKPLITQ-LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfdanfrHDW--LKR- 115
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-------NDVppAERg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 --------AIYlgsePYLfsgSIIDNLLFASKYDRKELIKIfdkfglcsfvsslpDQYDSQVGE----------NGKWLS 177
Cdd:PRK11000 77 vgmvfqsyALY----PHL---SVAENMSFGLKLAGAKKEEI--------------NQRVNQVAEvlqlahlldrKPKALS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2306450510 178 PGQRQQIAFGRAVAADKNFYIFDEVTSNIDhenAGI-------ILRAMKRLAKEKIVliITH-KIEDLKQSDQI 243
Cdd:PRK11000 136 GGQRQRVAIGRTLVAEPSVFLLDEPLSNLD---AALrvqmrieISRLHKRLGRTMIY--VTHdQVEAMTLADKI 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
57-238 |
3.03e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.42 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFS----------------DKKLRFDANFRH---DWlkRAI 117
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelrNQKLGFIYQFHHllpDF--TAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 118 YLGSEPYLFSGSiidnllfASKYDRKELIKIFDKFGLCSFVSSLPDQydsqvgengkwLSPGQRQQIAFGRAVAADKNFY 197
Cdd:PRK11629 106 ENVAMPLLIGKK-------KPAEINSRALEMLAAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2306450510 198 IFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHkieDLK 238
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTH---DLQ 207
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
176-257 |
3.33e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 176 LSPGQRQQIA----FGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK-IVLIITHKIEDLKQSDQIAFIteKK 250
Cdd:cd03227 78 LSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKLIHI--KK 155
|
....*..
gi 2306450510 251 AVIGPYE 257
Cdd:cd03227 156 VITGVYK 162
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
42-151 |
3.36e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.06 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 42 INNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSdKKLRfdanfrhdwlkraI-YL 119
Cdd:COG0488 1 LENLSKSFgGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR-------------IgYL 66
|
90 100 110
....*....|....*....|....*....|...
gi 2306450510 120 GSEPYLFSG-SIIDNLLFASKyDRKELIKIFDK 151
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDA-ELRALEAELEE 98
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-100 |
3.69e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 3.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2306450510 40 ITINNLSIGYD-KPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDK 100
Cdd:PRK15064 320 LEVENLTKGFDnGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN 381
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
62-223 |
4.78e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 62 KIGHLYALSGQSGSGKSTLAKTLvAQQKSlAGEISFSDKKLRF---DANFrhdwlKRAI-YLGSEP-YLFSGSIIDNLLF 136
Cdd:TIGR00956 787 KPGTLTALMGASGAGKTTLLNVL-AERVT-TGVITGGDRLVNGrplDSSF-----QRSIgYVQQQDlHLPTSTVRESLRF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 137 ASKYDRKELIKIFDKFglcSFVSSLPD-----QY-DSQVGENGKWLSPGQRQQIAFGRAVAADKNFYIF-DEVTSNIDHE 209
Cdd:TIGR00956 860 SAYLRQPKSVSKSEKM---EYVEEVIKllemeSYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQ 936
|
170
....*....|....
gi 2306450510 210 NAGIILRAMKRLAK 223
Cdd:TIGR00956 937 TAWSICKLMRKLAD 950
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
57-207 |
5.10e-05 |
|
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: 44.29 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 57 LSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSlAGEISFSDK---KLRFDANFRhdwLKRAI-------YlGS-EPYL 125
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQdldGLSRRALRP---LRRRMqvvfqdpF-GSlSPRM 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 126 FSGSIIDN-LLF----ASKYDRKELI-KIFDKFGLcsfvssLPDQYDSQVGEngkwLSPGQRQQIAFGRAVAADKNFYIF 199
Cdd:COG4172 380 TVGQIIAEgLRVhgpgLSAAERRARVaEALEEVGL------DPAARHRYPHE----FSGGQRQRIAIARALILEPKLLVL 449
|
....*...
gi 2306450510 200 DEVTSNID 207
Cdd:COG4172 450 DEPTSALD 457
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
38-276 |
6.88e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 43.54 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 38 LEITINNLSIGYDKPLITQL------SWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEIS--FSDKKLRfDANFR 109
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPTELkaldnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNK-KKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 110 HDWLKRAIYLG-----------------------SEPYLFSGSIIDNLLFA------SKYDRKELIKIFDKfglcsfVSS 160
Cdd:PRK13651 80 KEKVLEKLVIQktrfkkikkikeirrrvgvvfqfAEYQLFEQTIEKDIIFGpvsmgvSKEEAKKRAAKYIE------LVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 161 LPDQYDSQVGENgkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIED-LK 238
Cdd:PRK13651 154 LDESYLQRSPFE---LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNvLE 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 2306450510 239 QSDQIAFITEKKavigpyesLLKNSPSFKNLINQQFLL 276
Cdd:PRK13651 231 WTKRTIFFKDGK--------IIKDGDTYDILSDNKFLI 260
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
16-99 |
8.71e-05 |
|
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: 43.77 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 16 DDKNSFSSQKKQRTIANDIP-------KILEItiNNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQ 87
Cdd:TIGR03719 294 EELLSQEFQKRNETAEIYIPpgprlgdKVIEA--ENLTKAFgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ 371
|
90
....*....|..
