|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-212 |
1.69e-64 |
|
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: 198.86 E-value: 1.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVI 86
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHLDLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQR 166
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391525485 167 LDQEGIDWLGKRLRHEKEHNGlAIIMASHEPslVEAVGARIVRIGG 212
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGG-AVLLTTHQP--LELAAARVLDLGD 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-213 |
7.75e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.86 E-value: 7.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVID 87
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391525485 166 RLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-213 |
3.27e-46 |
|
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: 152.37 E-value: 3.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDtEISFRRNVATVID 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLLARAHGLEDTDelVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRL 167
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKR--IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391525485 168 DQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03268 158 DPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-222 |
2.92e-45 |
|
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: 150.78 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVI 86
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLfdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 165 QRLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIVRI-GGGLEETQSLAE 222
Cdd:COG4555 161 NGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILhKGKVVAQGSLDE 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-213 |
1.80e-43 |
|
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: 144.08 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVID 87
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDllarahgledtdelvdsileevqlvpqsgqlpgtLSSGQRRRLALATAFV-RPkKLLVLDEPEQR 166
Cdd:cd03230 81 EPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLhDP-ELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391525485 167 LDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03230 126 LDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-208 |
1.03e-39 |
|
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: 136.10 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGD--HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATV 85
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLpkSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1391525485 164 eqrldQEGIDWLGKR-----LRHEKEhnGLAIIMASHEPSLVEAVGARIV 208
Cdd:cd03263 161 -----TSGLDPASRRaiwdlILEVRK--GRSIILTTHSMDEAEALCDRIA 203
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-213 |
4.11e-37 |
|
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: 128.74 E-value: 4.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 9 KISNLVKKYGDHT--VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVATV 85
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDldffPD-----LSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLL 158
Cdd:cd03225 81 FQN----PDdqffgPTVEEEVAFGLENLGLpeEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 159 VLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-223 |
2.08e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 128.38 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYG----DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNV 82
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDD--LDFFPDLSVVEHLDLLARAHGLEDTDELVDSILEEVQLvPQS--GQLPGTLSSGQRRRLALATAFV-RPkKL 157
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGL-PPSflDRYPHQLSGGQRQRVAIARALIlEP-EL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 158 LVLDEPEQRLD---QEGIDWLGKRLRHEKehnGLAIIMASHEPSLVEAVGARIVRIGGG-LEETQSLAEP 223
Cdd:COG1124 160 LLLDEPTSALDvsvQAEILNLLKDLREER---GLTYLFVSHDLAVVAHLCDRVAVMQNGrIVEELTVADL 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-208 |
4.57e-35 |
|
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: 123.78 E-value: 4.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVID 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLD--LLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:cd03259 80 DYALFPHLTVAENIAfgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391525485 166 RLDQEgidwLGKRLRHE-----KEHnGLAIIMASHEPSLVEAVGARIV 208
Cdd:cd03259 160 ALDAK----LREELREElkelqREL-GITTIYVTHDQEEALALADRIA 202
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-213 |
1.43e-34 |
|
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: 122.25 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK--AKDTEIS-FRRNVAT 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINeLRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVEHLDL-LARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLaPIKVKGMskAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 162 EPEQRLDQEGI-DWLG--KRLRHEkehnGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03262 161 EPTSALDPELVgEVLDvmKDLAEE----GMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-214 |
2.70e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTeisfRRNVAT 84
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDF---FPdLSVVE--------HLDLLARAHGLEdtDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVR 153
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDvvlmgrygRRGLFRRPSRAD--REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 154 PKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIVRIGGGL 214
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-213 |
3.10e-34 |
|
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: 120.37 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS---FRRNVAT 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVEHLDLLarahgledtdelvdsileevqlvpqsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391525485 165 QRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-213 |
6.12e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.69 E-value: 6.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIeVLGEKAKDTE--ISFRRNVATV 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-YLDGKPLSAMppPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDlSVVEHLDLLARAHGLEDTDELVDSILEEVQLVPQS-GQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391525485 165 QRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-214 |
6.82e-34 |
|
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: 120.72 E-value: 6.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 9 KISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTeisfRRNVATV--I 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVpqR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDF-FPdLSvVEHLDLLARAHGL-------EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLL 158
Cdd:cd03235 77 RSIDRdFP-IS-VRDVVLMGLYGHKglfrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 159 VLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIVRIGGGL 214
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-213 |
7.81e-34 |
|
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: 120.90 E-value: 7.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKY-GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS-FRRNV--- 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLReLRRKVglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ----------ATVIDDLDFFPdlsvvehldllaRAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATA 150
Cdd:COG1122 81 fqnpddqlfaPTVEEDVAFGP------------ENLGLprEEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 151 FV-RPkKLLVLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG1122 149 LAmEP-EVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-213 |
9.34e-34 |
|
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: 121.07 E-value: 9.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 10 ISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTE-ISFRRNVATV 85
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisGLSEAElYRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDLSVVEHLDLLARAHG---LEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDE 162
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREHTrlsEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 163 PEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-213 |
1.52e-33 |
|
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: 118.12 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 9 KISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNvatvidd 88
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 89 ldffpdlsvvehldllarahgledtdelvdsileEVQLVPQsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:cd00267 74 ----------------------------------RIGYVPQ-------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1391525485 169 QEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd00267 113 PASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-213 |
3.26e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.00 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKY-GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEISF-RRN 81
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREIPYlRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VATVIDDLDFFPDLSVVEHLDLLARAHGLEDTD--ELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFV-RPkKLL 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEirRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVnRP-ELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 159 VLDEPEQRLDQE---GIdwlgkrLRHEKEHN--GLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG2884 160 LADEPTGNLDPEtswEI------MELLEEINrrGTTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-213 |
1.29e-32 |
|
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: 117.59 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGD----HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEISF-- 78
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 79 RRNVATVIDDLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVpkKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 157 LLVLDEPEQRLDQEgidwLGKR----LRHEKEHNGLAIIMASHEPSLVEAvGARIVRIGGG 213
Cdd:cd03255 161 IILADEPTGNLDSE----TGKEvmelLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDG 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-170 |
1.68e-32 |
|
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: 116.91 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVyESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVID 87
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLLARAHGLEDT--DELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKevKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
....*
gi 1391525485 166 RLDQE 170
Cdd:cd03264 160 GLDPE 164
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-195 |
9.89e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 9.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIsFRRNVA 83
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 TVIDDLDFFPDLSVVEHLdllarAHGL-------EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFV-RPk 155
Cdd:COG3842 81 MVFQDYALFPHLTVAENV-----AFGLrmrgvpkAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALApEP- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1391525485 156 KLLVLDEPEQRLDQEgidwLGKRLRHE-----KEHnGLAIIMASH 195
Cdd:COG3842 155 RVLLLDEPLSALDAK----LREEMREElrrlqREL-GITFIYVTH 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-163 |
1.27e-31 |
|
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: 112.74 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 23 IDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG-EKAKDTEISFRRNVATVIDDLDFFPDLSVVEHL 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 102 DLLARAHGLEDT--DELVDSILEEVQLVPQS----GQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:pfam00005 81 RLGLLLKGLSKRekDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-208 |
1.42e-31 |
|
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: 120.39 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 2 ARRSTVLKISNLVKKY-----GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKD 73
Cdd:COG1123 255 AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 74 TEIS-FRRNVATVIDDLD--FFPDLSVVEHLDLLARAHGL---EDTDELVDSILEEVQLVPQSGQ-LPGTLSSGQRRRLA 146
Cdd:COG1123 335 RSLReLRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLlsrAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 147 LATAFV-RPkKLLVLDEPEQRLD---QEGIdwlGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIV 208
Cdd:COG1123 415 IARALAlEP-KLLILDEPTSALDvsvQAQI---LNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-213 |
4.62e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.60 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGD----HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEIS 77
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 78 -FRR-NVATVIDDLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVR 153
Cdd:COG1136 82 rLRRrHIGFVFQFFNLLPELTALENVALPLLLAGVsrKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 154 PKKLLVLDEPEQRLDQEgidwLGKR----LRHEKEHNGLAIIMASHEPSLVEAVGaRIVRIGGG 213
Cdd:COG1136 162 RPKLILADEPTGNLDSK----TGEEvlelLRELNRELGTTIVMVTHDPELAARAD-RVIRLRDG 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-213 |
7.40e-31 |
|
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: 113.37 E-value: 7.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKY----GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEISFR 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RN-VATVIDD----LDffPDLSVVEHLDLLARAHGLEDTDEL----VDSILEEVQLVPQ-SGQLPGTLSSGQRRRLALAT 149
Cdd:cd03257 81 RKeIQMVFQDpmssLN--PRMTIGEQIAEPLRIHGKLSKKEArkeaVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391525485 150 AFVRPKKLLVLDEPEQRLD---QEGIDWLGKRLRHEKehnGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03257 159 ALALNPKLLIADEPTSALDvsvQAQILDLLKKLQEEL---GLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-208 |
5.17e-30 |
|
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: 110.85 E-value: 5.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 15 KKYGDHTVIDHFNLqvyESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISF-----RRNVATVIDDL 89
Cdd:cd03297 8 KRLPDFTLKIDFDL---NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 90 DFFPDLSVVEHLDLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQ 169
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391525485 170 EGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIV 208
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-213 |
3.40e-29 |
|
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: 106.38 E-value: 3.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlgekAKDTEISFrrnvatvid 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----GSTVKIGY--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 dldffpdlsvvehldllarahgledtdelvdsileevqlVPQsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPEQRL 167
Cdd:cd03221 68 ---------------------------------------FEQ-------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391525485 168 DQEGIDWLGKRLrheKEHNGlAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03221 102 DLESIEALEEAL---KEYPG-TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-213 |
4.58e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 12 NLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGT-----IEVLGEKAKDTEIsfRRNVATVI 86
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKVDERLI--RQEAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHL---DLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAF-VRPkKLLVLDE 162
Cdd:PRK09493 84 QQFYLFPHLTALENVmfgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALaVKP-KLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 163 PEQRLDQEgidwlgkrLRHEK-------EHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK09493 163 PTSALDPE--------LRHEVlkvmqdlAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-208 |
1.16e-28 |
|
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: 107.17 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGD----HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTeisfRRNVA 83
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP----GPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 TVIDDLDFFPDLSVVEHLDLLARAHGLEDTD--ELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLD 161
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEarERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391525485 162 EPEQRLDQ---EGI-DWLGKRLRHEkehnGLAIIMASHepSLVEAV--GARIV 208
Cdd:cd03293 157 EPFSALDAltrEQLqEELLDIWRET----GKTVLLVTH--DIDEAVflADRVV 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-199 |
2.59e-28 |
|
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: 107.05 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDteISFR---RNVA 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS--LSRRelaRRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 TVIDDLDFFPDLSVVE--------HLDLLARaHGLEDtDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPK 155
Cdd:COG1120 79 YVPQEPPAPFGLTVRElvalgrypHLGLFGR-PSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391525485 156 KLLVLDEPEQRLD---QegIDWLgKRLRHEKEHNGLAIIMASHEPSL 199
Cdd:COG1120 157 PLLLLDEPTSHLDlahQ--LEVL-ELLRRLARERGRTVVMVLHDLNL 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
7-212 |
2.74e-28 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 106.04 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNV---- 82
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 -ATVIDDldffpDLSVVEHLDLLARAHGLEDTDELVDsILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLD 161
Cdd:PRK13538 81 hQPGIKT-----ELTALENLRFYQRLHGPGDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 162 EPEQRLDQEGIDWLGKRLRHEKEHNGLAiIMASHEPSLVEAVGARIVRIGG 212
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTHQDLPVASDKVRKLRLGQ 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-213 |
5.39e-28 |
|
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: 106.22 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTE-ISFR 79
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditGLSEKElYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATViddldF-----FPDLSVVEHLDLLARAHGL---EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAF 151
