|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-219 |
6.40e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 6.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR-LVTENEKSLNNIHLMSE 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKLKIKSLFHLMEGFYG---NFDWRLANEMLSEFELEP--TKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVL 156
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGlprKEARERIDELLELFGLTDaaDRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 157 GLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENT 219
Cdd:COG1131 161 GLDPEARRELWE-LLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-220 |
2.68e-48 |
|
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: 160.79 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR-LVTENEKSLNNIHLMSE 81
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKLKIKSLFHLMEGFYGNFDWRL---ANEMLSEFELEPT--KRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVL 156
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELkkrIEELIELLGLEEFldRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505238906 157 GLDANHRELFYNYLIETYQEnPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENTH 220
Cdd:COG4555 162 GLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-206 |
5.99e-37 |
|
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: 129.05 E-value: 5.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEN-EKSLNNIHLMSE 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEpEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKLKIKslfhlmegfygnfdwrlanEMLsefeleptkrmnKLSTGYRsiAKLIIALCV---PcEYIFLDEPVLGL 158
Cdd:cd03230 81 EPSLYENLTVR-------------------ENL------------KLSGGMK--QRLALAQALlhdP-ELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505238906 159 DANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:cd03230 127 DPESRREFWE-LLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-209 |
8.83e-33 |
|
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: 119.61 E-value: 8.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQaEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNN-IHLMSE 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKLKIKSLFHLMEGFYG----NFDWRLAnEMLSEFELEP--TKRMNKLSTGYR---SIAKLIIALcvPcEYIFLD 152
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGipskEVKARVD-EVLELVNLGDraKKKIGSLSGGMRrrvGIAQALVGD--P-SILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 153 EPVLGLDANHRELFYNYLIETYQEnpRTFVISTHLIEEISNLLEKVIILDKGKIIKD 209
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-207 |
1.95e-32 |
|
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: 118.76 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGK--KNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR-LVTENEKSLNNIHLM 79
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 80 SEDDLYPSKLKIKSLFHLMEGFYGNFDW---RLANEMLSEFELEP--TKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEP 154
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSeikEEVELLLRVLGLTDkaNKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505238906 155 VLGLDANHRELFYNyLIETYQENpRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:cd03263 161 TSGLDPASRRAIWD-LILEVRKG-RSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-209 |
5.40e-31 |
|
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: 114.62 E-value: 5.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNI-HLMSEDD 83
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIgALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 84 LYP-----SKLKIKSLFHLmegfygnFDWRLANEMLSEFEL--EPTKRMNKLSTGYRsiAKLIIALCV---PcEYIFLDE 153
Cdd:cd03268 83 FYPnltarENLRLLARLLG-------IRKKRIDEVLDVVGLkdSAKKKVKGFSLGMK--QRLGIALALlgnP-DLLILDE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 154 PVLGLD----ANHRELFYNylietYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKD 209
Cdd:cd03268 153 PTNGLDpdgiKELRELILS-----LRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-205 |
2.78e-27 |
|
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: 103.48 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEnekslnnihlmseddl 84
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 ypsklkikslfhlmegfygNFDWRLANEMLSEFEleptkrmnkLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRE 164
Cdd:cd00267 66 -------------------LPLEELRRRIGYVPQ---------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505238906 165 LFYNYLIETYQENpRTFVISTHLIEEISNLLEKVIILDKGK 205
Cdd:cd00267 118 RLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-218 |
6.76e-27 |
|
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: 104.72 E-value: 6.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTY-GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenEKSLNNIH---- 77
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRELRrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 ----------LMS--EDDLypsklkiksLFHLMegfygNFD------WRLANEMLSEFELEP--TKRMNKLSTGYR---S 134
Cdd:COG1122 79 lvfqnpddqlFAPtvEEDV---------AFGPE-----NLGlpreeiRERVEEALELVGLEHlaDRPPHELSGGQKqrvA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 135 IAkLIIALCvPcEYIFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVEN 214
Cdd:COG1122 145 IA-GVLAME-P-EVLVLDEPTAGLDPRGRRELLE-LLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
....
gi 505238906 215 ILEN 218
Cdd:COG1122 221 VFSD 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-207 |
1.24e-26 |
|
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: 103.51 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKslNNIHLMSED 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR--NRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 -DLYPsKLKIKS-LFHL--MEGFYGNFDWRLANEMLSEFELEP--TKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVL 156
Cdd:cd03269 79 rGLYP-KMKVIDqLVYLaqLKGLKKEEARRRIDEWLERLELSEyaNKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505238906 157 GLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:cd03269 158 GLDPVNVELLKD-VIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-207 |
5.66e-25 |
|
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: 99.36 E-value: 5.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYG--KKNVLNNISVNFQAEK--IYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDG-RLVTENEKSLNNIH 77
Cdd:cd03266 2 ITADALTKRFRdvKKTVQAVDGVSFTVKPgeVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 LMSEDD-LYPsKLKIKSLFHLMEGFYG----NFDWRLaNEMLSEFELEPT--KRMNKLSTGYRSIAKLIIALCVPCEYIF 150
Cdd:cd03266 82 FVSDSTgLYD-RLTARENLEYFAGLYGlkgdELTARL-EELADRLGMEELldRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 151 LDEPVLGLDANHRELFYNYlIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:cd03266 160 LDEPTTGLDVMATRALREF-IRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-215 |
8.02e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.57 E-value: 8.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEneKSLNNIHLMSE 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP--EDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 D-DLYPsKLKIKSlfHLMegFYGnfdwRL-----------ANEMLSEFELEP--TKRMNKLSTGYRSIAKLIIAL-CVPc 146
Cdd:COG4152 79 ErGLYP-KMKVGE--QLV--YLA----RLkglskaeakrrADEWLERLGLGDraNKKVEELSKGNQQKVQLIAALlHDP- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 147 EYIFLDEPVLGLDANHRELFYNYLIEtYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENI 215
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-207 |
1.01e-24 |
|
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: 98.36 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHLMSED 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 D-LYPSKLKIKSL-FHLMEGFYGNFDWRL-ANEMLSEFELEP--TKRMNKLSTGYR---SIAKliiALCVPCEYIFLDEP 154
Cdd:cd03259 81 YaLFPHLTVAENIaFGLKLRGVPKAEIRArVRELLELVGLEGllNRYPHELSGGQQqrvALAR---ALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505238906 155 VLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-221 |
2.83e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.85 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSL------NNI 76
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIgyvpqrAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 77 hlmseDDLYPSK---------LKIKSLFhlmeGFYGNFDWRLANEMLSEFELEP--TKRMNKLSTGYR---SIAKliiAL 142
Cdd:COG1121 87 -----DWDFPITvrdvvlmgrYGRRGLF----RRPSRADREAVDEALERVGLEDlaDRPIGELSGGQQqrvLLAR---AL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 143 CVPCEYIFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGkIIKDDSVENILENTHI 221
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENL 231
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-278 |
2.81e-23 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 96.69 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 10 KTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR-LVTENEKSLNNIHLMSEDDLYPSK 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYdVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 89 LKIKSLFHLMEGFYGNFDWRL---ANEMLSEFEL-EPTKRMNK-LSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHR 163
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAeerAEELLELFELgEAADRPVGtYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 164 ELFYNYlIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENI--------LENTHIVTGSIEE------V 229
Cdd:TIGR01188 161 RAIWDY-IRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELkrrlgkdtLESRPRDIQSLKVevsmliA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 230 ETFTKQLQILEKTTLGGSLTAYVkGELPQKKM--------GNIKIESM-----SLQDYFMKI 278
Cdd:TIGR01188 240 ELGETGLGLLAVTVDSDRIKILV-PDGDETVPeiveaairNGIRIRSIsterpSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-215 |
4.99e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 93.97 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR-LVTENEKSLNNIHLMSE 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHdVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKLKIKSLFHLMEGFYG--NFDWR-LANEMLSEFEL--EPTKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVL 156
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGvpGAERReRIDELLDFVGLleAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 157 GLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENI 215
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-186 |
6.12e-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: 93.31 E-value: 6.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLN-NIHLM 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 80 SEDDLYPSKLKIKSLFHLMEGFYG-NFDWRLANEMLSEFELEP--TKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVL 156
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGlRADREAIDEALEAVGLAGlaDLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|
gi 505238906 157 GLDANHRELFYNyLIETYQENPRTFVISTH 186
Cdd:COG4133 161 ALDAAGVALLAE-LIAAHLARGGAVLLTTH 189
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-209 |
7.34e-23 |
|
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: 92.50 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIHLMSEDDL 84
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK----------DLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 -----Y-PSKLKIKSLFHLMEgfygnfdwrlanemlsefeleptKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGL 158
Cdd:cd03214 72 arkiaYvPQALELLGLAHLAD-----------------------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505238906 159 DANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKD 209
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-205 |
7.98e-23 |
|
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: 93.30 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKN--VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenEKSLNNIHLMS-- 80
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 --------------EDDLypsklkiksLFHL-MEGFYGNFDWRLANEMLSEFELEP--TKRMNKLSTGYRSIAKLIIALC 143
Cdd:cd03225 80 vfqnpddqffgptvEEEV---------AFGLeNLGLPEEEIEERVEEALELVGLEGlrDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 144 VPCEYIFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGK 205
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLE-LLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-216 |
3.12e-22 |
|
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: 92.80 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIHLMSED 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR----------DLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 DL---------------------------YPsklkikslfHLmeGFYGNF---DWRLANEMLSEFELEP--TKRMNKLST 130
Cdd:COG1120 72 ELarriayvpqeppapfgltvrelvalgrYP---------HL--GLFGRPsaeDREAVEEALERTGLEHlaDRPVDELSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 131 GYR---SIAKliiALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:COG1120 141 GERqrvLIAR---ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
....*....
gi 505238906 208 KDDSVENIL 216
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-216 |
8.58e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 91.30 E-value: 8.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEnekslnnihlMSEDDL 84
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT----------TPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 ------------YPSKLKIKSLFhlmeGFyGNF----------DWRLANEMLSEFELEP--TKRMNKLSTGYRSIAKLII 140
Cdd:COG4604 74 akrlailrqenhINSRLTVRELV----AF-GRFpyskgrltaeDREIIDEAIAYLDLEDlaDRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 141 ALCVPCEYIFLDEPVLGLDANH-RELFyNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENIL 216
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHsVQMM-KLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-205 |
1.11e-21 |
|
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: 89.17 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENekslnnihlmsED 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-----------ED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 DLYPSKLKIKSLFHlmegfygnfDWRLANEMlSEFEleptKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANH 162
Cdd:cd03229 70 ELPPLRRRIGMVFQ---------DFALFPHL-TVLE----NIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505238906 163 RELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGK 205
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-210 |
2.42e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 90.08 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 12 YGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKS-LNNIHLMSED------DL 84
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKfLRRIGVVFGQktqlwwDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 YP--SKLKIKSLFHLMEGFYGNFDWRLAnEMLsefELEPT--KRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDA 160
Cdd:cd03267 111 PVidSFYLLAAIYDLPPARFKKRLDELS-ELL---DLEELldTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505238906 161 NHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDD 210
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-220 |
3.41e-21 |
|
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: 89.65 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIHLMSEDDL 84
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQ----------DITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 YPSKLKI----------KSL-------FHLMEgfYGNFDW----RLANEMLSEFELEPT-KRM-NKLSTGYR---SIAKl 138
Cdd:COG1127 78 YELRRRIgmlfqggalfDSLtvfenvaFPLRE--HTDLSEaeirELVLEKLELVGLPGAaDKMpSELSGGMRkrvALAR- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 139 iiALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:COG1127 155 --ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
..
gi 505238906 219 TH 220
Cdd:COG1127 233 DD 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-206 |
3.81e-21 |
|
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: 88.74 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVtenEKSLNNIHLMSE--- 81
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL---EKERKRIGYVPQrrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 -DDLYPskLKIK-----SLFHLMEGF--YGNFDWRLANEML-----SEFElepTKRMNKLSTGYRSIAKLIIALCVPCEY 148
Cdd:cd03235 79 iDRDFP--ISVRdvvlmGLYGHKGLFrrLSKADKAKVDEALervglSELA---DRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 149 IFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYE-LLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
5.72e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.61 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR-LVTENEKSL-NNIHL 78
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpISMLSSRQLaRRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 MSEDDLYPSKLKIKSLFHlmegfYGNFDW-----RLA--NEMLSEFELEPT-------KRMNKLSTGYRSIAKLIIALCV 144
Cdd:PRK11231 81 LPQHHLTPEGITVRELVA-----YGRSPWlslwgRLSaeDNARVNQAMEQTrinhladRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 145 PCEYIFLDEPVLGLDANHR-ELFynYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENIL 216
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQvELM--RLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-218 |
4.02e-18 |
|
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: 81.23 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNI---- 76
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVgfvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 77 -------HLMSEDDL-----------YPSKLKIK----SLFHLMEgfygnFDWrLANEMLSEfeleptkrmnkLSTGYRS 134
Cdd:cd03296 81 qhyalfrHMTVFDNVafglrvkprseRPPEAEIRakvhELLKLVQ-----LDW-LADRYPAQ-----------LSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 135 IAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVEN 214
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
....