gi 2306450510 88 QKSLAGEISFSD 99
Cdd:TIGR03719 372 EQPDSGTIEIGE 383
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
54-239 |
9.39e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.89 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 54 ITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLrfDANFRHDWLKRA------IYLGSEPYLFS 127
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI--TPETGNKNLKKLrkkvslVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 128 GSIID-------NLLFASKYDRKELIKIFDKFGLcsfvsslpdqyDSQVGENGKW-LSPGQRQQIAFGRAVAADKNFYIF 199
Cdd:PRK13641 101 NTVLKdvefgpkNFGFSEDEAKEKALKWLKKVGL-----------SEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2306450510 200 DEVTSNIDHENAGIILRAMKRLAKE-KIVLIITHKIEDLKQ 239
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAE 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
54-243 |
1.04e-04 |
|
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: 42.42 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 54 ITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKL-RFDANfrhdwlKRAIyLG-----SEPYLFS 127
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPH------EIAR-LGigrtfQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 128 G-SIIDNLL----------FASKYDRKELIKIFDK-FGLCSFVSsLPDQYDSQVGEngkwLSPGQRQQIAFGRAVAADKN 195
Cdd:cd03219 89 ElTVLENVMvaaqartgsgLLLARARREEREARERaEELLERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2306450510 196 FYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITHKIEDLKQ-SDQI 243
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSlADRV 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
39-243 |
1.17e-04 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 43.14 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 39 EITINNLSIGYD-----KPLitqlswSLKI--GHLYALSGQSGSGKSTLAKTLvaqqkslA-------GEISFSDKklrf 104
Cdd:COG3839 3 SLELENVSKSYGgvealKDI------DLDIedGEFLVLLGPSGCGKSTLLRMI-------AgledptsGEILIGGR---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 105 DANfrhdWL---KR---------AIYlgsePYLfsgSIIDNLLFA------SKYDRKELIK-IFDKFGLCSFVSSLPDQy 165
Cdd:COG3839 66 DVT----DLppkDRniamvfqsyALY----PHM---TVYENIAFPlklrkvPKAEIDRRVReAAELLGLEDLLDRKPKQ- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 166 dsqvgengkwLSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHEnagiiLRA-----MKRLAKE-KIVLII-THkiedlk 238
Cdd:COG3839 134 ----------LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK-----LRVemraeIKRLHRRlGTTTIYvTH------ 192
|
....*
gi 2306450510 239 qsDQI 243
Cdd:COG3839 193 --DQV 195
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
40-102 |
2.30e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 2.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 40 ITINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQ--KSLAGEISFSDKKL 102
Cdd:PRK09580 2 LSIKDLHVSVeDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDL 67
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
37-232 |
2.38e-04 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 41.80 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 37 ILEITINNLsigydkPLITQLSWSLKIGhLYALSGQSGSGKSTL--AKTLVAQQKSLAGEISFSDKKL----RFDANFRH 110
Cdd:cd03241 1 LLELSIKNF------ALIEELELDFEEG-LTVLTGETGAGKSILldALSLLLGGRASADLIRSGAEKAvvegVFDISDEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 111 D---WLKRAIYLGSEPYLFSGSI---------IDNLLFASKYDRKELIKIFDKFGLCSFVSSLPDQY-----DSQVGENG 173
Cdd:cd03241 74 EakaLLLELGIEDDDDLIIRREIsrkgrsryfINGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERqldllDGGLDDVE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2306450510 174 KWLS--PGQRQ----QIAFG----------RAVAADKNF---YIFDEVTSNIDHENAGIILRAMKRLAKEKIVLIITH 232
Cdd:cd03241 154 FLFStnPGEPLkplaKIASGgelsrlmlalKAILARKDAvptLIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITH 231
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
64-101 |
2.53e-04 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 41.64 E-value: 2.53e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2306450510 64 GHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKK 101
Cdd:COG1162 166 GKTSVLVGQSGVGKSTLINALLPDADLATGEISEKLGR 203
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
54-246 |
3.26e-04 |
|
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: 40.38 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 54 ITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSdkklRFDANfrhdwlkRAIYLGSepylfSGSIIDN 133
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLP----KFSRN-------KLIFIDQ-----LQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 134 LLFASKYDRKelikifdkfglcsfVSSLpdqydsQVGENgkwlspgQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGI 213
Cdd:cd03238 75 GLGYLTLGQK--------------LSTL------SGGEL-------QRVKLASELFSEPPGTLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|....