Cdd:COG1127 82 RRIGML-----FqggalFDSLTVFENVAFPLREHTDlseAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 152 V-RPkKLLVLDEPEQRLDQEG---IDWLGKRLRHEkehNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG1127 157 AlDP-EILLYDEPTAGLDPITsavIDELIRELRDE---LGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-213 |
5.94e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 5.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 2 ARRS--TVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEvLGEKakdTEISFr 79
Cdd:COG0488 308 PERLgkKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGET---VKIGY- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 rnVATVIDDLDffPDLSVVEHLdllarAHGLEDTDEL-VDSIL-------EEVQlvpqsgQLPGTLSSGQRRRLALATAF 151
Cdd:COG0488 383 --FDQHQEELD--PDKTVLDEL-----RDGAPGGTEQeVRGYLgrflfsgDDAF------KPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 152 VRPKKLLVLDEPEQRLDQEGIDWLGKRLrheKEHNGlAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEAL---DDFPG-TVLLVSHDRYFLDRVATRILEFEDG 505
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-163 |
8.63e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 105.21 E-value: 8.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEISfRRNVAT 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditGLPPHERA-RAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVEHLDLLARAHGLEDTDELVDSILEEV-QLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-226 |
1.28e-27 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.08 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK--AKDTEIS-FRRNVA 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDltDSKKDINkLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 TVIDDLDFFPDLSVVEHLDL-LARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFV-RPKKLLv 159
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLaPIKVKKMskAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAmEPKVML- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 160 LDEPEQRLDQEgidWLG------KRLRHEkehnGLAIIMASHEPSLVEAVGARIVRIGGG--LEEtqslAEPEQL 226
Cdd:COG1126 160 FDEPTSALDPE---LVGevldvmRDLAKE----GMTMVVVTHEMGFAREVADRVVFMDGGriVEE----GPPEEF 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-208 |
1.28e-27 |
|
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: 104.26 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVID 87
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLdllarAHGLEDTDELVDSILEEVQLVPQSGQL-------PGTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:cd03301 80 NYALYPHMTVYDNI-----AFGLKLRKVPKDEIDERVREVAELLQIehlldrkPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1391525485 161 DEPEQRLDQEgidwLGKRLRHE-----KEHnGLAIIMASHEPSLVEAVGARIV 208
Cdd:cd03301 155 DEPLSNLDAK----LRVQMRAElkrlqQRL-GTTTIYVTHDQVEAMTMADRIA 202
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-227 |
1.29e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.84 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVidHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVID 87
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLlARAHGLEDTDE---LVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:COG3840 79 ENNLFPHLTVAQNIGL-GLRPGLKLTAEqraQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 165 QRLD----QEGIDWLgKRLRHEKehnGLAIIMASHEPSLVEAVGARIVRIGGG-------LEETQSLAEPEQLA 227
Cdd:COG3840 158 SALDpalrQEMLDLV-DELCRER---GLTVLMVTHDPEDAARIADRVLLVADGriaadgpTAALLDGEPPPALA 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-213 |
3.02e-27 |
|
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: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKakdTEISFRRNVATVID 87
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP---LDIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLkkEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391525485 166 RLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03269 158 GLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-163 |
4.32e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.93 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARrstvLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRR 80
Cdd:COG3839 1 MAS----LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NVATVIDDLDFFPDLSVVEHLdllarAHGL-------EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVR 153
Cdd:COG3839 76 NIAMVFQSYALYPHMTVYENI-----AFPLklrkvpkAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170
....*....|
gi 1391525485 154 PKKLLVLDEP 163
Cdd:COG3839 151 EPKVFLLDEP 160
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-208 |
5.76e-27 |
|
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: 103.09 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIsFRRNVATVID 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-HKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLdllarAHGL-------EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:cd03300 80 NYALFPHLTVFENI-----AFGLrlkklpkAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 161 DEPEQRLD-------QEGIDWLGKRLrhekehnGLAIIMASHEPSLVEAVGARIV 208
Cdd:cd03300 155 DEPLGALDlklrkdmQLELKRLQKEL-------GITFVFVTHDQEEALTMSDRIA 202
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-213 |
6.23e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 10 ISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlgekAKDTEISFrrnvatVIDDL 89
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----PKGLRIGY------LPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 90 DFFPDLSVVEHL--------DLLARAHGLE----DTDEL----------------------VDSILEEVQLVPQSGQLP- 134
Cdd:COG0488 71 PLDDDLTVLDTVldgdaelrALEAELEELEaklaEPDEDlerlaelqeefealggweaearAEEILSGLGFPEEDLDRPv 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 135 GTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLrheKEHNGlAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL---KNYPG-TVLVVSHDRYFLDRVATRILELDRG 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-213 |
1.71e-26 |
|
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: 101.42 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 25 HFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVIDDLDFFPDLSVVEHLDLl 104
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRPVSMLFQENNLFAHLTVEQNVGL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 105 ARAHGL---EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD---QEGIDWLGKR 178
Cdd:cd03298 94 GLSPGLkltAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1391525485 179 LRHEKehnGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03298 174 LHAET---KMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
8-182 |
2.25e-26 |
|
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: 102.03 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVID 87
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLdllarAHGLE-----------DTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAF-VRPK 155
Cdd:cd03296 82 HYALFRHMTVFDNV-----AFGLRvkprserppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALaVEPK 156
|
170 180 190
....*....|....*....|....*....|.
gi 1391525485 156 KLLvLDEPEQRLD----QEGIDWLgKRLRHE 182
Cdd:cd03296 157 VLL-LDEPFGALDakvrKELRRWL-RRLHDE 185
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-208 |
5.54e-26 |
|
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: 100.59 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEISfRRNVAT 84
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditGLPPHEIA-RLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVE------------HLDLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFV 152
Cdd:cd03219 80 TFQIPRLFPELTVLEnvmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 153 RPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIV 208
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVT 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-223 |
6.42e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 101.30 E-value: 6.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 11 SNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTI----EVLGEKAKDTEISFRRNVATVI 86
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgEPLAKLNRAQRKAFRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDL--DFFPDLSVVE-------HLDLLARAHGLEDTDELvdsiLEEVQLVPQ-SGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:PRK10419 96 QDSisAVNPRKTVREiireplrHLLSLDKAERLARASEM----LRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 157 LLVLDEPEQRLD---QEGIDWLGKRLRHEkehNGLAIIMASHEPSLVEAVGARIVRI-GGGLEETQSLAEP 223
Cdd:PRK10419 172 LLILDEAVSNLDlvlQAGVIRLLKKLQQQ---FGTACLFITHDLRLVERFCQRVMVMdNGQIVETQPVGDK 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
34-210 |
6.69e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 99.36 E-value: 6.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 34 DAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVIDDLDFFPDLSVVEHLDLLARAHGLEDT 113
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFWAAIHGGAQR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 114 DelVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRhEKEHNGLAIIMA 193
Cdd:TIGR01189 107 T--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLR-AHLARGGIVLLT 183
|
170
....*....|....*..
gi 1391525485 194 SHEPslVEAVGARIVRI 210
Cdd:TIGR01189 184 THQD--LGLVEARELRL 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-180 |
7.04e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATV- 85
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 -IDDLDffPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDE 162
Cdd:PRK13537 87 qFDNLD--PDFTVRENLLVFGRYFGLsaAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170
....*....|....*...
gi 1391525485 163 PEQRLDQEGIDWLGKRLR 180
Cdd:PRK13537 165 PTTGLDPQARHLMWERLR 182
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-226 |
8.09e-26 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 100.45 E-value: 8.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGD-HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDT-EISFRRNVATV 85
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQS--GQLPGTLSSGQRRRLALATAFVRPKKLLVLD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWpkEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391525485 162 EPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEpsLVEAV--GARIVRIGGGleETQSLAEPEQL 226
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD--IDEAFrlADRIAIMKNG--EIVQVGTPDEI 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-208 |
1.04e-25 |
|
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: 99.95 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGD-HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEI-SFRRNV 82
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDDLDFFPDLSVVEH-----------LDLLARAHGLEDTdELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAF 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrlgrrstWRSLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 152 VRPKKLLVLDEPEQRLD----QEGIDWLgKRLRHEKehnGLAIIMASHEPSLVEAVGARIV 208
Cdd:cd03256 160 MQQPKLILADEPVASLDpassRQVMDLL-KRINREE---GITVIVSLHQVDLAREYADRIV 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-213 |
1.40e-25 |
|
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: 98.28 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 9 KISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISFRRNVATVid 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 dldffpdLSVVEHLDLLarahgledtdELVDSILEEvqlvpqsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPEQRL 167
Cdd:cd03214 79 -------PQALELLGLA----------HLADRPFNE-------------LSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391525485 168 DQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-163 |
2.07e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 101.38 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIeVLGEKAKDTEISFR-RNVATVI 86
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI-VLNGRDLFTNLPPReRRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHL--DLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAF-VRPkKLLVLDEP 163
Cdd:COG1118 82 QHYALFPHMTVAENIafGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALaVEP-EVLLLDEP 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
10-213 |
3.89e-25 |
|
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: 98.21 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 10 ISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVIDDL 89
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 90 DFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRL 167
Cdd:cd03265 83 SVDDELTGWENLYIHARLYGVpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391525485 168 DQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-213 |
5.23e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.41 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDteisfrrnvatvi 86
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFF----------PDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFV-R 153
Cdd:COG4152 68 EDRRRIgylpeerglyPKMKVGEQLVYLARLKGLskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLhD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 154 PkKLLVLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG4152 148 P-ELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKG 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-213 |
5.65e-25 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 102.15 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 2 ARRSTVLKISNLVKKY--GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISF 78
Cdd:COG4987 328 APGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 79 RRNVATVIDDLDFFPDlSVVEHLdLLARAHGleDTDELVDSiLEEVQLVPQSGQLPG-----------TLSSGQRRRLAL 147
Cdd:COG4987 408 RRRIAVVPQRPHLFDT-TLRENL-RLARPDA--TDEELWAA-LERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 148 ATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEhnGLAIIMASHEPSLVEAVgARIVRIGGG 213
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDG 545
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-195 |
6.81e-25 |
|
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: 97.64 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCI-----VGSDKPTEGTIEVLGE---KAKDTEISFR 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDDLDFFPdLSVVEHLDLLARAHGL---EDTDELVDSILEEVQLVPQSG--QLPGTLSSGQRRRLALATAFVRP 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIklkEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391525485 155 KKLLVLDEPEQRLD---QEGIDWLGKRLRHEkehngLAIIMASH 195
Cdd:cd03260 160 PEVLLLDEPTSALDpisTAKIEELIAELKKE-----YTIVIVTH 198
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-195 |
7.27e-25 |
|
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: 98.23 E-value: 7.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEG-TIEVLGEKAKDTEIS-FRRNV 82
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWeLRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDDL--DFFPDLSVVE-----HLDLLARAHGLEDTD-ELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRP 154
Cdd:COG1119 81 GLVSPALqlRFPRDETVLDvvlsgFFDSIGLYREPTDEQrERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391525485 155 KKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASH 195
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-208 |
8.17e-25 |
|
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: 95.57 E-value: 8.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAkdteisfrrNVATVID 87
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------SFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 dldffpdlsvvehldllARAHGledtdelvdsileeVQLVPQsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPEQRL 167
Cdd:cd03216 72 -----------------ARRAG--------------IAMVYQ-------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391525485 168 DQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIV 208
Cdd:cd03216 114 TPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVT 153
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-208 |
8.77e-25 |
|
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: 97.22 E-value: 8.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 2 ARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGekakdteisfrrN 81
Cdd:cd03220 17 SSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VATVID-DLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLvPQSGQLP-GTLSSGQRRRLALATA-FVRPkK 156
Cdd:cd03220 85 VSSLLGlGGGFNPELTGRENIYLNGRLLGLsrKEIDEKIDEIIEFSEL-GDFIDLPvKTYSSGMKARLAFAIAtALEP-D 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391525485 157 LLVLDEpeqrldqegidWLG-----------KRLRHEKEHNGlAIIMASHEPSLVEAVGARIV 208
Cdd:cd03220 163 ILLIDE-----------VLAvgdaafqekcqRRLRELLKQGK-TVILVSHDPSSIKRLCDRAL 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-210 |
1.61e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.97 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK--AKDTEISFRRNV 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDDLDFFPDLSVVEHLDLLARAHGledTDELVDSILEEV-----QLVPQSGQLPGTLSSGQRRRLALATAFVRPKKL 157
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARR---DRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 158 LVLDEP-EqrldqegidwlgkrlrhekehnGLAiimashePSLVEAVGARIVRI 210
Cdd:COG0410 158 LLLDEPsL----------------------GLA-------PLIVEEIFEIIRRL 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
35-212 |
2.24e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.71 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 35 AVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIsfrRNVATVIDDLDFF-PDLSVVEHLDLLARAHGLEDT 113
Cdd:PRK13539 30 ALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHRNAMkPALTVAENLEFWAAFLGGEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 114 DelVDSILEEVQLVPqSGQLP-GTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLaIIM 192
Cdd:PRK13539 107 D--IAAALEAVGLAP-LAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGI-VIA 182
|
170 180
....*....|....*....|
gi 1391525485 193 ASHEPslVEAVGARIVRIGG 212
Cdd:PRK13539 183 ATHIP--LGLPGARELDLGP 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-168 |
4.58e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKisNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVI 86
Cdd:PRK11432 8 VLK--NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVpkEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
....