gi 505238906 215 ILEN 218
Cdd:cd03296 224 VYDH 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-220 |
4.29e-18 |
|
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: 81.01 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIHLMSEDDL 84
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGE----------DISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 YPSKLKIKSLFH-----------------LMEgfYGNFD----WRLANEMLSEFELEPTKRM--NKLSTGYR---SIAKl 138
Cdd:cd03261 73 YRLRRRMGMLFQsgalfdsltvfenvafpLRE--HTRLSeeeiREIVLEKLEAVGLRGAEDLypAELSGGMKkrvALAR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 139 iiALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:cd03261 150 --ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
..
gi 505238906 219 TH 220
Cdd:cd03261 228 DD 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-209 |
3.56e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 78.16 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIE--NLYKTYGKKN----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvteneksln 74
Cdd:COG1136 1 MSPLLElrNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 75 NIHLMSEDDLypSKLKIKSL------FHLMEGF-----------YGNFDWR----LANEMLSEFELEptKRMNK----LS 129
Cdd:COG1136 71 DISSLSEREL--ARLRRRHIgfvfqfFNLLPELtalenvalpllLAGVSRKerreRARELLERVGLG--DRLDHrpsqLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 130 TGYR---SIA-------KLIIAlcvpceyiflDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHlIEEISNLLEKVI 199
Cdd:COG1136 147 GGQQqrvAIAralvnrpKLILA----------DEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH-DPELAARADRVI 215
|
250
....*....|
gi 505238906 200 ILDKGKIIKD 209
Cdd:COG1136 216 RLRDGRIVSD 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-218 |
3.57e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 78.35 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTE---NEKS-LNNIHL 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKRArLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 MSEDDLYpSKLKIK-SLFHLMEGFYGNFDWRL--ANEMLSEFELEPTkRMNK---LSTGYRSIAKLIIALCVPCEYIFLD 152
Cdd:cd03218 81 PQEASIF-RKLTVEeNILAVLEIRGLSKKEREekLEELLEEFHITHL-RKSKassLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 153 EPVLGLDA-NHRELfyNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:cd03218 159 EPFAGVDPiAVQDI--QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-216 |
4.48e-17 |
|
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: 78.59 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 12 YGKKNVLNNIsvNFQAEKiyG----LLGNNGAGKSTLLNIINNRIFDTKGK-ITLDG-RLVTENEKSL-NNIHLMSED-- 82
Cdd:COG1119 13 RGGKTILDDI--SWTVKP--GehwaILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGeRRGGEDVWELrKRIGLVSPAlq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 DLYPSKLKIKSLfhLMEGFYGNF---------DWRLANEMLSEFELEP--TKRMNKLSTGYRS---IA-------KLIIa 141
Cdd:COG1119 89 LRFPRDETVLDV--VLSGFFDSIglyreptdeQRERARELLELLGLAHlaDRPFGTLSQGEQRrvlIAralvkdpELLI- 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 142 lcvpceyifLDEPVLGLDANHRELFYNyLIETY-QENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENIL 216
Cdd:COG1119 166 ---------LDEPTAGLDLGARELLLA-LLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-205 |
6.66e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.56 E-value: 6.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLdgrlvtenekslnnihlmsed 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 dlyPSKLKIkslfhlmeGFYgnfdwrlanemlsefeleptkrmNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANH 162
Cdd:cd03221 60 ---GSTVKI--------GYF-----------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505238906 163 RELFYNYLIETyqenPRTFVISTHLIEEISNLLEKVIILDKGK 205
Cdd:cd03221 106 IEALEEALKEY----PGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-223 |
8.82e-17 |
|
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: 79.95 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKN-----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIH 77
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGK----------DLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 LMSEDDLYPSKLKI--------KSLFHLM-------EG--FYGNFD----WRLANEMLSEFELEPtKRMNK----LSTGY 132
Cdd:COG1123 331 KLSRRSLRELRRRVqmvfqdpySSLNPRMtvgdiiaEPlrLHGLLSraerRERVAELLERVGLPP-DLADRypheLSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 133 R---SIA-------KLIIAlcvpceyiflDEPVLGLDANHRELFYNYLIETYQENPRTFVISTH---LIEEISNlleKVI 199
Cdd:COG1123 410 RqrvAIAralalepKLLIL----------DEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHdlaVVRYIAD---RVA 476
|
250 260
....*....|....*....|....*
gi 505238906 200 ILDKGKIIKDDSVENILEN-THIVT 223
Cdd:COG1123 477 VMYDGRIVEDGPTEEVFANpQHPYT 501
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-209 |
1.22e-16 |
|
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: 75.16 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenekslnnihlmseddl 84
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 ypsklkikslfhlmegFYGNFD-WRLANEMLSEfeleptkrmnkLSTGYR---SIAKliiALCVPCEYIFLDEPVLGLDA 160
Cdd:cd03216 66 ----------------FASPRDaRRAGIAMVYQ-----------LSVGERqmvEIAR---ALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505238906 161 NHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKD 209
Cdd:cd03216 116 AEVERLFK-VIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-217 |
1.29e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLII--ENLYKTY----------------------GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTK 56
Cdd:COG1134 1 MSSMIevENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 57 GKITLDGRLVtenekSL--------------NNIHL------MSEDDlypsklkIKSLFHLMEGFYGnfdwrlanemLSE 116
Cdd:COG1134 81 GRVEVNGRVS-----ALlelgagfhpeltgrENIYLngrllgLSRKE-------IDEKFDEIVEFAE----------LGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 117 FELEPTKRmnkLSTGYRsiAKLI--IALCVPCEYIFLDEpVLGL-DANHRELFYNyLIETYQENPRTFVISTHLIEEISN 193
Cdd:COG1134 139 FIDQPVKT---YSSGMR--ARLAfaVATAVDPDILLVDE-VLAVgDAAFQKKCLA-RIRELRESGRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|....
gi 505238906 194 LLEKVIILDKGKIIKDDSVENILE 217
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-215 |
4.34e-16 |
|
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: 75.68 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYG-KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKS----------- 72
Cdd:cd03256 3 VENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrqigm 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 73 ----LNNIHLMS--EDDLYPsKLKIKSLFHLMEGFYGNFDWRLANEMLSEFELEP--TKRMNKLSTGYR---SIA----- 136
Cdd:cd03256 83 ifqqFNLIERLSvlENVLSG-RLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDkaYQRADQLSGGQQqrvAIAralmq 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 137 --KLIIAlcvpceyiflDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVEN 214
Cdd:cd03256 162 qpKLILA----------DEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
.
gi 505238906 215 I 215
Cdd:cd03256 232 L 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-206 |
4.63e-16 |
|
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: 75.22 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYG----KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIHL 78
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT----------DISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 MSEDDLypSKLKIKSL------FHLMEG------------FYGNFDW---RLANEMLSEFELEptKRMNK----LSTGYR 133
Cdd:cd03255 71 LSEKEL--AAFRRRHIgfvfqsFNLLPDltalenvelpllLAGVPKKerrERAEELLERVGLG--DRLNHypseLSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 134 ---SIAKLIIalCVPcEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHlIEEISNLLEKVIILDKGKI 206
Cdd:cd03255 147 qrvAIARALA--NDP-KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH-DPELAEYADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-207 |
8.44e-16 |
|
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: 74.46 E-value: 8.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKN----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSL-----NN 75
Cdd:cd03257 4 VKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirrKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 IHLMSED---DLYPSkLKIKSlfHLMEGFYGNFD-------WRLANEMLSEFELePTKRMNK----LSTGYR---SIAkl 138
Cdd:cd03257 84 IQMVFQDpmsSLNPR-MTIGE--QIAEPLRIHGKlskkearKEAVLLLLVGVGL-PEEVLNRypheLSGGQRqrvAIA-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 139 iIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:cd03257 158 -RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-218 |
8.66e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.89 E-value: 8.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 11 TYGKKNVLNNISvnFQAEK--IYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLnnihlmseddlypsK 88
Cdd:COG4586 31 EYREVEAVDDIS--FTIEPgeIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEF--------------A 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 89 LKI------KS--LFHL--MEGF------YG----NFDWRLanEMLSE-FELEP--TKRMNKLSTGYRSIAKLIIALCVP 145
Cdd:COG4586 95 RRIgvvfgqRSqlWWDLpaIDSFrllkaiYRipdaEYKKRL--DELVElLDLGEllDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 146 CEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-207 |
3.47e-15 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 72.29 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKN-VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHLM--SE 81
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMqdVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKLKIKSLFHLMEGFYGNFDwrlANEMLSEFELEPTKRMN--KLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLD 159
Cdd:cd03226 82 YQLFTDSVREELLLGLKELDAGNEQ---AETVLKDLDLYALKERHplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505238906 160 ANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:cd03226 159 YKNMERVGE-LIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-67 |
3.79e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.14 E-value: 3.79e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT 67
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT 68
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-221 |
5.05e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.62 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR---LVTENEKSLNNIHL 78
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 MSEDDLYPSKLKI----KSLFHLMEGFYGNFDWRLANEMLSEFELEPTKRM--NKLSTGYRSIAKLIIALCVPCEYIFLD 152
Cdd:PRK10895 83 LPQEASIFRRLSVydnlMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSmgQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 153 EPVLGLDAnHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENTHI 221
Cdd:PRK10895 163 EPFAGVDP-ISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-259 |
7.78e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGK-----KNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNN 75
Cdd:PRK13637 1 MSIKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 IH----LMSEddlYPSklkiKSLFHlmEGFYGNFDWRLANEMLSEFELEP--TKRMN---------------KLSTGYRS 134
Cdd:PRK13637 81 IRkkvgLVFQ---YPE----YQLFE--ETIEKDIAFGPINLGLSEEEIENrvKRAMNivgldyedykdkspfELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 135 IAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDdsven 214
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ----- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 505238906 215 ilenthivtGSIEEVetfTKQLQILEKTTLGGSLTAYVKGELPQK 259
Cdd:PRK13637 227 ---------GTPREV---FKEVETLESIGLAVPQVTYLVRKLRKK 259
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-218 |
8.21e-15 |
|
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: 71.88 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTE---NEKSLNNI----- 76
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKRPVNTVfqnya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 77 ---HLMSEDDL-YPSKLKIKSLFHLMEGfygnfdwrlANEMLSEFELE--PTKRMNKLSTGYRSIAKLIIALCVPCEYIF 150
Cdd:cd03300 83 lfpHLTVFENIaFGLRLKKLPKAEIKER---------VAEALDLVQLEgyANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 151 LDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-218 |
8.54e-15 |
|
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: 72.08 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT---ENE-------KS 72
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglpPHEiarlgigRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 73 LNNIHlmseddLYPS-----KLKIKSLFHLMEGFYGNFDWR-------LANEMLSEFELEPtkRMN----KLSTGYRSIA 136
Cdd:cd03219 81 FQIPR------LFPEltvleNVMVAAQARTGSGLLLARARReereareRAEELLERVGLAD--LADrpagELSYGQQRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 137 KLIIALCVPCEYIFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENIL 216
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAE-LIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
..
gi 505238906 217 EN 218
Cdd:cd03219 232 NN 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
9.56e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.75 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKKN-----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKslnn 75
Cdd:PRK13634 1 MDITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 ihlmsEDDLYPSKLKIKSLFHLMEG--F---------YG--NFD------WRLANEMLSEFELEP---TKRMNKLSTG-Y 132
Cdd:PRK13634 77 -----NKKLKPLRKKVGIVFQFPEHqlFeetvekdicFGpmNFGvseedaKQKAREMIELVGLPEellARSPFELSGGqM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 133 RSIAkliIA--LCVPCEYIFLDEPVLGLDANHR----ELFYnyliETYQENPRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:PRK13634 152 RRVA---IAgvLAMEPEVLVLDEPTAGLDPKGRkemmEMFY----KLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
....*....