gi 2306450510 214 ILRAMKRLAKEK-IVLIITHKIEDLKQSDQIAFI 246
Cdd:cd03238 128 LLEVIKGLIDLGnTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
40-246 |
3.44e-04 |
|
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: 40.59 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 40 ITINNL--SIGyDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLA--GEISFSDKKLRfDANFrHDWLKR 115
Cdd:cd03217 1 LEIKDLhvSVG-GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDIT-DLPP-EERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 116 AIYLGS-EPYLFSGsiidnllfaskydrkelIKIFDkfglcsFVSSlpdqydsqVGENgkwLSPGQRQQIAFGRAVAADK 194
Cdd:cd03217 78 GIFLAFqYPPEIPG-----------------VKNAD------FLRY--------VNEG---FSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2306450510 195 NFYIFDEVTSNIDHENAGIILRAMKRLAKEKI-VLIITH--KIEDLKQSDQIAFI 246
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREEGKsVLIITHyqRLLDYIKPDRVHVL 178
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
64-101 |
3.58e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.22 E-value: 3.58e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2306450510 64 GHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKK 101
Cdd:pfam03193 106 GKTTVLAGQSGVGKSTLLNALLPELDLRTGEISEKLGR 143
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
64-101 |
4.52e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.46 E-value: 4.52e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2306450510 64 GHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKK 101
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGEISEKLGR 122
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
40-103 |
4.62e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 40.91 E-value: 4.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2306450510 40 ITINNLS--IGyDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLR 103
Cdd:PRK13548 3 LEARNLSvrLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA 67
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
176-269 |
7.92e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.07 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 176 LSPGQRQQIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLAKEK--IVLIITHKIEDLKQSDQIAFITEKKAVI 253
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVM 224
|
90
....*....|....*..
gi 2306450510 254 -GPYESLLKNSPSFKNL 269
Cdd:PRK13633 225 eGTPKEIFKEVEMMKKI 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
35-78 |
7.93e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.07 E-value: 7.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2306450510 35 PKILEItiNNLSIGYDKPLITQLSWSLKIGHLYALSGQSGSGKS 78
Cdd:PRK10418 2 PQQIEL--RNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKS 43
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-80 |
1.39e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 1.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2306450510 27 QRTIANDIPKILeitINNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTL 80
Cdd:PRK10938 251 RHALPANEPRIV---LNNGVVSYnDRPILHNLSWQVNPGEHWQIVGPNGAGKSTL 302
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
176-207 |
1.77e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.44 E-value: 1.77e-03
10 20 30
....*....|....*....|....*....|..
gi 2306450510 176 LSPGQRQQIAFGRAVAADKNFYIFDEVTSNID 207
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
36-232 |
1.86e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 36 KILEITINNLSIGyDKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQ--KSLAGEISFSDKK-LRFDANFRHdw 112
Cdd:CHL00131 6 PILEIKNLHASVN-ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESiLDLEPEERA-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 113 lKRAIYLGSE-PYLFSG-SIIDNLLFASKYDRKELIKifDKFGLCSFVSSLPDQYDsQVGENGKWL--------SPGQRQ 182
Cdd:CHL00131 83 -HLGIFLAFQyPIEIPGvSNADFLRLAYNSKRKFQGL--PELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2306450510 183 QIAFGRAVAADKNFYIFDEVTSNIDHENAGIILRAMKRLA-KEKIVLIITH 232
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITH 209
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
40-103 |
1.86e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.45 E-value: 1.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2306450510 40 ITINNLSIGYDK-----PLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLR 103
Cdd:PRK10261 13 LAVENLNIAFMQeqqkiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-95 |
1.86e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 16 DDKNSFSSQKKQRTIANDIP-------KILEItiNNLSIGY-DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQ 87
Cdd:PRK11819 296 EELLSEEYQKRNETNEIFIPpgprlgdKVIEA--ENLSKSFgDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ 373
|
....*...
gi 2306450510 88 QKSLAGEI 95
Cdd:PRK11819 374 EQPDSGTI 381
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
58-100 |
2.49e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 38.75 E-value: 2.49e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2306450510 58 SWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDK 100
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR 68
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
66-87 |
2.72e-03 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 37.59 E-value: 2.72e-03
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
58-103 |
2.97e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 2.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2306450510 58 SWsLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLR 103
Cdd:PRK01889 190 AW-LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVREDDSKGR 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
50-215 |
3.55e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 37.91 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 50 DKPLITQLSWSLKIGHLYALSGQSGSGKSTLAKTLVAQQKSLAGEISFSDKKLRFDANFRHdwlkrAIYLGSEPYLFSG- 128
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF-----MAYLGHLPGLKADl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2306450510 129 SIIDNLLFaskydrkelikifdkfgLCSFVSSLPDQYDSQ----VGENG------KWLSPGQRQQIAFGRAVAADKNFYI 198
Cdd:PRK13543 98 STLENLHF-----------------LCGLHGRRAKQMPGSalaiVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWL 160
|
170
....*....|....*..
gi 2306450510 199 FDEVTSNIDHEnaGIIL 215
Cdd:PRK13543 161 LDEPYANLDLE--GITL 175
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
64-92 |
5.28e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 36.97 E-value: 5.28e-03
10 20
....*....|....*....|....*....
gi 2306450510 64 GHLYALSGQSGSGKSTLAKTLVAQQKSLA 92
Cdd:COG0194 2 GKLIVLSGPSGAGKTTLVKALLERDPDLR 30
|
|
| |