gi 1391525485 165 QRLD 168
Cdd:PRK11432 165 SNLD 168
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-227 |
5.33e-24 |
|
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: 99.21 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKY--GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPT---EGTIEVLGEKAKDTEISFR 79
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 -RNVATVIDDLD--FFPdLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRP 154
Cdd:COG1123 82 gRRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLsrAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 155 KKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG--LEE---TQSLAEPEQLA 227
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGriVEDgppEEILAAPQALA 238
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
12-214 |
1.33e-23 |
|
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: 94.01 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 12 NLVKKY-GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEISF-RRNVATVI 86
Cdd:cd03292 5 NVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYlRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHLDLLARA--HGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1391525485 165 QRLDQEgIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGGL 214
Cdd:cd03292 165 GNLDPD-TTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
17-213 |
1.65e-23 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 93.77 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 17 YGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGeKAKDTEISFRRNVATVIDDLDFFPDLS 96
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND-QSHTGLAPYQRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 97 VVEHLDLLARAhGLEDT---DELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQ---E 170
Cdd:TIGR01277 87 VRQNIGLGLHP-GLKLNaeqQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPllrE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391525485 171 GIDWLGKRLRHEKEhngLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:TIGR01277 166 EMLALVKQLCSERQ---RTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-195 |
2.07e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.05 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRR 80
Cdd:PRK13536 35 GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NVATV--IDDLDffPDLSVVEHLDLLARAHGLE--DTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:PRK13536 115 RIGVVpqFDNLD--LEFTVRENLLVFGRYFGMStrEIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391525485 157 LLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASH 195
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTH 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-168 |
2.10e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.55 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRR 80
Cdd:PRK09452 8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-NR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NVATVIDDLDFFPDLSVVEHLdllarAHGL-------EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVR 153
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENV-----AFGLrmqktpaAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170
....*....|....*
gi 1391525485 154 PKKLLVLDEPEQRLD 168
Cdd:PRK09452 162 KPKVLLLDESLSALD 176
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-208 |
3.62e-23 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 94.03 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKY--GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD----TEIsfRRN 81
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenlWEI--RKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 V-------------ATVIDDLDFfpdlsvvehldllarahGLE----DTDEL---VDSILEEVQLVPQSGQLPGTLSSGQ 141
Cdd:TIGR04520 79 VgmvfqnpdnqfvgATVEDDVAF-----------------GLEnlgvPREEMrkrVDEALKLVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 142 RRRLALATAF-VRPkKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSlvEAVGA-RIV 208
Cdd:TIGR04520 142 KQRVAIAGVLaMRP-DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDME--EAVLAdRVI 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-226 |
4.17e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.67 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEiSFRRNVATVI 86
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHL------DLLARAhgleDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:PRK11607 98 QSYALFPHMTVEQNIafglkqDKLPKA----EIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 161 DEPEQRLDQEgidwLGKRLRHEK----EHNGLAIIMASHEPSLVEAVGARIVRIGGGleETQSLAEPEQL 226
Cdd:PRK11607 174 DEPMGALDKK----LRDRMQLEVvdilERVGVTCVMVTHDQEEAMTMAGRIAIMNRG--KFVQIGEPEEI 237
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-213 |
5.68e-23 |
|
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: 91.12 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGD--HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS-FRRNVAT 84
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNeLGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDlsvvehldllarahgledtdelvdSILEEVqlvpqsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:cd03246 81 LPQDDELFSG------------------------SIAENI------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391525485 165 QRLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVgARIVRIGGG 213
Cdd:cd03246 125 SHLDVEGERALNQAIAALKA-AGATRIVIAHRPETLASA-DRILVLEDG 171
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-201 |
9.03e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 9.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 15 KKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEkakdteisfrrnVATVID-DLDFFP 93
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------------VSALLElGAGFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 94 DLSVVEHLDLLARAHGL--EDTDELVDSILE--EVqlvpqsGQ---LP-GTLSSGQRRRLALATA-FVRPKKLLVlDEpe 164
Cdd:COG1134 102 ELTGRENIYLNGRLLGLsrKEIDEKFDEIVEfaEL------GDfidQPvKTYSSGMRARLAFAVAtAVDPDILLV-DE-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391525485 165 qrldqegidWLG-----------KRLRHEKEHNGlAIIMASHEPSLVE 201
Cdd:COG1134 173 ---------VLAvgdaafqkkclARIRELRESGR-TVIFVSHSMGAVR 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-163 |
1.20e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 91.84 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlgekaKDTEISF-------RR 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILL-----DGQDITKlpmhkraRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NVATVIDDLDFFPDLSVVEHLDLLARAHGLEDT--DELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLL 158
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKerEEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
....*
gi 1391525485 159 VLDEP 163
Cdd:cd03218 156 LLDEP 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
1.68e-22 |
|
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: 95.21 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 2 ARRSTVLKISNLVKKYGD-HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISFR 79
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVA-----------TVIDDLDFF-PDLSVVEHLDLLARAHGLEDTDEL---VDSILEEvqlvpqSGQlpgTLSSGQRRR 144
Cdd:COG4988 411 RQIAwvpqnpylfagTIRENLRLGrPDASDEELEAALEAAGLDEFVAALpdgLDTPLGE------GGR---GLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 145 LALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEhnGLAIIMASHEPSLVEAVGARIVRIGGGLEETQSLAE 222
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-222 |
3.69e-22 |
|
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: 90.72 E-value: 3.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDH----TVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGekakdTEIS----- 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG-----TDLTllsgk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 78 ----FRRNVATVIDDLDFFPDLSVVEHLDLLARAHGLEDT--DELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAF 151
Cdd:cd03258 76 elrkARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 152 VRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG-LEETQSLAE 222
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGeVVEEGTVEE 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-213 |
5.99e-22 |
|
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: 88.21 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGD--HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISFRRNVAT 84
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPdlsvvehldllarahgledtdelvDSILEEVqlvpqsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:cd03228 81 VPQDPFLFS------------------------GTIRENI------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391525485 165 QRLDQEGIDWLGKRLRheKEHNGLAIIMASHEPSLVEAVgARIVRIGGG 213
Cdd:cd03228 125 SALDPETEALILEALR--ALAKGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-213 |
8.66e-22 |
|
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: 92.97 E-value: 8.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHT--VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVAT 84
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPaSLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDlSVVEHLdLLARAHglEDTDELVDS-----ILEEVQLVPQSGQLP-----GTLSSGQRRRLALATAFVRP 154
Cdd:COG2274 554 VLQDVFLFSG-TIRENI-TLGDPD--ATDEEIIEAarlagLHDFIEALPMGYDTVvgeggSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1391525485 155 KKLLVLDEP--------EQRLDQegidwlgkRLRHEKehNGLAIIMASHEPSLVEAVGaRIVRIGGG 213
Cdd:COG2274 630 PRILILDEAtsaldaetEAIILE--------NLRRLL--KGRTVIIIAHRLSTIRLAD-RIIVLDKG 685
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-200 |
1.03e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 17 YGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKA-----KDTEISfRRNVATVID--DL 89
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpQRSEVP-DSLPLTVRDlvAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 90 DFFPDLSVVEHLDLLARAhgledtdeLVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQ 169
Cdd:NF040873 81 GRWARRGLWRRLTRDDRA--------AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|.