gi 505238906 207 IKDDSVENI 215
Cdd:PRK13634 225 FLQGTPREI 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-154 |
1.31e-14 |
|
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: 69.60 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIH---LMSEDDLYPSKLK---I 91
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEigyVFQDPQLFPRLTVrenL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 92 KSLFHLMEGFYGNFDWRLAnEMLSEFELE------PTKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEP 154
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAE-EALEKLGLGdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-210 |
1.71e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 71.02 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT--------ENEKS 72
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSllglgggfNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 73 -LNNIHLMseddlypsklkikslfHLMEGFYGNFDWRLANEMLsEF-ELEP--TKRMNKLSTGYRSIAKLIIALCVPCEY 148
Cdd:cd03220 101 gRENIYLN----------------GRLLGLSRKEIDEKIDEII-EFsELGDfiDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 149 IFLDEpVLGL-DANHRELFYnYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDD 210
Cdd:cd03220 164 LLIDE-VLAVgDAAFQEKCQ-RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-207 |
1.75e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.56 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 7 NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLN-NIHLMSE-DDL 84
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARaRIGVVPQfDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 YPSKLKIKSLfhLMEGFYGNFDWRLANEMLS---EF---ELEPTKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGL 158
Cdd:PRK13536 126 DLEFTVRENL--LVFGRYFGMSTREIEAVIPsllEFarlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505238906 159 DANHRELFYNYLiETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:PRK13536 204 DPHARHLIWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-206 |
3.74e-14 |
|
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: 69.59 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHLMSED 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 -DLYPSklkiKSLFHLMEgfygnFDWRLAN--------------EMLS-EFELEptKRMNKLSTGYRSIAKLIIALCVPC 146
Cdd:cd03301 81 yALYPH----MTVYDNIA-----FGLKLRKvpkdeidervrevaELLQiEHLLD--RKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 147 EYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-207 |
3.74e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQA-EKIyGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRL------------------ 65
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPgDRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigylpqeppldddltvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 66 ---------VTENEKSLNNI-HLMSEDDLYPSKL-KIKSLFHLMEGFygNFDWRlANEMLSEFEL---EPTKRMNKLSTG 131
Cdd:COG0488 80 dtvldgdaeLRALEAELEELeAKLAEPDEDLERLaELQEEFEALGGW--EAEAR-AEEILSGLGFpeeDLDRPVSELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 132 YR---SIAKLIIAlcvPCEYIFLDEPVLGLDANHRELFYNYLietyQENPRTFVISTH---LIEEISNlleKVIILDKGK 205
Cdd:COG0488 157 WRrrvALARALLS---EPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHdryFLDRVAT---RILELDRGK 226
|
..
gi 505238906 206 II 207
Cdd:COG0488 227 LT 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-217 |
5.73e-14 |
|
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: 69.09 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNII--NNRIFDTKGKITLDGRLVTE---NEKSLNNIH 77
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDlppEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 LMSEddlYPSK---LKIKS-LFHLMEGFYGNFDWRlaNEMLSEFELEPtkrmnklstgyrsiaKLIIalcvpceyifLDE 153
Cdd:cd03217 81 LAFQ---YPPEipgVKNADfLRYVNEGFSGGEKKR--NEILQLLLLEP---------------DLAI----------LDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 154 PVLGLDANHRELFYNyLIETYQENPRTFVISTHLiEEISNLLE--KVIILDKGKIIKDDSVENILE 217
Cdd:cd03217 131 PDSGLDIDALRLVAE-VINKLREEGKSVLIITHY-QRLLDYIKpdRVHVLYDGRIVKSGDKELALE 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-210 |
5.90e-14 |
|
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: 69.25 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 32 GLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNnihlmseddLYPSKLKIKSLF-------HL------- 97
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKIN---------LPPQQRKIGLVFqqyalfpHLnvrenla 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 98 --MEGFYGNFDWRLANEMLSEFELEPTKR--MNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIET 173
Cdd:cd03297 98 fgLKRKRNREDRISVDELLDLLGLDHLLNryPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 505238906 174 YQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDD 210
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-209 |
8.86e-14 |
|
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: 68.65 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKN----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSlnnIHL 78
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD---RGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 MSEDD-LYPSK---------LKIKSLfhlmegfyGNFDWR-LANEMLSEFELEPT--KRMNKLSTGYRSIAKLIIALCVP 145
Cdd:cd03293 78 VFQQDaLLPWLtvldnvalgLELQGV--------PKAEAReRAEELLELVGLSGFenAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 146 CEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDK--GKIIKD 209
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-218 |
1.04e-13 |
|
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: 70.70 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTY--GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDT---KGKITLDGRLVTENEKSL--NN 75
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALrgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 IHLMSED---DLYPSKLKIKSLFHLMEGFYGNFDWR-LANEMLSEFELEPTKRMN--KLSTGYRSIAKLIIALCVPCEYI 149
Cdd:COG1123 85 IGMVFQDpmtQLNPVTVGDQIAEALENLGLSRAEARaRVLELLEAVGLERRLDRYphQLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 150 FLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:COG1123 165 IADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
1.08e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT-----ENEKS----- 72
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprDAQAAgiaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 73 ---LN---------NIHLMSEddlyPSKlkikslfhlmegfYGNFDW----RLANEMLSEFELE--PTKRMNKLSTGYR- 133
Cdd:COG1129 85 hqeLNlvpnlsvaeNIFLGRE----PRR-------------GGLIDWramrRRARELLARLGLDidPDTPVGDLSVAQQq 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 134 --SIAKliiALCVPCEYIFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDS 211
Cdd:COG1129 148 lvEIAR---ALSRDARVLILDEPTASLTEREVERLFR-IIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGP 223
|
....
gi 505238906 212 VENI 215
Cdd:COG1129 224 VAEL 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-204 |
1.62e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.57 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT--ENEKSLnnihLMS 80
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAERGV----VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDDLYPSKLKIKSL-FHLMEGFYGNFDWR-LANEMLSEFELE--PTKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVL 156
Cdd:PRK11248 78 NEGLLPWRNVQDNVaFGLQLAGVEKMQRLeIAHQMLKKVGLEgaEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505238906 157 GLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKG 204
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-207 |
1.98e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEK-SLNNIHLMSE-D 82
Cdd:PRK13537 10 FRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARhARQRVGVVPQfD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 DLYPSKLKIKSLfhLMEGFYGNFDWRLANEM---LSEF---ELEPTKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVL 156
Cdd:PRK13537 90 NLDPDFTVRENL--LVFGRYFGLSAAAARALvppLLEFaklENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505238906 157 GLDANHRELFYNYLiETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:PRK13537 168 GLDPQARHLMWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-218 |
2.52e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 68.14 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenekSLN-------- 74
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT----GLPphriarlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 75 ------NIHL---MS--EDdlypskLKIKSLFHLMEGFYGNFDW------------RLANEMLSEFELEPtkRMNK---- 127
Cdd:COG0411 81 iartfqNPRLfpeLTvlEN------VLVAAHARLGRGLLAALLRlprarreerearERAEELLERVGLAD--RADEpagn 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 128 LSTGYR---SIAkliIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKG 204
Cdd:COG0411 153 LSYGQQrrlEIA---RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
250
....*....|....
gi 505238906 205 KIIKDDSVENILEN 218
Cdd:COG0411 230 RVIAEGTPAEVRAD 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-218 |
9.01e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.55 E-value: 9.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHLMSED 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 -DLYPSKLKIKSL-FHLMEGfygnfdwRLA--------NEMLSEFEL-EPTKRM-NKLSTGYRSIAKLIIALCVPCEYIF 150
Cdd:PRK11607 100 yALFPHMTVEQNIaFGLKQD-------KLPkaeiasrvNEMLGLVHMqEFAKRKpHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 151 LDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-206 |
9.24e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenekslnniHLMS 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS---------RLHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDDLYPSKLKIKSLFHLMEGFyGNFDWRL-----------------ANEMLSEFELE--PTKRMNKLSTGYRSIAKLIIA 141
Cdd:PRK10851 72 RDRKVGFVFQHYALFRHMTVF-DNIAFGLtvlprrerpnaaaikakVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505238906 142 LCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-209 |
1.44e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 65.21 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 22 SVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIH-LMSEDDLYPS-------KLKIKS 93
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSmLFQENNLFAHltveqnvGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 94 LFHLMEGFYGNFDWRLANEMLSEFELeptKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIET 173
Cdd:cd03298 98 GLKLTAEDRQAIEVALARVGLAGLEK---RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 505238906 174 YQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKD 209
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-206 |
3.98e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 8 LYKTYGKKNVlNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSL-NNIHLMSEDDLYP 86
Cdd:TIGR01257 937 IFEPSGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVrQSLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 87 SKLKIKSlfHLMegFYGNFDWRLANEMLSEFE--LEPTKRMNK-------LSTGYRSIAKLIIALCVPCEYIFLDEPVLG 157
Cdd:TIGR01257 1016 HHLTVAE--HIL--FYAQLKGRSWEEAQLEMEamLEDTGLHHKrneeaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505238906 158 LDANHRELFYNYLIEtYQENpRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:TIGR01257 1092 VDPYSRRSIWDLLLK-YRSG-RTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-218 |
4.31e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYG-----KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNN 75
Cdd:PRK13641 1 MSIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 IHLMSEDDL---YPSKlkikSLFH---LMEGFYGNFDWRLANEMLSEFELEPTKR-------MNK----LSTGYRSIAKL 138
Cdd:PRK13641 81 KKLRKKVSLvfqFPEA----QLFEntvLKDVEFGPKNFGFSEDEAKEKALKWLKKvglsedlISKspfeLSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 139 IIALCVPCEYIFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-68 |
5.08e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.09 E-value: 5.08e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 2 SLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIIN--NRIfdTKGKITLDGRLVTE 68
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAglEDP--TSGEILIGGRDVTD 69
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-218 |
5.61e-12 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 63.89 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNnisVNFQAEKI--YGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHLMS 80
Cdd:cd03299 1 LKVENLSKDWKEFKLKN---VSLEVERGdyFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDdlypsklkiKSLFHLMEgFYGN--FDWRLANEMLSEFE---LEPTKRMN----------KLSTGYRSIAKLIIALCVP 145
Cdd:cd03299 78 QN---------YALFPHMT-VYKNiaYGLKKRKVDKKEIErkvLEIAEMLGidhllnrkpeTLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 146 CEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-207 |
6.95e-12 |
|
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: 62.95 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 13 GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFD--TKGKITLDGRLVTENEKSLNNIHLMSEDDLYPSklk 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPT--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 91 ikslfhlmegfygnfdwrlanemLSEFE-LEPTKRMNKLSTGYR---SIAkliialcvpCEYI------FLDEPVLGLDA 160
Cdd:cd03213 97 -----------------------LTVREtLMFAAKLRGLSGGERkrvSIA---------LELVsnpsllFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505238906 161 nHRELFYNYLIETYQENPRTFVISTH-LIEEISNLLEKVIILDKGKII 207
Cdd:cd03213 145 -SSALQVMSLLRRLADTGRTIICSIHqPSSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-218 |
7.68e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 63.37 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYG----KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTE-NEKSLNNI--- 76
Cdd:cd03258 4 LKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKArrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 77 --------HLMSEDDL-----YPskLKIkslfhlmEGFYGNFDWRLANEMLSEFELEPTKRM--NKLSTGYR---SIAKl 138
Cdd:cd03258 84 igmifqhfNLLSSRTVfenvaLP--LEI-------AGVPKAEIEERVLELLELVGLEDKADAypAQLSGGQKqrvGIAR- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 139 iiALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:cd03258 154 --ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-225 |
8.41e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.49 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTYGKKN-----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKG-----------KITLDGRL 65
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 66 VTENEKSLNNIHLMS-------------------EDDLY--PSKLKI-KSLFHLMEGFYGNfDWRLANEML--SEFELep 121
Cdd:PRK13631 101 TNPYSKKIKNFKELRrrvsmvfqfpeyqlfkdtiEKDIMfgPVALGVkKSEAKKLAKFYLN-KMGLDDSYLerSPFGL-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 122 tkrmnklSTGYRSIAKLIIALCVPCEYIFLDEPVLGLD-ANHRELFYnyLIETYQENPRTFVISTHLIEEISNLLEKVII 200
Cdd:PRK13631 178 -------SGGQKRRVAIAGILAIQPEILIFDEPTAGLDpKGEHEMMQ--LILDAKANNKTVFVITHTMEHVLEVADEVIV 248