gi 1391525485 170 EGIDWLGKRLRHEKEhNGLAIIMASHEPSLV 200
Cdd:NF040873 153 ESRERIIALLAEEHA-RGATVVVVTHDLELV 182
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-211 |
1.45e-21 |
|
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: 88.32 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVID 87
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLLARAHGledtDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRL 167
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHS----DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391525485 168 DQEGIDWLGKRLRHEKEHNGlAIIMASHEPSLVEAVGARIVRIG 211
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGG-MVVLTTHQDLGLSEAGARELDLG 199
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
6-213 |
3.94e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.12 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAK---DTEISfRRNV 82
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpGHQIA-RMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDDLDFFPDLSVVEHLdLLARA--------HGLEDT-------DELVDSI---LEEVQLVPQSGQLPGTLSSGQRRR 144
Cdd:PRK11300 83 VRTFQHVRLFREMTVIENL-LVAQHqqlktglfSGLLKTpafrraeSEALDRAatwLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 145 LALATAFVRPKKLLVLDEPEQRLD-QEGIDW--LGKRLRHEkehNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNpKETKELdeLIAELRNE---HNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-213 |
7.60e-21 |
|
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: 90.84 E-value: 7.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 10 ISNLVKKY--GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVID 87
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLLARAHG--LEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPeq 165
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGrsWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP-- 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 166 rldQEGIDWLGKRLRHE---KEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:TIGR01257 1089 ---TSGVDPYSRRSIWDlllKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-213 |
1.05e-20 |
|
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: 86.27 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHT----VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVA 83
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 TVIDDLDFFPDLSVVEHLDLLARAHGLEDTDEL--VDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLD 161
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTarLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 162 EPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-223 |
1.06e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEV----LGEKAKDTEISFR 79
Cdd:PRK11247 9 QGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtapLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 rnvatvidDLDFFPDLSVVEHLDLLARAHGLEDTDElvdsILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLV 159
Cdd:PRK11247 89 --------DARLLPWKKVIDNVGLGLKGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 160 LDEPEQRLD-------QEGIDWLGkrlrheKEHnGLAIIMASHEPSLVEAVGARIVRIGG---GLEETQSLAEP 223
Cdd:PRK11247 157 LDEPLGALDaltriemQDLIESLW------QQH-GFTVLLVTHDVSEAVAMADRVLLIEEgkiGLDLTVDLPRP 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-195 |
1.21e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKA--KDTEISFRRNVAT 84
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVE--HLDLLARAHGLEDTDELVD---SILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLV 159
Cdd:COG1129 84 IHQELNLVPNLSVAEniFLGREPRRGGLIDWRAMRRrarELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1391525485 160 LDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASH 195
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISH 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-210 |
1.50e-20 |
|
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: 89.27 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKYGDHT-VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNV 82
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDDLDFFPDLSVVEHLdLLARAhglEDTDELVDSILEEVQLVPQSGQLPGT-----------LSSGQRRRLALATAF 151
Cdd:TIGR02857 398 IAWVPQHPFLFAGTIAENI-RLARP---DASDAEIREALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 152 VRPKKLLVLDEPEQRLDQEGIDWLGKRLRheKEHNGLAIIMASHEPSLVEAVGaRIVRI 210
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALR--ALAQGRTVLLVTHRLALAALAD-RIVVL 529
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-213 |
2.21e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.34 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlGEKAKDTEISF------- 78
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLsqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 79 ---RRNVATVIDDLDFFPDLSVVEHL---DLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFV 152
Cdd:PRK11264 81 rqlRQHVGFVFQNFNLFPHRTVLENIiegPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 153 RPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMaSHEPSLVEAVGARIVRIGGG 213
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIV-THEMSFARDVADRAIFMDQG 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-213 |
5.19e-20 |
|
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: 85.08 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHtVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAkdTEIS-FRRNVATVI 86
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPpEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHLdllarAHGL-------EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLV 159
Cdd:cd03299 78 QNYALFPHMTVYKNI-----AYGLkkrkvdkKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1391525485 160 LDEPEQRLD---QEGIDWLGKRLRHEkehNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03299 153 LDEPFSALDvrtKEKLREELKKIRKE---FGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-212 |
7.84e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKP---TEGTIEVLGEK--AKDTEisfRRNV 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRltALPAE---QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVI-DDLdFFPDLSVVEHLDL-LARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:COG4136 79 GILFqDDL-LFPHLSVGENLAFaLPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 161 DEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGaRIVRIGG 212
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-226 |
8.43e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.02 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE-----KAKDTEI------ 76
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvRDKDGQLkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 77 ---SFRRNVATVIDDLDFFPDLSVVEH-LDLLARAHGLEDTD--ELVDSILEEVQLVPQS-GQLPGTLSSGQRRRLALAT 149
Cdd:PRK10619 86 qlrLLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEarERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 150 AFVRPKKLLVLDEPEQRLDQEgidWLGKRLR--HEKEHNGLAIIMASHEPSLVEAVGARIVRIGGGLEETQslAEPEQL 226
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPE---LVGEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE--GAPEQL 239
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-203 |
2.67e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 85.86 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 18 GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAK--DTEiSFRRNVATVIDDLDFFPDl 95
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRE-TFGKHIGYLPQDVELFPG- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 96 SVVEHLdllARAHGLEDTDELVDS-----ILEEVQLVPQS-----GQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:TIGR01842 407 TVAENI---ARFGENADPEKIIEAaklagVHELILRLPDGydtviGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190
....*....|....*....|....*....|....*...
gi 1391525485 166 RLDQEGIDWLGKRLRHEKEHNGLAIImASHEPSLVEAV 203
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKARGITVVV-ITHRPSLLGCV 520
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
38-213 |
3.81e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 38 LTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEISF-RRNVATVIDDLDFFPDLSVVEH--LDLLARAHGLE 111
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHditRLKNREVPFlRRQIGMIFQDHHLLMDRTVYDNvaIPLIIAGASGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 112 DTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQ---EGIdwlgKRLRHEKEHNGL 188
Cdd:PRK10908 113 DIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDalsEGI----LRLFEEFNRVGV 188
|
170 180
....*....|....*....|....*
gi 1391525485 189 AIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK10908 189 TVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-168 |
5.94e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG---EKAKDTEISfrRNVAT 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvEALSARAAS--RRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDD--LDF-FPDLSVVE-----HLDLLARAHglEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:PRK09536 82 VPQDtsLSFeFDVRQVVEmgrtpHRSRFDTWT--ETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170
....*....|..
gi 1391525485 157 LLVLDEPEQRLD 168
Cdd:PRK09536 160 VLLLDEPTASLD 171
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-213 |
6.88e-19 |
|
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: 81.71 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHT-------VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE-------K 70
Cdd:COG4778 2 TTLLEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 71 AKDTEI-SFRRN--------------VATviddldffpdLSVVEHLdLLARAHGLEDTDELVDSILEEVQLVPQSGQL-P 134
Cdd:COG4778 82 ASPREIlALRRRtigyvsqflrviprVSA----------LDVVAEP-LLERGVDREEARARARELLARLNLPERLWDLpP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 135 GTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEG----IDwlgkrLRHEKEHNGLAIIMASHEPSLVEAVGARIVRI 210
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVE-----LIEEAKARGTAIIGIFHDEEVREAVADRVVDV 225
|
...
gi 1391525485 211 GGG 213
Cdd:COG4778 226 TPF 228
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-195 |
7.24e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 81.94 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFR--RNVAT 84
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERarLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVEHLD-LLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLD 161
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMaVLEIRKDLdrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190
....*....|....*....|....*....|....
gi 1391525485 162 EPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASH 195
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDH 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-163 |
1.13e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.23 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEkakdtEIS----FRR-- 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE-----DIThlpmHKRar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 -------NVATViddldfFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRL----AL 147
Cdd:COG1137 78 lgigylpQEASI------FRKLTVEDNILAVLELRKLskKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVeiarAL 151
|
170
....*....|....*.
gi 1391525485 148 ATafvRPKKLLvLDEP 163
Cdd:COG1137 152 AT---NPKFIL-LDEP 163
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
8-207 |
1.39e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.17 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYgDHTVIdHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVID 87
Cdd:PRK10771 2 LKLTDITWLY-HHLPM-RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLlarahGL-------EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:PRK10771 79 ENNLFSHLTVAQNIGL-----GLnpglklnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 161 DEPEQRLDQEgidwlgkrLRHEK--------EHNGLAIIMASHepSLVEAvgARI 207
Cdd:PRK10771 154 DEPFSALDPA--------LRQEMltlvsqvcQERQLTLLMVSH--SLEDA--ARI 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-213 |
1.48e-18 |
|
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: 80.84 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 15 KKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVI-DDLDFFP 93
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 94 DLSVVEHLDLLARAHGLEDTD--ELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD--- 168
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPARfkKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvva 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1391525485 169 QEGIDwlgKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:cd03267 189 QENIR---NFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
7-213 |
3.53e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.89 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHT-VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK---AKDTEISFRRNV 82
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVI---DDLDFFPdlSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKL 157
Cdd:PRK13639 81 GIVFqnpDDQLFAP--TVEEDVAFGPLNLGLskEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 158 LVLDEPEQRLDQEGIDWLgKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQI-MKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDG 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-168 |
5.93e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.23 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 10 ISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVIDDL 89
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 90 DFFPDLSVVEHLDL---LARAhGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQR 166
Cdd:PRK11000 85 ALYPHLSVAENMSFglkLAGA-KKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
..
gi 1391525485 167 LD 168
Cdd:PRK11000 164 LD 165
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-218 |
7.22e-18 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 79.01 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKYGDH----TVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEkakdtEIS-- 77
Cdd:COG4181 5 SAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ-----DLFal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 78 -------FR-RNVATVIDDLDFFPDLSVVE----------HLDLLARAHGLedtdelvdsiLEEVQLVPQSGQLPGTLSS 139
Cdd:COG4181 80 dedararLRaRHVGFVFQSFQLLPTLTALEnvmlplelagRRDARARARAL----------LERVGLGHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 140 GQRRRLALATAFVRPKKLLVLDEPEQRLDQE-G---IDWLgKRLRHEkehNGLAIIMASHEPSLVEAVGaRIVRIGGG-L 214
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAAtGeqiIDLL-FELNRE---RGTTLVLVTHDPALAARCD-RVLRLRAGrL 224
|
....
gi 1391525485 215 EETQ 218
Cdd:COG4181 225 VEDT 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-226 |
2.64e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.52 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHT--VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRN 81
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 V-------------ATVIDDLDFFPDLSVVEHLDLLARahgledtdelVDSILEEVQLVPQSGQLPGTLSSGQRRRLALA 148
Cdd:PRK13635 83 VgmvfqnpdnqfvgATVQDDVAFGLENIGVPREEMVER----------VDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 149 TAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEpsLVEAVGA-RIVRIGGGleETQSLAEPEQL 226
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHD--LDEAAQAdRVIVMNKG--EILEEGTPEEI 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-200 |
3.08e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.35 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 3 RRSTVLKISNLVKKYGDHT-VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIeVLGEKAKDTE----IS 77
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSrkglMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 78 FRRNVATVIDDLD--FFpDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVR 153
Cdd:PRK13636 80 LRESVGMVFQDPDnqLF-SASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391525485 154 PKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLV 200
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIV 205
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
34-203 |
5.11e-17 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 79.02 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 34 DAVALTGRNGSGKSTVLRCIVGSDKPTEGTI------------EVLGEK----AKDTEI---SFRRNVATviddldfFPD 94
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdrEELGRHigylPQDVELfdgTIAENIAR-------FGD 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 95 LS---VVEHLDLlARAHGLedtdelvdsILeevqlvpqsgQLP-----------GTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:COG4618 432 ADpekVVAAAKL-AGVHEM---------IL----------RLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391525485 161 DEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAV 203
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAAV 533
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-213 |
5.43e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.78 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHT-----VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTI-----EVLGEKAKDTEIs 77
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvDITDKKVKLSDI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 78 fRRNVA-------------TVIDDLDFFPdlsvvehldllaRAHGLEDtDELVDSILEEVQLVPQS-----GQLPGTLSS 139
Cdd:PRK13637 82 -RKKVGlvfqypeyqlfeeTIEKDIAFGP------------INLGLSE-EEIENRVKRAMNIVGLDyedykDKSPFELSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 140 GQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-170 |
6.52e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEV------LGEKAKDTEI-SFRR 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdFSKTPSDKAIrELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NVATVIDDLDFFPDLSVVEHL-DLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKL 157
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLiEAPCRVLGLskDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170
....*....|...
gi 1391525485 158 LVLDEPEQRLDQE 170
Cdd:PRK11124 163 LLFDEPTAALDPE 175
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-191 |
7.42e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.73 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDT---EISFRRNV 82
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWspaELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ----ATviddLDF-FPDLSVVEhLDLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVR---- 153
Cdd:PRK13548 81 lpqhSS----LSFpFTVEEVVA-MGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391525485 154 --PKKLLVLDEPEQRLD---QEGIDWLGKRLRHEkehNGLAII 191
Cdd:PRK13548 156 dgPPRWLLLDEPTSALDlahQHHVLRLARQLAHE---RGLAVI 195
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
8-205 |
1.05e-16 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 76.18 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVID 87
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:TIGR03864 82 QPTLDLDLSVRQNLRYHAALHGLsrAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPTV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1391525485 166 RLDQEGIDWLGKRLRHEKEHNGLAIIMASHepsLVEAVGA 205
Cdd:TIGR03864 162 GLDPASRAAITAHVRALARDQGLSVLWATH---LVDEIEA 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-213 |
1.30e-16 |
|
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: 77.94 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLR--CIVGSDKPTEGTIEVLGEKAK-----DTEisfR 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKasnirDTE---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDDLDFFPDLSVVEHLDL---LARAHGLEDTDELV---DSILEEVQLVPQSGQLP-GTLSSGQRRRLALATAFV 152
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLgneITLPGGRMAYNAMYlraKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 153 RPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-197 |
1.97e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.40 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 18 GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS-FRRNVATVIDDLDFFpDLS 96
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDeVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 97 VVEHLdLLARAhglEDTDELVDSILEEVQLVPQSGQLPG-----------TLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:TIGR02868 425 VRENL-RLARP---DATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|..