|
250 260
....*....|....*....|....*
gi 505238906 201 LDKGKIIKDDSVENILENTHIVTGS 225
Cdd:PRK13631 249 MDKGKILKTGTPYEIFTDQHIINST 273
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-205 |
8.41e-12 |
|
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: 62.40 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYG--KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTE-NEKSL-NNIHL 78
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 MSEDdlypsklkikslFHLMEGfygnfdwrlanemlsefelepTKRMNKLSTGYR---SIAKliiALCVPCEYIFLDEPV 155
Cdd:cd03228 81 VPQD------------PFLFSG---------------------TIRENILSGGQRqriAIAR---ALLRDPPILILDEAT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505238906 156 LGLDANHRELFYNyLIETYQENpRTFVISTHLIEEISNlLEKVIILDKGK 205
Cdd:cd03228 125 SALDPETEALILE-ALRALAKG-KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-61 |
9.27e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 9.27e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQA-EKIyGLLGNNGAGKSTLLNIINNRIFDTKGKITL 61
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRgDRI-GLIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-218 |
9.61e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.57 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 4 IIE--NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHL--- 78
Cdd:PRK09493 1 MIEfkNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 --MSEDDLYPsklKIKSLFHLMegfYGNFDWR---------LANEMLSEFELEptKRMN----KLSTGYR---SIAKlii 140
Cdd:PRK09493 81 mvFQQFYLFP---HLTALENVM---FGPLRVRgaskeeaekQARELLAKVGLA--ERAHhypsELSGGQQqrvAIAR--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 141 ALCVPCEYIFLDEPVLGLDAnhrELFYNYL--IETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDP---ELRHEVLkvMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-216 |
9.85e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.85 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 6 ENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTE--NEKSLNNIHLMSEDD 83
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 84 LYPSKLKIKSLfhLMEGFYGN----FDWRLANEMLSEFELEPT-------KRMNKLSTGYRSIAKLIIALCVPCEYIFLD 152
Cdd:PRK10253 91 TTPGDITVQEL--VARGRYPHqplfTRWRKEDEEAVTKAMQATgithladQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505238906 153 EPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENIL 216
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-218 |
1.06e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSlnniHLMSED 82
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA----KIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 -DLYPSKLKIKSLFHL-----MEGFYGN---FDWRLAN--EMLSEFELEPTKRMNKLSTGYRSIAKLIIALCVPCEYIFL 151
Cdd:PRK11614 82 vAIVPEGRRVFSRMTVeenlaMGGFFAErdqFQERIKWvyELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505238906 152 DEPVLGLDANHRELFYNYLIETYQENPRTFvisthLIEEISN----LLEKVIILDKGKIIKDDSVENILEN 218
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIF-----LVEQNANqalkLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-207 |
1.22e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 63.06 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 14 KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFD---TKGKITLDGRLVtENEKSLNNIHLMSEDDLYPSKLK 90
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPR-KPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 91 IKSLFHlmegFYGNFdwRLANEMlSEFELEPT----------------KRMNKLSTGYRSIAKLIIALCVPCEYIFLDEP 154
Cdd:cd03234 98 VRETLT----YTAIL--RLPRKS-SDAIRKKRvedvllrdlaltriggNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 155 VLGLDAnhreLFYNYLIET---YQENPRTFVISTHLI-EEISNLLEKVIILDKGKII 207
Cdd:cd03234 171 TSGLDS----FTALNLVSTlsqLARRNRIVILTIHQPrSDLFRLFDRILLLSSGEIV 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-64 |
1.27e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.25 E-value: 1.27e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR 64
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGR 64
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-209 |
1.66e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 62.80 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKN----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEnekSLNNIHL 78
Cdd:COG1116 8 LELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---PGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 M-SEDDLYPSK---------LKIKslfhlmeGFYGNFDWRLANEMLSEFELEptKRMNK----LSTGYR---SIAKliiA 141
Cdd:COG1116 85 VfQEPALLPWLtvldnvalgLELR-------GVPKAERRERARELLELVGLA--GFEDAyphqLSGGMRqrvAIAR---A 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505238906 142 LCVPCEYIFLDEPvLG-LDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDK--GKIIKD 209
Cdd:COG1116 153 LANDPEVLLMDEP-FGaLDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-218 |
2.18e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 63.19 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNriFD--TKGKITLDGRLVTE---NEKslnNI 76
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAG--FEtpDSGRILLDGRDVTGlppEKR---NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 77 HLMSEDDlypsklkikSLF-HL-----------MEGFYGNFDWRLANEMLSEFELEP-TKRM-NKLSTGY-------RSI 135
Cdd:COG3842 80 GMVFQDY---------ALFpHLtvaenvafglrMRGVPKAEIRARVAELLELVGLEGlADRYpHQLSGGQqqrvalaRAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 136 A---KLiialcvpceyIFLDEPvLG-LDANHRELFYNYLIETYQENPRTFVISTHLIEE---ISNlleKVIILDKGKIIK 208
Cdd:COG3842 151 ApepRV----------LLLDEP-LSaLDAKLREEMREELRRLQRELGITFIYVTHDQEEalaLAD---RIAVMNDGRIEQ 216
|
250
....*....|
gi 505238906 209 DDSVENILEN 218
Cdd:COG3842 217 VGTPEEIYER 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-223 |
2.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.72 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKN-----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIH 77
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 LMS----------EDDLYPSKLKIKSLF---HLmeGFYGNFDWRLANEMLSEFEL--EPTKRMN-KLSTGYRSIAKLIIA 141
Cdd:PRK13645 87 RLRkeiglvfqfpEYQLFQETIEKDIAFgpvNL--GENKQEAYKKVPELLKLVQLpeDYVKRSPfELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 142 LCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENTHI 221
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
..
gi 505238906 222 VT 223
Cdd:PRK13645 245 LT 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-241 |
3.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.40 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 4 IIE--NLYKTYGK-KNVLNNIsvNFQAEK--IYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHL 78
Cdd:PRK13639 1 ILEtrDLKYSYPDgTEALKGI--NFKAEKgeMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 M-------SEDDLYPSKLKIKSLFHLME-GFYGNFDWRLANEMLSEFELE--PTKRMNKLSTGYRSIAKLIIALCVPCEY 148
Cdd:PRK13639 79 TvgivfqnPDDQLFAPTVEEDVAFGPLNlGLSKEEVEKRVKEALKAVGMEgfENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 149 IFLDEPVLGLDANHRELFYNYLIETYQENpRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENTHIVTGSIEE 228
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLR 237
|
250
....*....|...
gi 505238906 229 VETFTKQLQILEK 241
Cdd:PRK13639 238 LPRVAHLIEILNK 250
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-217 |
4.72e-11 |
|
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: 62.93 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTYG--KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGRlvtenekSLNNIHL 78
Cdd:COG2274 473 DIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL-LGLYEpTSGRILIDGI-------DLRQIDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 ----------MSEDDLypsklkikslfhlmegFYG----NFdwRLANEMLSEFEL----------EPTKRM--------- 125
Cdd:COG2274 545 aslrrqigvvLQDVFL----------------FSGtireNI--TLGDPDATDEEIieaarlaglhDFIEALpmgydtvvg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 126 ---NKLSTGYRSiaKLIIALCV---PcEYIFLDEPVLGLDANHRELFYNYLIETYQenPRTFVISTH---LIEeisnLLE 196
Cdd:COG2274 607 eggSNLSGGQRQ--RLAIARALlrnP-RILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHrlsTIR----LAD 677
|
250 260
....*....|....*....|.
gi 505238906 197 KVIILDKGKIIKDDSVENILE 217
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLA 698
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-237 |
5.56e-11 |
|
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: 62.51 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInnRIFD----TKGKI----------------TLDGR 64
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL--RGMDqyepTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 65 --LVTENEKSLNNIHLMSEDDLYPSKLKIKSLFHLMEGF--YGNfDWRLAN--EMLSEFELEPTKRMNK----------- 127
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFalYGD-DTVLDNvlEALEEIGYEGKEAVGRavdliemvqls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 128 ---------LSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKV 198
Cdd:TIGR03269 160 hrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 505238906 199 IILDKGKIIK----DDSVENILEnthivtgSIEEVETFTKQLQ 237
Cdd:TIGR03269 240 IWLENGEIKEegtpDEVVAVFME-------GVSEVEKECEVEV 275
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-206 |
1.06e-10 |
|
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: 59.85 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNI-------- 76
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkvgmvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 77 -HLmsedDLYPSKlkiKSLFHLMEGFYGNFDW------RLANEMLSEFELEP--TKRMNKLSTGYR---SIAKliiALCV 144
Cdd:cd03262 83 qQF----NLFPHL---TVLENITLAPIKVKGMskaeaeERALELLEKVGLADkaDAYPAQLSGGQQqrvAIAR---ALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505238906 145 PCEYIFLDEPVLGLDAnhrELFYNYL--IETYQENPRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:cd03262 153 NPKVMLFDEPTSALDP---ELVGEVLdvMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-217 |
1.13e-10 |
|
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: 60.32 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKK--NVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGRLVTENE-KSL-NNIHLM 79
Cdd:cd03251 3 FKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLI-PRFYDvDSGRILIDGHDVRDYTlASLrRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 80 SEDDLypsklkiksLFH--LMEGF-YGNFD---------WRLAN------EMLSEFELEPTKRMNKLSTGYR---SIAKl 138
Cdd:cd03251 82 SQDVF---------LFNdtVAENIaYGRPGatreeveeaARAANahefimELPEGYDTVIGERGVKLSGGQRqriAIAR- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 139 iiALCVPCEYIFLDEPVLGLDaNHRELFYNYLIETYQENPRTFVIStHLIEEISNlLEKVIILDKGKIIKDDSVENILE 217
Cdd:cd03251 152 --ALLKDPPILILDEATSALD-TESERLVQAALERLMKNRTTFVIA-HRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-67 |
1.21e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 1.21e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGK-----KNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT 67
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT 71
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-216 |
1.56e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.77 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVlnNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenekslnnihlmsed 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 DLYPSKLKIKSLF-------HLME------GF-----YGNFDWRLANEMLSEFELEP--TKRMNKLSTGYRSIAKLiiAL 142
Cdd:COG3840 65 ALPPAERPVSMLFqennlfpHLTVaqniglGLrpglkLTAEQRAQVEQALERVGLAGllDRLPGQLSGGQRQRVAL--AR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 143 CV----PCeyIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENIL 216
Cdd:COG3840 143 CLvrkrPI--LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-215 |
1.60e-10 |
|
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: 59.50 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIIN-----NRIFDTKGKITLDGRLVTENEKSLNNIHL- 78
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlndlIPGAPDEGEVLLDGKDIYDLDVDVLELRRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 ------------MS--EDDLYPSKL-KIKSLFHLMEgfygnfdwrLANEMLSEFEL--EPTKRMN--KLSTGYR---SIA 136
Cdd:cd03260 83 vgmvfqkpnpfpGSiyDNVAYGLRLhGIKLKEELDE---------RVEEALRKAALwdEVKDRLHalGLSGGQQqrlCLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 137 KliiALCVPCEYIFLDEPVLGLD-ANHRElfynylIE---TYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSV 212
Cdd:cd03260 154 R---ALANEPEVLLLDEPTSALDpISTAK------IEeliAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
...
gi 505238906 213 ENI 215
Cdd:cd03260 225 EQI 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-64 |
2.55e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.36 E-value: 2.55e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR 64
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR 63
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-213 |
3.05e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.31 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKItLDGRLVTENEKslNNIHLMSED 82
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAR--EDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 -DLYPSKLKIKSLFHLMEGfygnfDWR-LANEMLSEFELEPtkRMNK----LSTGYRSIAKLIIALCVPCEYIFLDEPVL 156
Cdd:PRK11247 90 aRLLPWKKVIDNVGLGLKG-----QWRdAALQALAAVGLAD--RANEwpaaLSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 157 GLDANHReLFYNYLIET-YQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVE 213
Cdd:PRK11247 163 ALDALTR-IEMQDLIESlWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-207 |
5.43e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.87 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGrlvteneKSLNnihlMSED 82
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-------KPLD----YSKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 DLYPSKLKIKSLFHLMEG--FYGNFDWRLANEM--LSEFELEPTKRMNK-----------------LSTGYRSIAKLIIA 141
Cdd:PRK13638 71 GLLALRQQVATVFQDPEQqiFYTDIDSDIAFSLrnLGVPEAEITRRVDEaltlvdaqhfrhqpiqcLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 142 LCVPCEYIFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIA-IIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-210 |
6.62e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 57.75 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKN-VLNNISVNFQA-EKIYgLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIHLMSED 82
Cdd:COG2884 4 FENVSKRYPGGReALSDVSLEIEKgEFVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ----------DLSRLKRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 DLYPSKLKI-------KSLFHL---------ME--GFYGNFDWRLANEMLSEFELEptKRMNK----LSTGYR---SIA- 136
Cdd:COG2884 73 EIPYLRRRIgvvfqdfRLLPDRtvyenvalpLRvtGKSRKEIRRRVREVLDLVGLS--DKAKAlpheLSGGEQqrvAIAr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 137 ------KLIIAlcvpceyiflDEPVLGLD-ANHRELFynYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKD 209
Cdd:COG2884 151 alvnrpELLLA----------DEPTGNLDpETSWEIM--ELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRD 218
|
.
gi 505238906 210 D 210
Cdd:COG2884 219 E 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
8.40e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 8.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIE--NLYKTYGKKN-VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT-ENEKSL-NN 75
Cdd:PRK13647 1 MDNIIEveDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVrSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 IHLM---SEDDLYPSKLKIKSLFhlmegfyGNFDWRLANEMLSEFELEPTK--RMNK--------LSTGYRSIAKLIIAL 142
Cdd:PRK13647 81 VGLVfqdPDDQVFSSTVWDDVAF-------GPVNMGLDKDEVERRVEEALKavRMWDfrdkppyhLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 143 CVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENpRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVEnILENTHIV 222
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQG-KTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDEDIV 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-237 |
8.68e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.21 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKslnnihlmsEDDLYPSKLKIKSLFHL 97
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSK---------QKEIKPVRKKVGVVFQF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 98 MEG-----------FYGNFDWRLANEMLSEFELEPTKRMN-----------KLSTGYRSIAKLIIALCVPCEYIFLDEPV 155
Cdd:PRK13643 93 PESqlfeetvlkdvAFGPQNFGIPKEKAEKIAAEKLEMVGladefwekspfELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 156 LGLDANHReLFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENTHIVTG---SIEEVETF 232
Cdd:PRK13643 173 AGLDPKAR-IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAhelGVPKATHF 251
|
....*
gi 505238906 233 TKQLQ 237
Cdd:PRK13643 252 ADQLQ 256
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-215 |
8.85e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.73 E-value: 8.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 27 AEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNnihlmseddLYPSKLKIKSLFHLMEGF--Y-- 102
Cdd:PRK11144 23 AQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIC---------LPPEKRRIGYVFQDARLFphYkv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 103 -GNFDWRLANEMLSEFE-------LEP-TKRM-NKLSTGYR---SIAKliiALCVPCEYIFLDEPVLGLDA-NHRELFyN 168
Cdd:PRK11144 94 rGNLRYGMAKSMVAQFDkivallgIEPlLDRYpGSLSGGEKqrvAIGR---ALLTAPELLLMDEPLASLDLpRKRELL-P 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505238906 169 YLIETYQE--NPRTFVisTHLIEEISNLLEKVIILDKGKIIKDDSVENI 215
Cdd:PRK11144 170 YLERLAREinIPILYV--SHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-67 |
9.26e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 57.68 E-value: 9.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT 67
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT 68
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-67 |
1.65e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 1.65e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505238906 1 MSLIIE--NLYKTYGkkNVLNNISVNFQAEK--IYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT 67
Cdd:COG3845 2 MPPALElrGITKRFG--GVVANDDVSLTVRPgeIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR 70
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-64 |
1.88e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 56.97 E-value: 1.88e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD------TKGKITLDGR 64
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-NRMNDlipgarVEGEILLDGE 78
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-221 |
2.84e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.71 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGK-----KNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKslnn 75
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 ihlmsEDDLYPSKLKIKSLFHLMEG-----------FYG--NFDWRL------ANEMLSEFELePTKRMNK----LSTG- 131
Cdd:PRK13646 77 -----DKYIRPVRKRIGMVFQFPESqlfedtvereiIFGpkNFKMNLdevknyAHRLLMDLGF-SRDVMSQspfqMSGGq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 132 YRSIAKLIIaLCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDS 211
Cdd:PRK13646 151 MRKIAIVSI-LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
250
....*....|....*.
gi 505238906 212 VENI------LENTHI 221
Cdd:PRK13646 230 PKELfkdkkkLADWHI 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-219 |
4.22e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGrlvtenekslNNIHLMSEDDL 84
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG----------ENIPAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 85 YPSKLKIKSLFHLMEGF-----YGNFDWRL-ANEMLSEFELEPTKRMNKLSTGYRSIAKLI-----------------IA 141
Cdd:PRK11831 80 YTVRKRMSMLFQSGALFtdmnvFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMpselsggmarraalaraIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 142 LcvPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENT 219
Cdd:PRK11831 160 L--EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-216 |
4.70e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR--------LVTEN------- 69
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhkLAAQLgigiiyq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 70 EKSLNNiHLMSEDDLYPSKLKIKSLFHLmegfyGNFDWR----LANEMLSEFEL--EPTKRMNKLSTGYRSIAKLIIALC 143
Cdd:PRK09700 88 ELSVID-ELTVLENLYIGRHLTKKVCGV-----NIIDWRemrvRAAMMLLRVGLkvDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 144 VPCEYIFLDEPVLGLdaNHRELFYNYLI-ETYQENPRTFVISTHLIEEISNLLEKVIILDKG-----KIIKDDSVENIL 216
Cdd:PRK09700 162 LDAKVIIMDEPTSSL--TNKEVDYLFLImNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVSNDDIV 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-73 |
4.96e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 56.24 E-value: 4.96e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505238906 5 IENLYKTYGKKN----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTE-NEKSL 73
Cdd:COG1135 4 LENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSEREL 77
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-207 |
6.92e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.21 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 13 GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRI---FDTKGKITLDGRLVTENEkslnnIHLMS----EDDLY 85
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPIDAKE-----MRAISayvqQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 86 psklkIKSLF---HLMegFYGNFdwRLANEMLSEfeleptKRMNKLS-----TGYRSIAKLIIA---------------L 142
Cdd:TIGR00955 111 -----IPTLTvreHLM--FQAHL--RMPRRVTKK------EKRERVDevlqaLGLRKCANTRIGvpgrvkglsggerkrL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 143 CVPCEYI------FLDEPVLGLDAnhrelFYNY-LIETYQE---NPRTFVISTHL-IEEISNLLEKVIILDKGKII 207
Cdd:TIGR00955 176 AFASELLtdppllFCDEPTSGLDS-----FMAYsVVQVLKGlaqKGKTIICTIHQpSSELFELFDKIILMAEGRVA 246
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-67 |
7.27e-09 |
|
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: 54.75 E-value: 7.27e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT 67
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT 65
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-207 |
7.78e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.24 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSL----NNIHLMSED---DLYPSKLK 90
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLmklrESVGMVFQDpdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 91 IKSLFHLM------EGFYGNFDWRLANEMLSEFELEPTkrmNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRE 164
Cdd:PRK13636 102 QDVSFGAVnlklpeDEVRKRVDNALKRTGIEHLKDKPT---HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505238906 165 LFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-242 |
9.63e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.19 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 14 KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIF---DTKGKITLDGrlVTENEKSLNNIH------------- 77
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLpddNPNSKITVDG--ITLTAKTVWDIRekvgivfqnpdnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 ---LMSEDDLY-------PSKLKIKSLFHLMEGFYGnfdwrlaneMLSEFELEPTKrmnkLSTGYRSIAKLIIALCVPCE 147
Cdd:PRK13640 97 fvgATVGDDVAfglenraVPRPEMIKIVRDVLADVG---------MLDYIDSEPAN----LSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 148 YIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEiSNLLEKVIILDKGKIIKDDSVENILENTHIVTGSIE 227
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGL 242
|
250
....*....|....*
gi 505238906 228 EVETFTKQLQILEKT 242
Cdd:PRK13640 243 DIPFVYKLKNKLKEK 257
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-207 |
1.02e-08 |
|
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: 53.86 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKN--VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNniHLMS 80
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS--SLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDDLYPsklkikslfHLmegfygnFDWRLANEMLSEFeleptkrmnklSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDA 160
Cdd:cd03247 79 VLNQRP---------YL-------FDTTLRNNLGRRF-----------SGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505238906 161 NHRELFYNYLIETYQEnpRTFVISTHLIEEISNlLEKVIILDKGKII 207
Cdd:cd03247 132 ITERQLLSLIFEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKII 175
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-65 |
1.02e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 1.02e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 1 MSLII--ENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRL 65
Cdd:PRK09544 1 MTSLVslENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL 67
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-204 |
1.11e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKN--VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENeksLNNIH--- 77
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---ISDVHqnm 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 -----LMSEDDLYPSKLKIkSLFHLMEGFYGNFDWRLANEMLSEFELE--PTKRMNKLSTGYRSIAKLIIAL--CVPceY 148
Cdd:TIGR01257 2015 gycpqFDAIDDLLTGREHL-YLYARLRGVPAEEIEKVANWSIQSLGLSlyADRLAGTYSGGNKRKLSTAIALigCPP--L 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 149 IFLDEPVLGLDANHRELFYNYLIETYQENpRTFVISTHLIEEISNLLEKVIILDKG 204
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREG-RAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-186 |
1.39e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 53.72 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlVTENEKSLNNIHLMS 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-DIDDPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDDlypsklKIKSLFHLME------GFYGNFDWRLAnEMLSEFELEP--TKRMNKLSTGYR---SIAKLIIA-----Lcv 144
Cdd:PRK13539 80 HRN------AMKPALTVAEnlefwaAFLGGEELDIA-AALEAVGLAPlaHLPFGYLSAGQKrrvALARLLVSnrpiwI-- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505238906 145 pceyifLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTH 186
Cdd:PRK13539 151 ------LDEPTAALDAAAVALFAE-LIRAHLAQGGIVIAATH 185
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-207 |
1.48e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.22 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTY--GKKNVLNNISVNFQA-EKIyGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGRLVTE-NEKSLNN- 75
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAgEKV-ALLGRTGCGKSTLLQLL-TRAWDpQQGEILLNGQPIADySEAALRQa 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 -------IHLMS---EDDLYPSKLKIKslfhlmegfygnfDWRLAnEMLSEFEL----EPTKRMN--------KLSTGYR 133
Cdd:PRK11160 416 isvvsqrVHLFSatlRDNLLLAAPNAS-------------DEALI-EVLQQVGLekllEDDKGLNawlgeggrQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 134 ---SIAKliiALCVPCEYIFLDEPVLGLDA-NHRELFynYLIETYQENpRTFVISTHLIEEISNlLEKVIILDKGKII 207
Cdd:PRK11160 482 rrlGIAR---ALLHDAPLLLLDEPTEGLDAeTERQIL--ELLAEHAQN-KTVLMITHRLTGLEQ-FDRICVMDNGQII 552
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-241 |
1.62e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.37 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYG-----KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSlnn 75
Cdd:PRK13649 1 MGINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 ihlmseDDLYPSKLKIKSLFHLMEG-----------FYG--NFDW------RLANEML-----SE--FELEPTKrmnkLS 129
Cdd:PRK13649 78 ------KDIKQIRKKVGLVFQFPESqlfeetvlkdvAFGpqNFGVsqeeaeALAREKLalvgiSEslFEKNPFE----LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 130 TG-YRSIAkliIA--LCVPCEYIFLDEPVLGLD-ANHRELFYnyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGK 205
Cdd:PRK13649 148 GGqMRRVA---IAgiLAMEPKILVLDEPTAGLDpKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 505238906 206 IIKDDSVENILENTHIVTGSIEEVETFTKQLQILEK 241
Cdd:PRK13649 223 LVLSGKPKDIFQDVDFLEEKQLGVPKITKFAQRLAD 258
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-206 |
1.64e-08 |
|
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: 54.01 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 9 YKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT--ENEKSLNNIHLMSEDDLYP 86
Cdd:cd03248 21 YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyEHKYLHSKVSLVGQEPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 87 SK---------LKIKSLFHLMEGFYGNFDWRLANEMLSEFELEPTKRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLG 157
Cdd:cd03248 101 ARslqdniaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505238906 158 LDANHRELFYNYLIEtYQENPRTFVISTHLieeisNLLEK---VIILDKGKI 206
Cdd:cd03248 181 LDAESEQQVQQALYD-WPERRTVLVIAHRL-----STVERadqILVLDGGRI 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-218 |
1.65e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 54.32 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 15 KNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGrLVTENEKSLNNIH----------------- 77
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-LDTSDEENLWDIRnkagmvfqnpdnqivat 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 LMSEDDLY-PSKLKIKSlfhlmEGFYGNFDWRLANEMLSEFELEPTkrmNKLSTGYR---SIAKlIIALCVPCeyIFLDE 153
Cdd:PRK13633 102 IVEEDVAFgPENLGIPP-----EEIRERVDESLKKVGMYEYRRHAP---HLLSGGQKqrvAIAG-ILAMRPEC--IIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505238906 154 PVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNlLEKVIILDKGKIIKDDSVENILEN 218
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
1.82e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.42 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLI-IENLYKTY-GKKNVLNNIsvNFQAEKI--YGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT-----ENEK 71
Cdd:PRK13652 1 MHLIeTRDLCYSYsGSKEALNNI--NFIAPRNsrIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkenirEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 72 SLNNIHLMSEDDLYPSKLKIKSLFhlmegfyGNFDWRLANE-----------MLSEFELEpTKRMNKLSTGYRSIAKLII 140
Cdd:PRK13652 79 FVGLVFQNPDDQIFSPTVEQDIAF-------GPINLGLDEEtvahrvssalhMLGLEELR-DRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 141 ALCVPCEYIFLDEPVLGLDANHRE---LFYNYLIETYQenpRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILE 217
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKeliDFLNDLPETYG---MTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
250 260
....*....|....*....|...