gi 1391525485 166 RLDQEGIDWLGKRLRHEKEhnGLAIIMASHEP 197
Cdd:TIGR02868 501 HLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-198 |
2.31e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 12 NLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCI-----VGSDKPTEGTIEVLGEKAKDTE---ISFRRNVA 83
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDvdpIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 TVIDDLDFFPDLSVVEHLDLLARAHGL----EDTDELVDSILEEVQLVPQS----GQLPGTLSSGQRRRLALATAFVRPK 155
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGLvkskKELDERVEWALKKAALWDEVkdrlNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391525485 156 KLLVLDEPEQRLDQEGIDWLGKRLRHEKEHngLAIIMASHEPS 198
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPA 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-212 |
2.52e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.50 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 25 HFNLQVYEsdAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfrRNVATVIDDLDFFPDLSVVEHLDLL 104
Cdd:PRK13543 31 DFHVDAGE--ALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--RFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 105 ARAHGLEdTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDwLGKRLRHEKE 184
Cdd:PRK13543 107 CGLHGRR-AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT-LVNRMISAHL 184
|
170 180
....*....|....*....|....*...
gi 1391525485 185 HNGLAIIMASHEPSLVEAVGARIVRIGG 212
Cdd:PRK13543 185 RGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-208 |
3.62e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 75.91 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 37 ALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISF-----RRNVATVIDDLDFFPDLSVVEHLDL-LARAHGL 110
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflpphRRRIGYVFQEARLFPHLSVRGNLLYgRKRAPRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 111 EDTDELvDSILEEVQLVPQSGQLPGTLSSGQRRRLALATA-FVRPkKLLVLDEPEQRLD----QEGIDWLgKRLRHEKeh 185
Cdd:COG4148 109 ERRISF-DEVVELLGIGHLLDRRPATLSGGERQRVAIGRAlLSSP-RLLLMDEPLAALDlarkAEILPYL-ERLRDEL-- 183
|
170 180
....*....|....*....|...
gi 1391525485 186 nGLAIIMASHEPSLVEAVGARIV 208
Cdd:COG4148 184 -DIPILYVSHSLDEVARLADHVV 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-208 |
4.79e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.53 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlgekAKDTEISfR------RN 81
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY----EQDLIVA-RlqqdppRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VA-TVID-----------DLDFFPDLSVV-------EHLDLLARA------HGLEDTDELVDSILEEVQLVPQSgQLpGT 136
Cdd:PRK11147 79 VEgTVYDfvaegieeqaeYLKRYHDISHLvetdpseKNLNELAKLqeqldhHNLWQLENRINEVLAQLGLDPDA-AL-SS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 137 LSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLrheKEHNGlAIIMASHEPSLVEAVGARIV 208
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL---KTFQG-SIIFISHDRSFIRNMATRIV 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-213 |
7.41e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG---SDKPTEGTIEVLGEK-------AKDTE 75
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTvqregrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 76 ISfRRNVATVIDDLDFFPDLSVVEHLDLLA-----------RAHGLEDTDELVDSiLEEVQLVPQSGQLPGTLSSGQRRR 144
Cdd:PRK09984 83 KS-RANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfSWFTREQKQRALQA-LTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 145 LALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-216 |
8.39e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.27 E-value: 8.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYG--DH--TVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFR--- 79
Cdd:PRK10584 6 IVEVHHLKKSVGqgEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 --RNVATVIDDLDFFPDLSVVEHLDLLARAHGLEDTDELVDSI--LEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPK 155
Cdd:PRK10584 86 raKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 156 KLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGGLEE 216
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-213 |
9.52e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGD------HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFR- 79
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RN-------------VATVI-DDLDFFPdlsvvEHLDLLArahglEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRL 145
Cdd:PRK13633 84 RNkagmvfqnpdnqiVATIVeEDVAFGP-----ENLGIPP-----EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 146 ALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHepSLVEAVGA-RIVRIGGG 213
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH--YMEEAVEAdRIIVMDSG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
37-205 |
1.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.63 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 37 ALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS-FRRNVATVIDDldffPDLSVVEHLDLLARAHGLE---- 111
Cdd:PRK13648 39 SIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVFQN----PDNQFVGSIVKYDVAFGLEnhav 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 112 ---DTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGL 188
Cdd:PRK13648 115 pydEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNI 194
|
170
....*....|....*..
gi 1391525485 189 AIIMASHEpsLVEAVGA 205
Cdd:PRK13648 195 TIISITHD--LSEAMEA 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-208 |
1.13e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 74.32 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKY----GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKP---TEGTIEVLGE---KAKDTEI 76
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdllKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 77 -SFR-RNVATVIDD----LDffPDLSVVEHLDLLARAHGL---EDTDELVDSILEEVQLVPQSGQL---PGTLSSGQRRR 144
Cdd:COG0444 81 rKIRgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGlskAEARERAIELLERVGLPDPERRLdryPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 145 LALATAFV-RPkKLLVLDEPEQRLD---QEGIDWLGKRLRHEKehnGLAIIMASHEPSLVEAVGARIV 208
Cdd:COG0444 159 VMIARALAlEP-KLLIADEPTTALDvtiQAQILNLLKDLQREL---GLAILFITHDLGVVAEIADRVA 222
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-212 |
1.30e-15 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 72.96 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 28 LQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTeisfRRNVATVIDDLDFFPDLSV-VEHLDLLAR 106
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG----WRHIGYVPQRHEFAWDFPIsVAHTVMSGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 107 AHGL-------EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKrL 179
Cdd:TIGR03771 77 TGHIgwlrrpcVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE-L 155
|
170 180 190
....*....|....*....|....*....|....*
gi 1391525485 180 RHEKEHNGLAIIMASHEpsLVEAVGA--RIVRIGG 212
Cdd:TIGR03771 156 FIELAGAGTAILMTTHD--LAQAMATcdRVVLLNG 188
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-182 |
1.56e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.35 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE-----KAKDTEISFR-RN 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlHARDRKVGFVfQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VA-----TVIDDLDFfpDLSVVEHLDLLARAhgleDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:PRK10851 83 YAlfrhmTVFDNIAF--GLTVLPRRERPNAA----AIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190
....*....|....*....|....*....|
gi 1391525485 157 LLVLDEPEQRLD----QEGIDWLgkRLRHE 182
Cdd:PRK10851 157 ILLLDEPFGALDaqvrKELRRWL--RQLHE 184
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-203 |
3.22e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK---AKDTEISFRRNVA 83
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldySKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 TVIDDLD---FFPDLSvvEHLDLLARAHGLEDtDELVDSILEEVQLVPQSG---QLPGTLSSGQRRRLALATAFVRPKKL 157
Cdd:PRK13638 81 TVFQDPEqqiFYTDID--SDIAFSLRNLGVPE-AEITRRVDEALTLVDAQHfrhQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391525485 158 LVLDEPEQRLDQEG---IDWLGKRLRHEKEHnglaIIMASHEPSLVEAV 203
Cdd:PRK13638 158 LLLDEPTAGLDPAGrtqMIAIIRRIVAQGNH----VIISSHDIDLIYEI 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-171 |
3.88e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.33 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKYGDHT--VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISF-RR 80
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEiRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NV-------------ATVIDDLDFfpdlsvvehldllarahGLE----DTDELVDSILEEVQLVPQSGQL---PGTLSSG 140
Cdd:PRK13632 84 KIgiifqnpdnqfigATVEDDIAF-----------------GLEnkkvPPKKMKDIIDDLAKKVGMEDYLdkePQNLSGG 146
|
170 180 190
....*....|....*....|....*....|.
gi 1391525485 141 QRRRLALATAFVRPKKLLVLDEPEQRLDQEG 171
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKG 177
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-170 |
5.99e-15 |
|
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: 71.10 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 9 KISNLVKKY-GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISFRRNVATVI 86
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDlSVVEHLDLlaraHGLEDTDELVDSILEEVQLVPQSGQLP-----------GTLSSGQRRRLALATAFVRPK 155
Cdd:cd03254 84 QDTFLFSG-TIMENIRL----GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDP 158
|
170
....*....|....*
gi 1391525485 156 KLLVLDEPEQRLDQE 170
Cdd:cd03254 159 KILILDEATSNIDTE 173
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-163 |
1.02e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.46 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 12 NLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVIDDLDF 91
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSL 350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 92 FPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFV-RPkKLLVLDEP 163
Cdd:NF033858 351 YGELTVRQNLELHARLFHLpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIhKP-ELLILDEP 424
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-213 |
1.02e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 10 ISNLVK-KYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVidd 88
Cdd:COG4586 24 LKGLFRrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVV--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 89 ldF------FPDLSVVEHLDLLARAHGLEDT------DELVDsILEevqLVPQSGQLPGTLSSGQRRRLALATAFV-RPk 155
Cdd:COG4586 101 --FgqrsqlWWDLPAIDSFRLLKAIYRIPDAeykkrlDELVE-LLD---LGELLDTPVRQLSLGQRMRCELAAALLhRP- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391525485 156 KLLVLDEPEQRLD---QEGIdwlgkR--LRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:COG4586 174 KILFLDEPTIGLDvvsKEAI-----RefLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-211 |
1.32e-14 |
|
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: 72.14 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKY-----GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEV-LGEKAKD-TEISF- 78
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDmTKPGPd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 79 -----RRNVATVIDDLDFFPDLSVvehLDLLARAHGLEDTDE---------LVDSILEEVQLVPQSGQLPGTLSSGQRRR 144
Cdd:TIGR03269 359 grgraKRYIGILHQEYDLYPHRTV---LDNLTEAIGLELPDElarmkavitLKMVGFDEEKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 145 LALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAV--------GARIVRIG 211
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVcdraalmrDGKIVKIG 510
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-208 |
1.56e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 15 KKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDkPTEGTIEVLGE---KAKDTEI-SFRRNVATVIDD-- 88
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQdldGLSRRALrPLRRRMQVVFQDpf 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 89 --LDffPDLSV----VEHLDLLARAHGLEDTDELVDSILEEVQLVPQSGQ-LPGTLSSGQRRRLALATAFV-RPkKLLVL 160
Cdd:COG4172 373 gsLS--PRMTVgqiiAEGLRVHGPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALIlEP-KLLVL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 161 DEPEQRLD---QEGIDWLGKRLRheKEHnGLAIIMASHEPSLVEAVGARIV 208
Cdd:COG4172 450 DEPTSALDvsvQAQILDLLRDLQ--REH-GLAYLFISHDLAVVRALAHRVM 497
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-170 |
1.61e-14 |
|
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: 69.95 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHT--VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVAT 84
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDlSVVEHLdllarAHGLED-TDELVDSILEEVQL------VPQS-----GQLPGTLSSGQRRRLALATAFV 152
Cdd:cd03251 81 VSQDVFLFND-TVAENI-----AYGRPGaTREEVEEAARAANAhefimeLPEGydtviGERGVKLSGGQRQRIAIARALL 154
|
170
....*....|....*...
gi 1391525485 153 RPKKLLVLDEPEQRLDQE 170
Cdd:cd03251 155 KDPPILILDEATSALDTE 172
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-195 |
1.62e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCI-----VGSDKPTEGTIEVLGEKAKDTE 75
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 76 IS---FRRNVATVIDDLDFFPdLSVVEHLdllarAHGLE--------DTDELVDSILEEVQLVPQ-SGQLPGT---LSSG 140
Cdd:PRK14258 81 VNlnrLRRQVSMVHPKPNLFP-MSVYDNV-----AYGVKivgwrpklEIDDIVESALKDADLWDEiKHKIHKSaldLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 141 QRRRLALATAFVRPKKLLVLDEPEQRLDQEG---IDWLGKRLRHEKEhngLAIIMASH 195
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRLRSE---LTMVIVSH 209
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-196 |
1.62e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVI 86
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEH--LDLLARAHGLEdTDELVDSI-LEEVQLVPqsgqlPGTLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:PRK13540 81 HRSGINPYLTLRENclYDIHFSPGAVG-ITELCRLFsLEHLIDYP-----CGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 1391525485 164 EQRLDQEGIDWLGKRLRHEKEHNGlAIIMASHE 196
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGG-AVLLTSHQ 186
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-213 |
1.67e-14 |
|
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: 69.54 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS-FRRNVATVIDDLDFFPDlSV 97
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdLRRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 98 VEHLDLlarAHGLEDTDELVDS-----ILEEVQLVPQSGQLP-----GTLSSGQRRRLALATAFVRPKKLLVLDEPEQRL 167
Cdd:cd03245 95 RDNITL---GAPLADDERILRAaelagVTDFVNKHPNGLDLQigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1391525485 168 DQEGIDWLGKRLRHEKEHNglAIIMASHEPSLVEAVGaRIVRIGGG 213
Cdd:cd03245 172 DMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVD-RIIVMDSG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-168 |
1.81e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.04 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISFRRNVAt 84
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 viddldFFP-------DLSVVE--------HLDLLARahgLEDTDE-LVDSILEEVQLVPQSGQLPGTLSSGQRRRLALA 148
Cdd:PRK11231 80 ------LLPqhhltpeGITVRElvaygrspWLSLWGR---LSAEDNaRVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180
....*....|....*....|
gi 1391525485 149 TAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLD 170
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-207 |
2.08e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAK--DTEISFRRNVATV 85
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDLSVVEHL----DLLARAHGLEDTD-----ELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:PRK09700 86 YQELSVIDELTVLENLyigrHLTKKVCGVNIIDwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 157 LLVLDEPEQRLDQEGIDWL---GKRLRHEkehnGLAIIMASHEPSLVEAVGARI 207
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLfliMNQLRKE----GTAIVYISHKLAEIRRICDRY 215
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-170 |
2.32e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlGEKakdTEIS-FRRNVAtv 85
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTK---LEVAyFDQHRA-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 idDLDffPDLSVVEHLdllarAHGLEDT-----DELVDSILEEVQLVPQSGQLP-GTLSSGQRRRLALATAFVRPKKLLV 159
Cdd:PRK11147 393 --ELD--PEKTVMDNL-----AEGKQEVmvngrPRHVLGYLQDFLFHPKRAMTPvKALSGGERNRLLLARLFLKPSNLLI 463
|
170
....*....|.
gi 1391525485 160 LDEPEQRLDQE 170
Cdd:PRK11147 464 LDEPTNDLDVE 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-213 |
3.48e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.73 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLR--CIVGSDKPTEGTIEVLGEK-----AKDTEisfR 79
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlSGVYPHGTYEGEIIFEGEElqasnIRDTE---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDDLDFFPDLSVVEHLDLLA--RAHGLEDTDELV---DSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRP 154
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNeiTPGGIMDYDAMYlraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 155 KKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-202 |
4.52e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 10 ISNLVKKY-GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK-AKDTEISFRRNVATVID 87
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlSSLSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDlSVVEHLDLlarahGLEDTDELVDSILEEVQLVPQSGQLPG-----------TLSSGQRRRLALATAFVRPKK 156
Cdd:PRK10790 423 DPVVLAD-TFLANVTL-----GRDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391525485 157 LLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIImaSHEPS-LVEA 202
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVI--AHRLStIVEA 541
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-170 |
4.91e-14 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 70.52 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYG--DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVAT 84
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLaSLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPD-------------LSVVEHLDLLARAHGLEDTDELVDSILEEVqlvpqsGQLPGTLSSGQRRRLALATAF 151
Cdd:TIGR02203 411 VSQDVVLFNDtianniaygrteqADRAEIERALAAAYAQDFVDKLPLGLDTPI------GENGVLLSGGQRQRLAIARAL 484
|
170
....*....|....*....
gi 1391525485 152 VRPKKLLVLDEPEQRLDQE 170
Cdd:TIGR02203 485 LKDAPILILDEATSALDNE 503
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-196 |
6.10e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 69.72 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKY----GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEI-SFR 79
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdltALSERELrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATViddldFfpdlsvvEHLDLLAR-------AHGLE-------DTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRL 145
Cdd:COG1135 82 RKIGMI-----F-------QHFNLLSSrtvaenvALPLEiagvpkaEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 146 ----ALATafvRPkKLLVLDEPEQRLDQE---GIDWLGKRLRHEKehnGLAIIMASHE 196
Cdd:COG1135 150 giarALAN---NP-KVLLCDEATSALDPEttrSILDLLKDINREL---GLTIVLITHE 200
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-168 |
6.29e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.04 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRC-------IVGSDkpTEGTIEVLGEKAKD 73
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFR--VEGKVTFHGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 74 TEI---SFRRNVATVIDDLDFFPDlSVVEHLDLLARAHGLE-DTDELVDSILEEVQL-------VPQSGQlpgTLSSGQR 142
Cdd:PRK14243 82 PDVdpvEVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgDMDELVERSLRQAALwdevkdkLKQSGL---SLSGGQQ 157
|
170 180
....*....|....*....|....*.
gi 1391525485 143 RRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-213 |
7.07e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.40 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCI-----VGSDKPTEGTIEVLGEKA-KDTEISFR 79
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIfKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDDLDFFPDLSVVEHLDL---LAR-AHGLEDTDELVDSILEEVQL---VPQSGQLP-GTLSSGQRRRLALATAF 151
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALglkLNRlVKSKKELQERVRWALEKAQLwdeVKDRLDAPaGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 152 VRPKKLLVLDEPEQRLDQEG---IDWLGKRLRHEkehngLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENtakIESLFLELKKD-----MTIVLVTHFPQQAARISDYVAFLYKG 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-207 |
7.51e-14 |
|
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: 70.43 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKYGDHT--VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEkakdteiSFRRN 81
Cdd:TIGR01257 1934 KTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK-------SILTN 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VATVIDDLDFFPDLSVV-------EHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFV 152
Cdd:TIGR01257 2007 ISDVHQNMGYCPQFDAIddlltgrEHLYLYARLRGVpaEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 153 RPKKLLVLDEPEQRLDQEGIDWLGKR----LRHEKehnglAIIMASHEPSLVEAVGARI 207
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTivsiIREGR-----AVVLTSHSMEECEALCTRL 2140
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-170 |
8.09e-14 |
|
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: 69.96 E-value: 8.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlGEKAKdteISFrrnVATVI 86
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK---LAY---VDQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDffPDLSVVEH----LDLL--------ARAH----GLEDTDElvdsileevqlvpqsGQLPGTLSSGQRRRLALATA 150
Cdd:TIGR03719 395 DALD--PNKTVWEEisggLDIIklgkreipSRAYvgrfNFKGSDQ---------------QKKVGQLSGGERNRVHLAKT 457
|
170 180
....*....|....*....|
gi 1391525485 151 FVRPKKLLVLDEPEQRLDQE 170
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVE 477
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-226 |
1.02e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.60 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYG---DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRR 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NV-------------ATVIDDLDFFPDLSVVEHLDLLARahgledtdelVDSILEEVQLVPQSGQLPGTLSSGQRRRLAL 147
Cdd:PRK13650 82 KIgmvfqnpdnqfvgATVEDDVAFGLENKGIPHEEMKER----------VNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 148 ATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVeAVGARIVRIGGGleETQSLAEPEQL 226
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNG--QVESTSTPREL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-205 |
1.26e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.29 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 22 VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG---SDKPTEGTIEVLGEK-AKDTEISFRRNV-------------AT 84
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITlTAKTVWDIREKVgivfqnpdnqfvgAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFfpdlsvvehlDLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:PRK13640 102 VGDDVAF----------GLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391525485 165 QRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEpsLVEAVGA 205
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHD--IDEANMA 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
7-200 |
1.39e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.91 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKY-GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVAT 84
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VI---DDLDFFPdlSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLV 159
Cdd:PRK13652 83 VFqnpDDQIFSP--TVEQDIAFGPINLGLdeETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391525485 160 LDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLV 200
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLV 201
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-162 |
1.79e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.42 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTV-----IDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEISfr 79
Cdd:COG1101 2 LELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtKLPEYKRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDD--LDFFPDLSVVEHLDL---------LARAHGLEDTDELVDSI------LEEvQLvpqsGQLPGTLSSGQR 142
Cdd:COG1101 80 KYIGRVFQDpmMGTAPSMTIEENLALayrrgkrrgLRRGLTKKRRELFRELLatlglgLEN-RL----DTKVGLLSGGQR 154
|
170 180
....*....|....*....|
gi 1391525485 143 RRLALATAFVRPKKLLVLDE 162
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDE 174
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-204 |
2.03e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.38 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRC------IVGSDKPTEGTIEVLGEKAKDTE-ISFR 79
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDaIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDDLDFFPDLSVVEHLDLLARAHGLEDTDEL---VDSILEEVQL---VPQSGQLPGT-LSSGQRRRLALATAFV 152
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIkkiVEECLRKVGLwkeVYDRLNSPASqLSGGQQQRLTIARALA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 153 RPKKLLVLDEPEQRLD---QEGIDWLGKRLRHEkehngLAIIMASHEPSLVEAVG 204
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDivnSQAIEKLITELKNE-----IAIVIVSHNPQQVARVA 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-168 |
2.50e-13 |
|
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: 65.80 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYG--DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATV 85
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDldffpdlsvvehldllaRAHgLEDTdelvdSILEEVqlvpqsgqlpGT-LSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:cd03247 80 LNQ-----------------RPY-LFDT-----TLRNNL----------GRrFSGGERQRLALARILLQDAPIVLLDEPT 126
|
....
gi 1391525485 165 QRLD 168
Cdd:cd03247 127 VGLD 130
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-196 |
2.60e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFN---LQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNV 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDDLDF-FPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLV 159
Cdd:PRK13642 84 GMVFQNPDNqFVGATVEDDVAFGMENQGIprEEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1391525485 160 LDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHE 196
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-202 |
2.97e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 20 HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG--SDKPTEGTIEVLgekakdtEISFRRNVaTVIDDLDffPDLSV 97
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVP-------DNQFGREA-SLIDAIG--RKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 98 VEHLDLLARAhGLEDtdelvdsileeVQLVPQSgqlPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGK 177
Cdd:COG2401 113 KDAVELLNAV-GLSD-----------AVLWLRR---FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|....*
gi 1391525485 178 RLRHEKEHNGLAIIMASHEPSLVEA 202
Cdd:COG2401 178 NLQKLARRAGITLVVATHHYDVIDD 202
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-213 |
3.06e-13 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 68.35 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISF-RRNVATVIDDLDFFPDlSV 97
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADlRRNIGYVPQDPRLFYG-TL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 98 VEHLDLLARAhgLEDTDEL----VDSILEEVQLVPQSGQLP-----GTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:TIGR03375 556 RDNIALGAPY--ADDEEILraaeLAGVTEFVRRHPDGLDMQigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMD 633
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1391525485 169 QEGIDWLGKRLRHEKEHNGLaiIMASHEPSLVEAVGaRIVRIGGG 213
Cdd:TIGR03375 634 NRSEERFKDRLKRWLAGKTL--VLVTHRTSLLDLVD-RIIVMDNG 675
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-199 |
3.56e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.38 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGD---HT-VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGtiEVLGEKAKDTEISFRR 80
Cdd:PRK11629 3 KILLQCDNLCKRYQEgsvQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG--DVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NVATVIDDLDF-------FPDLSVVEH--LDLLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAF 151
Cdd:PRK11629 81 KAELRNQKLGFiyqfhhlLPDFTALENvaMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391525485 152 VRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSL 199
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-170 |
3.61e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.93 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGD--HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISFRRNVAT 84
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDlSVVEHLdLLARAHGledTDELVDSILEEV---QLVPQS-------GQLPGTLSSGQRRRLALATAFVRP 154
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNL-LLAAPNA---SDEALIEVLQQVgleKLLEDDkglnawlGEGGRQLSGGEQRRLGIARALLHD 493
|
170
....*....|....*.