gi 505238906 218 NTHIVTGSIEEVETFTKQLQILE 240
Cdd:PRK13652 228 QPDLLARVHLDLPSLPKLIRSLQ 250
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-67 |
2.28e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 54.42 E-value: 2.28e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 5 IENLYKTY--GKKNV--LNNISVNFQAEKIYGLLGNNGAGKSTLLNIIN--NRifDTKGKITLDGRLVT 67
Cdd:PRK11153 4 LKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINllER--PTSGRVLVDGQDLT 70
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-207 |
2.30e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLI-IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT------------ 67
Cdd:PRK11147 1 MSLIsIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVarlqqdpprnve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 68 ------------ENEKSLNNIHLMS---EDDlyPSKLKIKSLFHLMEGFYGNFDWRL---ANEMLSEFELEPTKRMNKLS 129
Cdd:PRK11147 81 gtvydfvaegieEQAEYLKRYHDIShlvETD--PSEKNLNELAKLQEQLDHHNLWQLenrINEVLAQLGLDPDAALSSLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 130 TGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIeTYQEnprTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK-TFQG---SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-215 |
2.71e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 7 NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLV--TENEKSLN--------NI 76
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALAagvaiiyqEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 77 HLMSE----DDLYpsklkiksLFHLMEGFyGNFDWRLAN----EMLSEF--ELEPTKRMNKLSTGYRS---IAKliiALC 143
Cdd:PRK11288 89 HLVPEmtvaENLY--------LGQLPHKG-GIVNRRLLNyearEQLEHLgvDIDPDTPLKYLSIGQRQmveIAK---ALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 144 VPCEYIFLDEPVLGLdaNHRE---LFynYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKD-DSVENI 215
Cdd:PRK11288 157 RNARVIAFDEPTSSL--SAREieqLF--RVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQV 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-208 |
3.15e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.22 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLI-IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIIN-------NRIfdTKGKITLDGRLVTENEKS 72
Cdd:PRK11264 1 MSAIeVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeaGTI--RVGDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 73 LnnIHLMSED--------DLYPSKLKIKSLFH---LMEGFYGNFDWRLANEMLSEFELE--PTKRMNKLSTGYRSIAKLI 139
Cdd:PRK11264 79 L--IRQLRQHvgfvfqnfNLFPHRTVLENIIEgpvIVKGEPKEEATARARELLAKVGLAgkETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505238906 140 IALCVPCEYIFLDEPVLGLDAnhrELFYNYL--IETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIK 208
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDP---ELVGEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-218 |
3.18e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.38 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRI-----FDTKGKITLDGRLVTENEKSL---- 73
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIElrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 74 --------NNIHLMSEDDLYPSKLKIKSLFHLMEGFYGNFDWRLANEMLSEfelEPTKRMN----KLSTGYRSIAKLIIA 141
Cdd:PRK14247 84 vqmvfqipNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWD---EVKDRLDapagKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 142 LCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQEnpRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-218 |
3.56e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.05 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIHLMSED 82
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQ----------TINLVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 D---LYPSKLKIKSLFHLMEGFYGNFD-WR----LANEM--------LSEFELE--PTKRMNK--------------LST 130
Cdd:PRK10619 76 DgqlKVADKNQLRLLRTRLTMVFQHFNlWShmtvLENVMeapiqvlgLSKQEARerAVKYLAKvgideraqgkypvhLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 131 GYRSIAKLIIALCVPCEYIFLDEPVLGLDAnhrELFYNYL--IETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIK 208
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLriMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250
....*....|
gi 505238906 209 DDSVENILEN 218
Cdd:PRK10619 233 EGAPEQLFGN 242
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-209 |
4.15e-08 |
|
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: 52.59 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 14 KKNVLNNISVNFQA-EKIyGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSL--NNIHLMSEDdlypsklk 90
Cdd:cd03245 16 EIPALDNVSLTIRAgEKV-AIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrRNIGYVPQD-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 91 ikslFHLmegFYGNF------------DWRL--ANEM--LSEF--------ELEPTKRMNKLSTGYR---SIAKLIIAlc 143
Cdd:cd03245 87 ----VTL---FYGTLrdnitlgapladDERIlrAAELagVTDFvnkhpnglDLQIGERGRGLSGGQRqavALARALLN-- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 144 VPcEYIFLDEPVLGLDANHRElfynYLIETYQE--NPRTFVISTHLIeEISNLLEKVIILDKGKIIKD 209
Cdd:cd03245 158 DP-PILLLDEPTSAMDMNSEE----RLKERLRQllGDKTLIIITHRP-SLLDLVDRIIVMDSGRIVAD 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-68 |
4.18e-08 |
|
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: 53.99 E-value: 4.18e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 2 SLIIENLYKTY-GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTE 68
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD 403
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-217 |
4.75e-08 |
|
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: 53.65 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTY-----GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKI-----------TLDGRLVTE 68
Cdd:TIGR03269 282 VRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPDGRG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 69 NEKSLNNIhLMSEDDLYPSKLKIKSL-----------FHLMEGFY----GNFDWRLANEMLSefeleptKRMNKLSTGYR 133
Cdd:TIGR03269 362 RAKRYIGI-LHQEYDLYPHRTVLDNLteaiglelpdeLARMKAVItlkmVGFDEEKAEEILD-------KYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 134 SIAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVE 213
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
....
gi 505238906 214 NILE 217
Cdd:TIGR03269 514 EIVE 517
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-66 |
6.16e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.47 E-value: 6.16e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFDTKGKITLDGRLV 66
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIV 68
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-64 |
7.85e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 53.24 E-value: 7.85e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 505238906 13 GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGR 64
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLL-LRFYDpTSGRILIDGV 402
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-160 |
8.31e-08 |
|
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: 51.48 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 13 GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNR--IFDTKGKITLDGRLVTEN-EKSlnnIHLMSEDDLYPSKL 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRktAGVITGEILINGRPLDKNfQRS---TGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 90 KIKS--LFHlmegfygnfdwrlANemLSEFELEPTKRmnkLSTGYRSIAKLIIalcvpceyIFLDEPVLGLDA 160
Cdd:cd03232 95 TVREalRFS-------------AL--LRGLSVEQRKR---LTIGVELAAKPSI--------LFLDEPTSGLDS 141
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-206 |
8.38e-08 |
|
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: 51.06 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYG--KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIH--- 77
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 LMSEDDLYPSklkikslfhlmegfygnfdwrlanemlsefelepTKRMNKLSTGYRSIAKLIIALcvpceY-----IFLD 152
Cdd:cd03246 81 LPQDDELFSG----------------------------------SIAENILSGGQRQRLGLARAL-----YgnpriLVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505238906 153 EPVLGLDaNHRELFYNYLIETYQENPRTFVISTHLIEEIsNLLEKVIILDKGKI 206
Cdd:cd03246 122 EPNSHLD-VEGERALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-221 |
8.91e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNrIF---DTKGKITLDGR-LVTEN-----EKSL 73
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYphgTWDGEIYWSGSpLKASNirdteRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 74 NNIHlmSEDDLYPSKLKIKSLFHLME----GFYGNFD--WRLANEMLSEFELEP---TKRMNKLSTGYRSIAKLIIALCV 144
Cdd:TIGR02633 81 VIIH--QELTLVPELSVAENIFLGNEitlpGGRMAYNamYLRAKNLLRELQLDAdnvTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 145 PCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVIStHLIEEISNLLEKVIILDKGKIIKDDSVENILENTHI 221
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYIS-HKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-222 |
1.04e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.92 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYG--KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT-ENEKSLNN------ 75
Cdd:PRK13632 10 VENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEIRKkigiif 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 -------IHLMSEDDL--------YPSKlKIKSLFHlmegfygnfDWRLANEMLSEFELEPtkrmNKLSTGYRSIAKLII 140
Cdd:PRK13632 90 qnpdnqfIGATVEDDIafglenkkVPPK-KMKDIID---------DLAKKVGMEDYLDKEP----QNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 141 ALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNlLEKVIILDKGKIIKDDSVENILENTH 220
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKE 234
|
..
gi 505238906 221 IV 222
Cdd:PRK13632 235 IL 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-233 |
1.22e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 11 TYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFDTKGKITLDGrlvteneKSLNNIHLMSEDDLY---PS 87
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL-LRLLSTEGEIQIDG-------VSWNSVTLQTWRKAFgviPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 88 KlkiksLFHLMEGFYGNFD----------WRLANE--MLSEFELEPTKrMN--------KLSTGYRSIAKLIIALCVPCE 147
Cdd:TIGR01271 1300 K-----VFIFSGTFRKNLDpyeqwsdeeiWKVAEEvgLKSVIEQFPDK-LDfvlvdggyVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 148 YIFLDEPVLGLDANHRELFYNYLIETYQENprTFVISTHLIEEisnLLE--KVIILDKGKIIKDDSVENIL-ENTHI--V 222
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQSFSNC--TVILSEHRVEA---LLEcqQFLVIEGSSVKQYDSIQKLLnETSLFkqA 1448
|
250
....*....|.
gi 505238906 223 TGSIEEVETFT 233
Cdd:TIGR01271 1449 MSAADRLKLFP 1459
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-67 |
1.40e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.40e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505238906 7 NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVT 67
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA 76
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-211 |
1.94e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKG----------KITLDGRLVTENEKSLN 74
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRLARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 75 NIHLMSEDDLYPSKLKIksLFHLMEGFYGNFD-WRLANEMLSEFELEPT--------------KRMNKLSTGYRSIAKLI 139
Cdd:PRK09984 87 NTGYIFQQFNLVNRLSV--LENVLIGALGSTPfWRTCFSWFTREQKQRAlqaltrvgmvhfahQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 140 IALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDS 211
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-163 |
2.29e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenekSLNNIHLMSE 81
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE----SWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKL------KIKSL-------FHLMEGFYGNFDWRLANEMLSEFELEP--TKRMNKLSTGYRSIAKLIIALCVPC 146
Cdd:PRK10575 87 VAYLPQQLpaaegmTVRELvaigrypWHGALGRFGAADREKVEEAISLVGLKPlaHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170
....*....|....*..
gi 505238906 147 EYIFLDEPVLGLDANHR 163
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQ 183
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-206 |
3.17e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 51.00 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVteneKSLNNIHLMS 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV----EALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDDLYPSKLKIkslfhlmeGFygNFDWRLANEM-----LSEFE-LEPTKR------MNK-------------LSTGYRSI 135
Cdd:PRK09536 78 RVASVPQDTSL--------SF--EFDVRQVVEMgrtphRSRFDtWTETDRaaveraMERtgvaqfadrpvtsLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 136 AKLIIALCVPCEYIFLDEPVLGLDANH--RELfynYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHqvRTL---ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-207 |
3.47e-07 |
|
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: 49.92 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKN-VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGRLVTE-NEKSL-------- 73
Cdd:cd03254 5 FENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-MRFYDpQKGQILIDGIDIRDiSRKSLrsmigvvl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 74 -----------NNI---HLMSEDDLYPSKLKIKSLFHLMEgfygnfdwRLANemlsEFELEPTKRMNKLSTGYRSIAKLI 139
Cdd:cd03254 84 qdtflfsgtimENIrlgRPNATDEEVIEAAKEAGAHDFIM--------KLPN----GYDTVLGENGGNLSQGERQLLAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 140 IALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQEnpRTFVISTHLIEEISNlLEKVIILDKGKII 207
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-201 |
4.90e-07 |
|
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: 50.75 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTY-GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEnekslnnihlMS 80
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD----------AD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDDLYPSKLKIKSLFHLMEGFYGNfDWRLA------------------NEMLSE----FELEPTKRMNKLSTGYRSIAKL 138
Cdd:TIGR02857 391 ADSWRDQIAWVPQHPFLFAGTIAE-NIRLArpdasdaeirealeraglDEFVAAlpqgLDTPIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 139 IIALCVPCEYIFLDEPVLGLDANHRELFYnYLIETYQENpRTFVISTHLIeEISNLLEKVIIL 201
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVL-EALRALAQG-RTVLLVTHRL-ALAALADRIVVL 529
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
5-205 |
6.02e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.26 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDT--KGKITLDGRLVTenEKSLNNIHLMSED 82
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT--KQILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 D-LYP-----SKLKIKSLFHLMEGFYGNFDWRLANEMLSEFELepTKRMNK---------LSTGYRSIAKLIIALCVPCE 147
Cdd:PLN03211 149 DiLYPhltvrETLVFCSLLRLPKSLTKQEKILVAESVISELGL--TKCENTiignsfirgISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 148 YIFLDEPVLGLDANHRELFYNYLIETYQENpRTFVISTHL-IEEISNLLEKVIILDKGK 205
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKG-KTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-210 |
1.18e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 35 GNNGAGKSTLLNIINNRIF-----DTKGKITLDgRLVTENEKSLNnIHLMSEDDlYPSKLKIKSLFHLMEGFY----GNF 105
Cdd:cd03240 29 GQNGAGKTTIIEALKYALTgelppNSKGGAHDP-KLIREGEVRAQ-VKLAFENA-NGKKYTITRSLAILENVIfchqGES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 106 DWRLanemlsefeLEPTKRmnkLSTGYRSIAKLIIAL------CVPCEYIFLDEPVLGLDANHRELFYNYLIETY--QEN 177
Cdd:cd03240 106 NWPL---------LDMRGR---CSGGEKVLASLIIRLalaetfGSNCGILALDEPTTNLDEENIEESLAEIIEERksQKN 173
|
170 180 190
....*....|....*....|....*....|...