gi 1391525485 155 KKLLVLDEPEQRLDQE 170
Cdd:PRK11160 494 APLLLLDEPTEGLDAE 509
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-211 |
4.10e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 67.06 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARRSTVLKISNLVKKY---------GDHTV--IDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE 69
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 70 ---KAKDTEI-SFRRNVATVIDD----LDffPDLSVvehLDLLA---RAHGLEDTDEL---VDSILEEVQLVP-QSGQLP 134
Cdd:COG4608 81 ditGLSGRELrPLRRRMQMVFQDpyasLN--PRMTV---GDIIAeplRIHGLASKAERrerVAELLELVGLRPeHADRYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 135 GTLSSGQRRRLALATAF-VRPKkLLVLDEPEQRLD---QEGIDWLGKRLRHEKehnGLAIIMASHEPSLVE------AV- 203
Cdd:COG4608 156 HEFSGGQRQRIGIARALaLNPK-LIVCDEPVSALDvsiQAQVLNLLEDLQDEL---GLTYLFISHDLSVVRhisdrvAVm 231
|
250
....*....|
gi 1391525485 204 --GaRIVRIG 211
Cdd:COG4608 232 ylG-KIVEIA 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-197 |
4.67e-13 |
|
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: 65.76 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 22 VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG---SDKPTEGTIEVLGEKAKDTEisFRRNVATVIDDLDFFPDLSVV 98
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 99 EHLDLLARAHGLEDTDELVDSILEEVQLVPQ------SGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGI 172
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKRVEDVLLRDlaltriGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTA 179
|
170 180
....*....|....*....|....*
gi 1391525485 173 DWLGKRLRHEKEHNGLaIIMASHEP 197
Cdd:cd03234 180 LNLVSTLSQLARRNRI-VILTIHQP 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-195 |
4.74e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlgekaKDTEISF-------R 79
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII-----DDEDISLlplharaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDDLDFFPDLSVVEHL-DLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNLmAVLQIRDDLsaEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391525485 157 LLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASH 195
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDH 195
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-207 |
4.89e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 23 IDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG------------EKAKDTEISF---------RRN 81
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdllgmkddewrAVRSDIQMIFqdplaslnpRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VATVIDD--LDFFPDLSVvehldllarahglEDTDELVDSILEEVQLVPQS-GQLPGTLSSGQRRRLALATAFVRPKKLL 158
Cdd:PRK15079 117 IGEIIAEplRTYHPKLSR-------------QEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 159 VLDEPEQRLD---QEGIDWLGKRLRHEKehnGLAIIMASHEPSLVEAVGARI 207
Cdd:PRK15079 184 ICDEPVSALDvsiQAQVVNLLQQLQREM---GLSLIFIAHDLAVVKHISDRV 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-163 |
6.52e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.83 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCI------VGSDKpTEGTIEVLGEK--AKDTE-I 76
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlIPGAR-VEGEILLDGEDiyDPDVDvV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 77 SFRRNVATViddldF-----FPdLSVVEHLDLLARAHGL---EDTDELVDSIL------EEV--QLvpqsgQLPGT-LSS 139
Cdd:COG1117 89 ELRRRVGMV-----FqkpnpFP-KSIYDNVAYGLRLHGIkskSELDEIVEESLrkaalwDEVkdRL-----KKSALgLSG 157
|
170 180
....*....|....*....|....*
gi 1391525485 140 GQRRRLALATAF-VRPKKLLvLDEP 163
Cdd:COG1117 158 GQQQRLCIARALaVEPEVLL-MDEP 181
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-207 |
6.80e-13 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 66.13 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 25 HFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTEIS--FRRNVATVIDDLDFFPDLSVVE 99
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiaAMSRKELRelRRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 100 HLdllarAHGLE-------DTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD---- 168
Cdd:cd03294 122 NV-----AFGLEvqgvpraEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplir 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391525485 169 QEGIDWLgkrLRHEKEHnGLAIIMASHEpsLVEAV--GARI 207
Cdd:cd03294 197 REMQDEL---LRLQAEL-QKTIVFITHD--LDEALrlGDRI 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-195 |
7.70e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.20 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 25 HFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEvLGE-------KAKDTEiSFRRNV-------------AT 84
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGErvitagkKNKKLK-PLRKKVgivfqfpehqlfeET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFP-DLSVVEhldllarahglEDTDELVDSILEEVQLVPQ-SGQLPGTLSSGQRRRLALATAFVRPKKLLVLDE 162
Cdd:PRK13634 103 VEKDICFGPmNFGVSE-----------EDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1391525485 163 PEQRLDQEG---IDWLGKRLRHEKehnGLAIIMASH 195
Cdd:PRK13634 172 PTAGLDPKGrkeMMEMFYKLHKEK---GLTTVLVTH 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-210 |
8.28e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIE-----VLGEKAKDTEISFRrnv 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenaNIGYYAQDHAYDFE--- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 atviDDLDFFpdlsvvehlDLLARAHGLEDTDELVDSILeevqlvpqsGQL----------PGTLSSGQRRRLALATAFV 152
Cdd:PRK15064 397 ----NDLTLF---------DWMSQWRQEGDDEQAVRGTL---------GRLlfsqddikksVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 153 RPKKLLVLDEPEQRLDQEGIDWLGKRLrheKEHNGlAIIMASHEPSLVEAVGARIVRI 210
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMAL---EKYEG-TLIFVSHDREFVSSLATRIIEI 508
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-163 |
1.36e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS--FRRNVAT 84
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVEHldlLARAHGLEDTDELVDSILEEVQLVP----QSGQLPGTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:PRK11614 85 VPEGRRVFSRMTVEEN---LAMGGFFAERDQFQERIKWVYELFPrlheRRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
...
gi 1391525485 161 DEP 163
Cdd:PRK11614 162 DEP 164
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-173 |
1.37e-12 |
|
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: 64.87 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS-FRRNVATVIDDLDFFpDLSV 97
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwLRSQIGLVSQEPVLF-DGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 98 VEHLdllarAHGLED-TDELVDS------ILEEVQLVPQS-----GQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:cd03249 94 AENI-----RYGKPDaTDEEVEEaakkanIHDFIMSLPDGydtlvGERGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170
....*....|....*
gi 1391525485 166 RLD-------QEGID 173
Cdd:cd03249 169 ALDaeseklvQEALD 183
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-168 |
1.67e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.80 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCI--VGSDKP---TEGTIEVLGEKA----KDTe 75
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIysprTDT- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 76 ISFRRNVATVIDDLDFFPdLSVVEHLDLLARAHGLEDT---DELVD------SILEEVQLVPQSGQLpgTLSSGQRRRLA 146
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKqvlDEAVEkslkgaSIWDEVKDRLHDSAL--GLSGGQQQRVC 158
|
170 180
....*....|....*....|..
gi 1391525485 147 LATAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALD 180
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-213 |
1.74e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 64.76 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHT-VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG-EKAKDTEISFRRNVAT 84
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrEVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDldffPD-----LSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKL 157
Cdd:PRK13647 84 VFQD----PDdqvfsSTVWDDVAFGPVNMGLdkDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 158 LVLDEPEQRLDQEGIDWLGKRLrHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-195 |
1.91e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 27 NLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK----AKDTEI-SFRRNVATVIDdldfFPDLSVVEHL 101
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstSKNKDIkQIRKKVGLVFQ----FPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 102 DLLARAHGLED----TDELVDSILEEVQLVPQSGQL----PGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGID 173
Cdd:PRK13649 103 VLKDVAFGPQNfgvsQEEAEALAREKLALVGISESLfeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180
....*....|....*....|..
gi 1391525485 174 WLgKRLRHEKEHNGLAIIMASH 195
Cdd:PRK13649 183 EL-MTLFKKLHQSGMTIVLVTH 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-163 |
2.70e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 65.19 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 18 GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVATVIDDLDFFpDLS 96
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLeSLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 97 VVEHLdllarAHGLED-TDELVDSILEEVQLVPQSGQLPG-----------TLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:COG1132 430 IRENI-----RYGRPDaTDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-195 |
3.92e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 37 ALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAK--DTEISFRRNVATVIDDLDFFPDLSVVEHLDL--LARAHGLED 112
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEMTVAENLYLgqLPHKGGIVN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 113 TDELVDSILEEVQ-----LVPQSgQLpGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGK---RLRHEke 184
Cdd:PRK11288 114 RRLLNYEAREQLEhlgvdIDPDT-PL-KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRvirELRAE-- 189
|
170
....*....|.
gi 1391525485 185 hnGLAIIMASH 195
Cdd:PRK11288 190 --GRVILYVSH 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-198 |
4.00e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.68 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 31 YESDAVALTGRNGSGKSTVLRCIVGSDKP---TEGTIEVLGEKAKDTEIsfRRNVATVI-DDLdFFPDLSVVEHLDLLAR 106
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEM--RAISAYVQqDDL-FIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 107 AHGLEDTD-----ELVDSILEEVQLVP-------QSGQLPGtLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDW 174
Cdd:TIGR00955 126 LRMPRRVTkkekrERVDEVLQALGLRKcantrigVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180
....*....|....*....|....
gi 1391525485 175 LGKRLRHEKEhNGLAIIMASHEPS 198
Cdd:TIGR00955 205 VVQVLKGLAQ-KGKTIICTIHQPS 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
27-195 |
8.80e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 27 NLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIE----VLGEKAKDTEIS-FRRNVATVIDdldfFPDLSVVEHL 101
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdiVVSSTSKQKEIKpVRKKVGVVFQ----FPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 102 DLLARAHGLED---TDELVDSI-LEEVQLVPQSGQL----PGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEG-I 172
Cdd:PRK13643 102 VLKDVAFGPQNfgiPKEKAEKIaAEKLEMVGLADEFweksPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArI 181
|
170 180
....*....|....*....|...
gi 1391525485 173 DWLgkRLRHEKEHNGLAIIMASH 195
Cdd:PRK13643 182 EMM--QLFESIHQSGQTVVLVTH 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-196 |
1.08e-11 |
|
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: 63.42 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKY-GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEG--------TIEVLGEKAK-DTEI 76
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpgiKVGYLPQEPQlDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 77 SFRRNV----ATVIDDLDFFPDLSVV-----EHLDLLAR----------AHGLEDTDELVDSILEEVQLvPQSGQLPGTL 137
Cdd:TIGR03719 84 TVRENVeegvAEIKDALDRFNEISAKyaepdADFDKLAAeqaelqeiidAADAWDLDSQLEIAMDALRC-PPWDADVTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 138 SSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGkrlRHEKEHNGlAIIMASHE 196
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLE---RHLQEYPG-TVVAVTHD 217
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-168 |
1.30e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKY-GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISfRRNVATVI 86
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFFPDLSVVEHLdllarAHGL-------EDTDELVD---SILEEVQLVPQSgqlPGTLSSGQRRRLALATAFVRPKK 156
Cdd:PRK11650 83 QNYALYPHMSVRENM-----AYGLkirgmpkAEIEERVAeaaRILELEPLLDRK---PRELSGGQRQRVAMGRAIVREPA 154
|
170
....*....|..