gi 505238906 178 PRTFVISTHliEEISNLLEKVIildkgKIIKDD 210
Cdd:cd03240 174 FQLIVITHD--EELVDAADHIY-----RVEKDG 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.26e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 1 MSLIIENLYKTYGKK-----NVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNN 75
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 IHLMSEDDLYPSKLK----IKSL------------FHLME--------------GFYGNFDWRLANEMLSEFELePTKRM 125
Cdd:PRK13651 81 EKVLEKLVIQKTRFKkikkIKEIrrrvgvvfqfaeYQLFEqtiekdiifgpvsmGVSKEEAKKRAAKYIELVGL-DESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 126 NK----LSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENpRTFVISTHLIEEISNLLEKVIIL 201
Cdd:PRK13651 160 QRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQG-KTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*...
gi 505238906 202 DKGKIIKDDSVENILENT 219
Cdd:PRK13651 239 KDGKIIKDGDTYDILSDN 256
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-217 |
1.79e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.86 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNV--LNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGRLVTENE-KSL-NNIH 77
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLL-TRFYDiDEGEILLDGHDLRDYTlASLrNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 LMSEDdlypsklkikslFHLMEGFYGNFDWRLANEMLSEFELEPTKRM-------NK---------------LSTGYR-- 133
Cdd:PRK11176 421 LVSQN------------VHLFNDTIANNIAYARTEQYSREQIEEAARMayamdfiNKmdngldtvigengvlLSGGQRqr 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 134 -SIAKliiALCVPCEYIFLDEPVLGLDANHRELFYNYLiETYQENpRTFVISTHLIEEISNLLEkVIILDKGKIIKDDSV 212
Cdd:PRK11176 489 iAIAR---ALLRDSPILILDEATSALDTESERAIQAAL-DELQKN-RTSLVIAHRLSTIEKADE-ILVVEDGEIVERGTH 562
|
....*
gi 505238906 213 ENILE 217
Cdd:PRK11176 563 AELLA 567
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-221 |
1.88e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEN------EKSLNNIHlmSEDDLYPsKLKI 91
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkssqEAGIGIIH--QELNLIP-QLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 92 KSLFHLMEGF---YGNFDWRL----ANEMLSEFELE--PTKRMNKLSTGYRS---IAKliiALCVPCEYIFLDEPVLGL- 158
Cdd:PRK10762 97 AENIFLGREFvnrFGRIDWKKmyaeADKLLARLNLRfsSDKLVGELSIGEQQmveIAK---VLSFESKVIIMDEPTDALt 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 159 DANHRELFynYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENTHI 221
Cdd:PRK10762 174 DTETESLF--RVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLI 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-48 |
1.96e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.96e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 505238906 10 KTYG-KKNVLNNISVNF-QAEKIyGLLGNNGAGKSTLLNII 48
Cdd:PRK11819 14 KVVPpKKQILKDISLSFfPGAKI-GVLGLNGAGKSTLLRIM 53
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-211 |
2.64e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.18 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHLMSED 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 83 dlYpsklkikSLFHLMEgFYGNFDWRLanEMLSEFELEPTKRM-----------------NKLSTGYRSIAKLIIALCVP 145
Cdd:PRK11432 87 --Y-------ALFPHMS-LGENVGYGL--KMLGVPKEERKQRVkealelvdlagfedryvDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 146 CEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDS 211
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGS 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-230 |
2.82e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTY--GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFDTKGKITLDGrlvteneKSLNNIHLMS 80
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAF-LRLLNTEGDIQIDG-------VSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDDLY---PSKLKIKS-LFHLMEGFYGNFD----WRLANE--MLSEFELEPTKRMNK-------LSTGYRSIAKLIIALC 143
Cdd:cd03289 75 WRKAFgviPQKVFIFSgTFRKNLDPYGKWSdeeiWKVAEEvgLKSVIEQFPGQLDFVlvdggcvLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 144 VPCEYIFLDEPVLGLDANHRELFYNYLIETYQENprTFVISTHLIEEISNlLEKVIILDKGKIIKDDSVENILENTHIVT 223
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFADC--TVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKSHFK 231
|
....*..
gi 505238906 224 GSIEEVE 230
Cdd:cd03289 232 QAISPSD 238
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-206 |
2.85e-06 |
|
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: 47.02 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 6 ENLYKTYGKKNV-LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSL-----NNIHLM 79
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 80 SEDDLYPSKLKI--KSLFHLMEGFYGNFDWR-LANEMLSEFELEPTKRM--NKLSTG-------YRSIA---KLIIAlcv 144
Cdd:cd03292 84 FQDFRLLPDRNVyeNVAFALEVTGVPPREIRkRVPAALELVGLSHKHRAlpAELSGGeqqrvaiARAIVnspTILIA--- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 145 pceyiflDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKI 206
Cdd:cd03292 161 -------DEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-186 |
4.87e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.73 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKN----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekSLNNIHL 78
Cdd:PRK11629 6 LQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-------PMSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 MSEDDLYPSKLK-IKSLFHLMEGFYG--NFDWRL-------------ANEMLSEFELE--PTKRMNKLSTGYRSIAKLII 140
Cdd:PRK11629 79 AAKAELRNQKLGfIYQFHHLLPDFTAleNVAMPLligkkkpaeinsrALEMLAAVGLEhrANHRPSELSGGERQRVAIAR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505238906 141 ALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTH 186
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
110-215 |
9.22e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 110 ANEMLSEFELEPT--KRMNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYlIETYQENPRTFVISTHL 187
Cdd:NF000106 125 ADELLERFSLTEAagRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE-VRSMVRDGATVLLTTQY 203
|
90 100
....*....|....*....|....*...
gi 505238906 188 IEEISNLLEKVIILDKGKIIKDDSVENI 215
Cdd:NF000106 204 MEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-218 |
9.29e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 7 NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTL---LNIINNRI--FDTKGKITLDGRLVTENEKSLNNIHLMSE 81
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFlrtLNRMNDKVsgYRYSGDVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKLKIKSLFHLMEGFYGN-----FDWR-LANEMLSEFEL--EPTKRMN----KLSTGYRSIAKLIIALCVPCEYI 149
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAGVRAHklvprKEFRgVAQARLTEVGLwdAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 150 FLDEPVLGLDANHRELFYNYLIETyqENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-207 |
9.65e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 45.33 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 4 IIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRI---FDTKGKITLDGRLVTEN-EKSLNNIHLM 79
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHYNGIPYKEFaEKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 80 SEDDLYPSKLKIKslfHLMEgfygnFDWRL-ANEMLSefeleptkrmnKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGL 158
Cdd:cd03233 89 SEEDVHFPTLTVR---ETLD-----FALRCkGNEFVR-----------GISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505238906 159 DANHRELFYNYL-IETYQENPRTFVISTHLIEEISNLLEKVIILDKGKII 207
Cdd:cd03233 150 DSSTALEILKCIrTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-217 |
1.13e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.09 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 4 IIE--NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenekslnniHLMSE 81
Cdd:PRK09452 14 LVElrGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT---------HVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDLYPSKLKIKSLFHLMEGFyGNFDWRLANEMLSEFELEP----TKRMNKLS-TGYRSIAKL--------IIALCV---P 145
Cdd:PRK09452 85 NRHVNTVFQSYALFPHMTVF-ENVAFGLRMQKTPAAEITPrvmeALRMVQLEeFAQRKPHQLsggqqqrvAIARAVvnkP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 146 cEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILE 217
Cdd:PRK09452 164 -KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-48 |
1.17e-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: 46.47 E-value: 1.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 505238906 7 NLYKTY-GKKNVLNNISVNF-QAEKIyGLLGNNGAGKSTLLNII 48
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFfPGAKI-GVLGLNGAGKSTLLRIM 51
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-61 |
1.29e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITL 61
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
33-186 |
1.29e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.12 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 33 LLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSlNNIHLMSeddlypsklKIKSLFHLM------EGFYGN-- 104
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-DYRKLFS---------AVFTDFHLFdqllgpEGKPANpa 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 105 --FDW--RLanEMLSEFELEPTKRMN-KLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPR 179
Cdd:PRK10522 424 lvEKWleRL--KMAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGK 501
|
....*..
gi 505238906 180 TFVISTH 186
Cdd:PRK10522 502 TIFAISH 508
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-217 |
1.35e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 8 LYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKST----LLNIINNRifdtkGKITLDGRlvtenekslnNIHLMSEDD 83
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQ----------PLHNLNRRQ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 84 LYPSKLKIKSLFH---------------LMEGFYGNFDWRLANE-------MLSEFELEPTKRM---NKLSTGYR---SI 135
Cdd:PRK15134 357 LLPVRHRIQVVFQdpnsslnprlnvlqiIEEGLRVHQPTLSAAQreqqviaVMEEVGLDPETRHrypAEFSGGQRqriAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 136 AKliiALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENI 215
Cdd:PRK15134 437 AR---ALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
..
gi 505238906 216 LE 217
Cdd:PRK15134 514 FA 515
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-217 |
1.52e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 45.39 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTY--GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTenEKSLNNIHLM--- 79
Cdd:PRK13635 8 VEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--EETVWDVRRQvgm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 80 -------------SEDDL--------YPSKLKIKSLfhlmegfygnfDWRLANEMLSEF-ELEPtkrmNKLSTGYR---S 134
Cdd:PRK13635 86 vfqnpdnqfvgatVQDDVafglenigVPREEMVERV-----------DQALRQVGMEDFlNREP----HRLSGGQKqrvA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 135 IAKlIIALcVPcEYIFLDEPVLGLDANHRElfynYLIETYQ---ENPRTFVIS-THLIEEISNlLEKVIILDKGKIIKDD 210
Cdd:PRK13635 151 IAG-VLAL-QP-DIIILDEATSMLDPRGRR----EVLETVRqlkEQKGITVLSiTHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
....*..
gi 505238906 211 SVENILE 217
Cdd:PRK13635 223 TPEEIFK 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-63 |
1.62e-05 |
|
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: 44.79 E-value: 1.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 5 IENLYKTY--GKKNVLNNISVNFQA-EKIyGLLGNNGAGKSTLLNIINNRIFDTKGKITLDG 63
Cdd:cd03244 5 FKNVSLRYrpNLPPVLKNISFSIKPgEKV-GIVGRTGSGKSSLLLALFRLVELSSGSILIDG 65
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-207 |
1.62e-05 |
|
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: 44.91 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYG-KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGRLVTE-NEKSL-NNIHL 78
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL-FRFYDvSSGSILIDGQDIREvTLDSLrRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 MSEDDLypsklkiksLFHLMEGF---YGNFDwrlANE------------------MLSEFELEPTKRMNKLSTGYR---S 134
Cdd:cd03253 80 VPQDTV---------LFNDTIGYnirYGRPD---ATDeevieaakaaqihdkimrFPDGYDTIVGERGLKLSGGEKqrvA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 135 IAKLIiaLCVPcEYIFLDEPVLGLDANHRELFYNYLIETYQEnpRTFVISTHLIEEISNlLEKVIILDKGKII 207
Cdd:cd03253 148 IARAI--LKNP-PILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-61 |
1.67e-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: 46.08 E-value: 1.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITL 61
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-66 |
1.80e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.04 E-value: 1.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLV 66
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL 74
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-64 |
1.95e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.86 E-value: 1.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505238906 5 IENLYKTYGK-KNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR 64
Cdd:PRK10790 343 IDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR 403
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-201 |
2.08e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.70 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 9 YKTYGKKnVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEnekslnnihlmseddLYPSK 88
Cdd:PRK10247 15 YLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST---------------LKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 89 LKIK--------SLFHlmEGFYGN--FDWRLANEM---------LSEFELEPT---KRMNKLSTGYRSIAKLIIALCVPC 146
Cdd:PRK10247 79 YRQQvsycaqtpTLFG--DTVYDNliFPWQIRNQQpdpaiflddLERFALPDTiltKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 147 EYIFLDEPVLGLDANHRELFyNYLIETYQENPRTFVI-STHLIEEISNlLEKVIIL 201
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNV-NEIIHRYVREQNIAVLwVTHDKDEINH-ADKVITL 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-49 |
2.88e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 44.23 E-value: 2.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 505238906 1 MSLIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIIN 49
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN 49
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-194 |
3.42e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 44.26 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFDTKGKITLDGRL------VTENEKSLNNIH- 77
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVeffnqnIYERRVNLNRLRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 78 ----LMSEDDLYPsklkiKSLFHLMEGFYGNFDWR-------------LANEMLSEFELEPTKRMNKLSTGYRSIAKLII 140
Cdd:PRK14258 89 qvsmVHPKPNLFP-----MSVYDNVAYGVKIVGWRpkleiddivesalKDADLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 141 ALCVPCEYIFLDEPVLGLDAnhrelFYNYLIETYQENPR-----TFVISTHLIEEISNL 194
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDP-----IASMKVESLIQSLRlrselTMVIVSHNLHQVSRL 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-59 |
3.59e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 3.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQA-EKIyGLLGNNGAGKSTLLNIINNRIFDTKGKI 59
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAgERL-AIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-81 |
4.11e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.15 E-value: 4.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenEKSLNNIHLMSE 81
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR-----DGQLRDLYALSE 80
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-166 |
4.96e-05 |
|
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: 43.25 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSL-NNIHLMSE 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIaRGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 DDlypsklKIKSLFHLMEG--FYGNFDWR------LANEMLSEFELEPtkrMNKLSTGYR---SIAKLIiaLCVPCEYIf 150
Cdd:cd03231 81 AP------GIKTTLSVLENlrFWHADHSDeqveeaLARVGLNGFEDRP---VAQLSAGQQrrvALARLL--LSGRPLWI- 148
|
170
....*....|....*.
gi 505238906 151 LDEPVLGLDANHRELF 166
Cdd:cd03231 149 LDEPTTALDKAGVARF 164
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-223 |
7.28e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 7 NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNrIF---DTKGKITLDGRLV-------TEnEKSLNNI 76
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYphgTYEGEIIFEGEELqasnirdTE-RAGIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 77 H--LMseddLYPSKLKIKSLF---HLMEGFYGNFD--WRLANEMLSEFELE--PTKRMNKLSTGYRS---IAKliiALCV 144
Cdd:PRK13549 88 HqeLA----LVKELSVLENIFlgnEITPGGIMDYDamYLRAQKLLAQLKLDinPATPVGNLGLGQQQlveIAK---ALNK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 145 PCEYIFLDEPVLGLDANHRELFYNyLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILENtHIVT 223
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLD-IIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTED-DIIT 237
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
127-203 |
7.44e-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: 42.35 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 127 KLSTGYRSIA----KLIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVIsTHLiEEISNLLEKVIILD 202
Cdd:cd03227 77 QLSGGEKELSalalILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVI-THL-PELAELADKLIHIK 154
|
.
gi 505238906 203 K 203
Cdd:cd03227 155 K 155
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-62 |
7.46e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 7.46e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 505238906 7 NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLD 62
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-207 |
7.61e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 43.33 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTEN-EKSLNNIHLMSEDDLYPSKLKIKSLfh 96
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlQKNLVAYVPQSEEVDWSFPVLVEDV-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 97 LMEGFYGNFDW-RLANEMLSEFELEPTKRMNKLSTGYRSIAK----------LIIALCVPCEYIFLDEPVLGLDANHREL 165
Cdd:PRK15056 101 VMMGRYGHMGWlRRAKKRDRQIVTAALARVDMVEFRHRQIGElsggqkkrvfLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505238906 166 FYNYLIETYQENpRTFVISTHLIEEISNLLEKVIILdKGKII 207
Cdd:PRK15056 181 IISLLRELRDEG-KTMLVSTHNLGSVTEFCDYTVMV-KGTVL 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-64 |
9.04e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 42.91 E-value: 9.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNrIFDTKGKITLDGR 64
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGR 57
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-78 |
9.53e-05 |
|
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: 42.91 E-value: 9.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 17 VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGrlvtENEKSLNNIHL 78
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL-ERFYDpTSGEILLDG----VDIRDLNLRWL 75
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-209 |
9.72e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.16 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 3 LIIENLYKTYGKK---NVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDG-RLVTENEKSLNN--- 75
Cdd:PRK13642 5 LEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGeLLTAENVWNLRRkig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 76 ----------IHLMSEDDL--------YPSKLKIKSLFHLMegfygnfdwrLANEMLSEFELEPTkrmnKLSTGYRSIAK 137
Cdd:PRK13642 85 mvfqnpdnqfVGATVEDDVafgmenqgIPREEMIKRVDEAL----------LAVNMLDFKTREPA----RLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505238906 138 LIIALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQENPRTFVISTHLIEEISNlLEKVIILDKGKIIKD 209
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-218 |
1.66e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.14 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 6 ENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIIN-----NRIFDTKGKITLDGRLVTENEksLNNIHLMS 80
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLFGRNIYSPD--VDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 81 EDDL---YPSK-------------LKIKSLFHLMEGFYGNFDWRLANEMLSEfelEPTKRMN----KLSTGYRSIAKLII 140
Cdd:PRK14267 86 EVGMvfqYPNPfphltiydnvaigVKLNGLVKSKKELDERVEWALKKAALWD---EVKDRLNdypsNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 141 ALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQEnpRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENILEN 218
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-160 |
1.71e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 13 GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIfdTKGKITLDGRLV------TENEKSL-----NNIHL--- 78
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVngrpldSSFQRSIgyvqqQDLHLpts 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 79 -------------------MSEDDLYPSK-LKIKSLFHLMEGFYGnfdwrLANEMLSefeLEPTKRmnkLSTGYRSIAKl 138
Cdd:TIGR00956 852 tvreslrfsaylrqpksvsKSEKMEYVEEvIKLLEMESYADAVVG-----VPGEGLN---VEQRKR---LTIGVELVAK- 919
|
170 180
....*....|....*....|..
gi 505238906 139 iialcvPCEYIFLDEPVLGLDA 160
Cdd:TIGR00956 920 ------PKLLLFLDEPTSGLDS 935
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-64 |
5.28e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 40.74 E-value: 5.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 505238906 19 NNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR 64
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ 67
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-48 |
5.48e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 5.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNII 48
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI 47
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-211 |
6.41e-04 |
|
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: 40.09 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 2 SLIIENLYKTYGKK--NVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRlvtenekslnNIHLM 79
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----------DISTI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 80 SEDDLYpSKLKI----KSLFhlMEGFYGNFDwrlANEMLSEFE----LEPTKRMNKLSTGYRSIAKLIIALCVPCEYIFL 151
Cdd:cd03369 76 PLEDLR-SSLTIipqdPTLF--SGTIRSNLD---PFDEYSDEEiygaLRVSEGGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 152 DEPVLGLDANHRELFYNYLIETYQENprTFVISTHLIEEISNlLEKVIILDKGKIIKDDS 211
Cdd:cd03369 150 DEATASIDYATDALIQKTIREEFTNS--TILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-65 |
6.42e-04 |
|
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: 40.15 E-value: 6.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 3 LIIENLYKTYGKKN-----VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRL 65
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI 68
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-67 |
7.61e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.85 E-value: 7.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 505238906 15 KNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDGRLVT 67
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI-QRHFDvSEGDIRFHDIPLT 380
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-207 |
8.67e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 40.71 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 13 GKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIInNRIFD-TKGKITLDG---RLVTenEKSL--------------- 73
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-QRVFDpQSGRILIDGtdiRTVT--RASLrrniavvfqdaglfn 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 74 ----NNIHLMSED----DLYPSkLKIKSLFHLMEGFYGNFDwrlanEMLSEfeleptkRMNKLSTGYR---SIAKliiAL 142
Cdd:PRK13657 423 rsieDNIRVGRPDatdeEMRAA-AERAQAHDFIERKPDGYD-----TVVGE-------RGRQLSGGERqrlAIAR---AL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505238906 143 CVPCEYIFLDEPVLGLDANhRELFYNYLIETYQENPRTFVIStHLIEEISNlLEKVIILDKGKII 207
Cdd:PRK13657 487 LKDPPILILDEATSALDVE-TEAKVKAALDELMKGRTTFIIA-HRLSTVRN-ADRILVFDNGRVV 548
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-217 |
1.02e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 39.73 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHL-----MSEDDLYPSKLKIK 92
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIgivfqNPDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 93 SLFHLmEGFYGNFD--WRLANEMLSEFEL------EPtkrmNKLSTGYRSIAKLIIALCVPCEYIFLDEPVLGLDANHRE 164
Cdd:PRK13648 105 VAFGL-ENHAVPYDemHRRVSEALKQVDMleradyEP----NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505238906 165 LFYNYLIETYQENPRTFVISTHLIEEISNlLEKVIILDKGKIIKDDSVENILE 217
Cdd:PRK13648 180 NLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-62 |
1.09e-03 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 39.34 E-value: 1.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 3 LIIENLYKTY------GKK-NVLNNISVNFQAEKIYGLLGNNGAGKSTLLNII--NNRIfdTKGKITLD 62
Cdd:COG4778 5 LEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLP--DSGSILVR 71
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-63 |
1.34e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDG 63
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-76 |
1.68e-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: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505238906 2 SLIIENLYKTY-GKKNVLNNISVNF-QAEKIYgLLGNNGAGKSTLLNIIN--NRIfdTKGKITLDGRLVTENEKSLNNI 76
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVaDGEFIV-LVGPSGCGKSTLLRMVAglERI--TSGEIWIGGRVVNELEPADRDI 78
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-63 |
1.80e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 38.79 E-value: 1.80e-03
10 20 30
....*....|....*....|....*....|....*...
gi 505238906 26 QAEKIyGLLGNNGAGKSTLLNIINNRIFDTKGKITLDG 63
Cdd:PRK10771 24 RGERV-AILGPSGAGKSTLLNLIAGFLTPASGSLTLNG 60
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-68 |
1.86e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.76 E-value: 1.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 18 LNNISVN---------FQAEKIYGLLGNNGAGKSTLLNIINNrIFDTKGKITLDGRLVTE 68
Cdd:PRK03695 3 LNDVAVStrlgplsaeVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEA 61
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-48 |
2.20e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 2.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 505238906 6 ENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNII 48
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-221 |
2.23e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.65 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 17 VLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDT--------KGKITLDGR-LVTENEKSLNNIHLM-------- 79
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEpLAAIDAPRLARLRAVlpqaaqpa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 80 ---SEDDL-----YPSKLKIKSLFHLmegfygnfDWRLANEMLSEFELEPTKR--MNKLSTG-------YRSIAKLIIA- 141
Cdd:PRK13547 96 fafSAREIvllgrYPHARRAGALTHR--------DGEIAWQALALAGATALVGrdVTTLSGGelarvqfARVLAQLWPPh 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 142 -LCVPCEYIFLDEPVLGLDANHRelfyNYLIETYQENPRTFVISTHLIEEISNL----LEKVIILDKGKIIKDDSVENIL 216
Cdd:PRK13547 168 dAAQPPRYLLLDEPTAALDLAHQ----HRLLDTVRRLARDWNLGVLAIVHDPNLaarhADRIAMLADGAIVAHGAPADVL 243
|
....*
gi 505238906 217 ENTHI 221
Cdd:PRK13547 244 TPAHI 248
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-64 |
2.31e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.39 E-value: 2.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 505238906 7 NLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGR 64
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ 63
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-48 |
2.32e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.47 E-value: 2.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 505238906 3 LIIENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNII 48
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI 53
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-68 |
2.69e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 38.56 E-value: 2.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505238906 1 MSLIIE--NL---YKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTE 68
Cdd:PRK13650 1 MSNIIEvkNLtfkYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE 73
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-186 |
2.76e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 38.29 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 35 GNNGAGKSTLLNIINNRIFDTKGKITLDGRLVTENEKSLNNIHLMSEDDLYPSKLKIKSLfHLMEGFYGNFDWRLANEML 114
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENL-HFLCGLHGRRAKQMPGSAL 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 115 SEFELEPTKR--MNKLSTGYR---SIAKLIIAlcvPCEYIFLDEPVLGLDANHRELFyNYLIETYQENPRTFVISTH 186
Cdd:PRK13543 123 AIVGLAGYEDtlVRQLSAGQKkrlALARLWLS---PAPLWLLDEPYANLDLEGITLV-NRMISAHLRGGGAALVTTH 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-215 |
3.36e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.56 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 5 IENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDGRLV---TENEKSLNNIHLMSE 81
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 82 -----------DDLYPSKLKIKSLFHLMEGFYgnfdwRLANEMLSEFELE--PTKRMNKLSTGYRSIAKLIIALCVPCEY 148
Cdd:PRK10982 81 elnlvlqrsvmDNMWLGRYPTKGMFVDQDKMY-----RDTKAIFDELDIDidPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 149 IFLDEPVLGL---DANHreLFynYLIETYQENPRTFVISTHLIEEISNLLEKVIILDKGKIIKDDSVENI 215
Cdd:PRK10982 156 VIMDEPTSSLtekEVNH--LF--TIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-63 |
3.65e-03 |
|
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: 37.85 E-value: 3.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505238906 6 ENLYKTYG--KKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDG 63
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG 63
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-64 |
3.69e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 38.22 E-value: 3.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505238906 6 ENLYKTYGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLL---NIINNRI--FDTKGKITLDGR 64
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIpgFRVEGKVTFHGK 77
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-63 |
3.89e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 3.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 505238906 18 LNNISVNFQAEKIYGLLGNNGAGKSTLLNIINNRIFDTKGKITLDG 63
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
141-207 |
6.90e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 37.90 E-value: 6.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505238906 141 ALCVPCEYIFLDEPVLGLDANHRELFYNYLIETYQEnpRTFVISTHLIEEISNlLEKVIILDKGKII 207
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQ-WDQIWVMQDGQIV 562
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-48 |
9.55e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.30 E-value: 9.55e-03
10 20 30
....*....|....*....|....*....|....*..
gi 505238906 12 YGKKNVLNNISVNFQAEKIYGLLGNNGAGKSTLLNII 48
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| |