gi 1391525485 157 LLVLDEPEQRLD 168
Cdd:PRK11650 155 VFLFDEPLSNLD 166
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-226 |
1.47e-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: 63.28 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSD--KPTEGTI--------------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 65 --EVLGEKAKDTEISF------------RRNVATVIDDLDFFPDLSVVEH-LDLLARA--HGLEDTDELVDsILEEVQLV 127
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDFwnlsdklrrrirKRIAIMLQRTFALYGDDTVLDNvLEALEEIgyEGKEAVGRAVD-LIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 128 PQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARI 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*....
gi 1391525485 208 VRIGGGleETQSLAEPEQL 226
Cdd:TIGR03269 240 IWLENG--EIKEEGTPDEV 256
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-186 |
1.75e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.66 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 11 SNLVKKYGDhtvidhFNLQV-----YESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAK--------DTEIS 77
Cdd:cd03237 4 PTMKKTLGE------FTLEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 78 FRRNVATVIDDLDFFPDLSvVEHLDLLArahgledtdelVDSILEevQLVPqsgqlpgTLSSGQRRRLALATAFVRPKKL 157
Cdd:cd03237 78 VRDLLSSITKDFYTHPYFK-TEIAKPLQ-----------IEQILD--REVP-------ELSGGELQRVAIAACLSKDADI 136
|
170 180
....*....|....*....|....*....
gi 1391525485 158 LVLDEPEQRLDQEGIDWLGKRLRHEKEHN 186
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-222 |
2.03e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.82 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTE-ISFRRNVATVIDDLDFFPDlSV 97
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhHYLHRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 98 VEHLdllarAHGLEDTDElvdsilEEVQLVPQS-------GQLPGT-----------LSSGQRRRLALATAFVRPKKLLV 159
Cdd:TIGR00958 572 RENI-----AYGLTDTPD------EEIMAAAKAanahdfiMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391525485 160 LDEPEQRLDQEgidwLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGGLEETQSLAE 222
Cdd:TIGR00958 641 LDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-198 |
3.85e-11 |
|
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: 59.97 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 15 KKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG---SDKPTEGTIEVLGEKAKDTEISFRRNVATVIDDLDF 91
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrteGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 92 FPDLSVVEHLDLLARAHGledtDELVDSIleevqlvpqsgqlpgtlSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQE- 170
Cdd:cd03233 95 FPTLTVRETLDFALRCKG----NEFVRGI-----------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSt 153
|
170 180
....*....|....*....|....*...
gi 1391525485 171 GIDWLgKRLRHEKEHNGLAIIMASHEPS 198
Cdd:cd03233 154 ALEIL-KCIRTMADVLKTTTFVSLYQAS 180
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-196 |
4.35e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 10 ISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKA--KDTEISFRRNVATVID 87
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDL--LARAHGLEDTDELVD---SILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDE 162
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLgrYPTKGMFVDQDKMYRdtkAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190
....*....|....*....|....*....|....
gi 1391525485 163 PEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHE 196
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKE-RGCGIVYISHK 193
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-170 |
4.77e-11 |
|
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: 60.58 E-value: 4.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 22 VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG-EKAKDTEISFRRNVATVIDDLDFF-------- 92
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhDLALADPAWLRRQVGVVLQENVLFnrsirdni 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 93 ------PDLSVVEHLDLLARAHG-LEDTDELVDSILeevqlvpqsGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:cd03252 97 aladpgMSMERVIEAAKLAGAHDfISELPEGYDTIV---------GEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
....*
gi 1391525485 166 RLDQE 170
Cdd:cd03252 168 ALDYE 172
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-167 |
5.65e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 2 ARRSTVLKISNLVKKYGDhtvidhFNL-----QVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEV---------- 66
Cdd:PRK13409 335 SERETLVEYPDLTKKLGD------FSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPelkisykpqy 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 67 LGEKAKDTEISFRRNVATVIDDLDFFPDLsvVEHLDLlarahgledtDELVDSILEEvqlvpqsgqlpgtLSSGQRRRLA 146
Cdd:PRK13409 409 IKPDYDGTVEDLLRSITDDLGSSYYKSEI--IKPLQL----------ERLLDKNVKD-------------LSGGELQRVA 463
|
170 180
....*....|....*....|....*..
gi 1391525485 147 LATAFVRPKKLLVLDEP------EQRL 167
Cdd:PRK13409 464 IAACLSRDADLYLLDEPsahldvEQRL 490
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-213 |
6.02e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.28 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKY--GDHT--VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGekakdteisfrR 80
Cdd:PRK10535 2 TALLELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG-----------Q 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NVATVIDD----------------LDFFPDLSVVEHLDLLARAHGLEDTDEL--VDSILEEVQLVPQSGQLPGTLSSGQR 142
Cdd:PRK10535 71 DVATLDADalaqlrrehfgfifqrYHLLSHLTAAQNVEVPAVYAGLERKQRLlrAQELLQRLGLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 143 RRLALATAFVRPKKLLVLDEPEQRLDQ---EGIDWLGKRLRHEkehnGLAIIMASHEPsLVEAVGARIVRIGGG 213
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQLRDR----GHTVIIVTHDP-QVAAQAERVIEIRDG 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-171 |
6.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 23 IDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG-----EKAKDTEISFRRNVATVIDdldfFPDL-- 95
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpETGNKNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 96 ---SVVEHLDLLARAHGLEDtDELVDSILEEVQLVPQSGQL----PGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLSEDLisksPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
...
gi 1391525485 169 QEG 171
Cdd:PRK13641 178 PEG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-208 |
7.72e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.80 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLvkkyGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKdteisfRRNVATV 85
Cdd:COG1129 255 VVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 ID-----------DLDFFPDLSVVE-----HLDLLARaHGLEDT---DELVDSILEEVQLVPQSGQLP-GTLSSGQRRRL 145
Cdd:COG1129 325 IRagiayvpedrkGEGLVLDLSIREnitlaSLDRLSR-GGLLDRrreRALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKV 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 146 ALATAFVRPKKLLVLDEPEQrldqeGIDWLGK----RLRHEKEHNGLAIIMASHEpsLVEAVGA--RIV 208
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTR-----GIDVGAKaeiyRLIRELAAEGKAVIVISSE--LPELLGLsdRIL 465
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-170 |
9.28e-11 |
|
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: 59.43 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDH--TVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEkakdtEIS------FR 79
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV-----DISkiglhdLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDDLDFFPDlSVVEHLDLLARAhgledTDELVDSILEEVQLVPQSGQLPGTL-----------SSGQRRRLALA 148
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNLDPFGEY-----SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180
....*....|....*....|..
gi 1391525485 149 TAFVRPKKLLVLDEPEQRLDQE 170
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPE 173
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
38-162 |
9.38e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 38 LTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVATViddldfFPDLsvveHL--DLLARAHglEDTD 114
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNReAYRQLFSAV------FSDF----HLfdRLLGLDG--EADP 430
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1391525485 115 ELVDSILEEVQL---VP-QSGQLPGT-LSSGQRRRLALATAFVRPKKLLVLDE 162
Cdd:COG4615 431 ARARELLERLELdhkVSvEDGRFSTTdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-196 |
1.03e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.79 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEV----LGEKAKDTEI-SFRRNVATVIDdldfFP 93
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVdditITHKTKDKYIrPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 94 DLSVVEhlDLLARAhgLEDTDELVDSILEEV-----QLVPQSG-------QLPGTLSSGQRRRLALATAFVRPKKLLVLD 161
Cdd:PRK13646 95 ESQLFE--DTVERE--IIFGPKNFKMNLDEVknyahRLLMDLGfsrdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1391525485 162 EPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHE 196
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-195 |
1.10e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKA--KDTEISFRRNVAT 84
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVriRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVEHLDLlarahGLEDTDELV---DSILEEVQLVpqSGQLP---------GTLSSGQRRRLALATAFV 152
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVL-----GLEPTKGGRldrKAARARIREL--SERYGldvdpdakvEDLSVGEQQRVEILKALY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391525485 153 RPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASH 195
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFITH 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-163 |
1.34e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 20 HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKakdTEISFRRNVATVI---DDLDF-FPDL 95
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP---TRQALQKNLVAYVpqsEEVDWsFPVL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 96 --SVVE-----HLDLLARAHglEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:PRK15056 97 veDVVMmgrygHMGWLRRAK--KRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-202 |
1.58e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEvlgekakdTEISFRRNVAT 84
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDLSVVEHLDLLArahGLEDTDELvdSILEEVQ---LVPQSGQlpgTLSSGQRRRLALATAFVRPKKLLVLD 161
Cdd:PRK09544 74 QKLYLDTTLPLTVNRFLRLRP---GTKKEDIL--PALKRVQaghLIDAPMQ---KLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391525485 162 EPEQRLD---QEGIDWLGKRLRHEKehnGLAIIMASHEPSLVEA 202
Cdd:PRK09544 146 EPTQGVDvngQVALYDLIDQLRREL---DCAVLMVSHDLHLVMA 186
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-168 |
1.96e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAK---DTEIS 77
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaSKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 78 frRNVATVIDDLDFFPDLSVVE--------HLDLLARAHglEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALAT 149
Cdd:PRK10253 81 --RRIGLLAQNATTPGDITVQElvargrypHQPLFTRWR--KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAM 156
|
170
....*....|....*....
gi 1391525485 150 AFVRPKKLLVLDEPEQRLD 168
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLD 175
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-202 |
2.04e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 18 GDHTVIDHFNLQVYESDAVALTGRNGSGKST----VLRCIvgsdkPTEGTIEVLGEK----AKDTEISFRRNVATVIDDL 89
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPlhnlNRRQLLPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 90 D--FFPDLSVVEHLDLLARAH----GLEDTDELVDSILEEVQLVPQSGQ-LPGTLSSGQRRRLALATAFVRPKKLLVLDE 162
Cdd:PRK15134 372 NssLNPRLNVLQIIEEGLRVHqptlSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391525485 163 PEQRLD---QEGIDWLGKRLrheKEHNGLAIIMASHEPSLVEA 202
Cdd:PRK15134 452 PTSSLDktvQAQILALLKSL---QQKHQLAYLFISHDLHVVRA 491
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
27-162 |
2.04e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.60 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 27 NLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK-AKDTEISFRRNVATVIDDLDFFpdlsvvehlDLLA 105
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPvTAEQPEDYRKLFSAVFTDFHLF---------DQLL 413
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 106 RAHGLEDTDELVDSILEEVQLVP----QSGQLPGT-LSSGQRRRLALATAFVRPKKLLVLDE 162
Cdd:PRK10522 414 GPEGKPANPALVEKWLERLKMAHklelEDGRISNLkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-170 |
2.19e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlGEKAKdteISFrrnVAT 84
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK---LAY---VDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDffPDLSVVEH----LDLL--------ARAH----GLEDTDElvdsileevqlvpqsGQLPGTLSSGQRRRLALA 148
Cdd:PRK11819 395 SRDALD--PNKTVWEEisggLDIIkvgnreipSRAYvgrfNFKGGDQ---------------QKKVGVLSGGERNRLHLA 457
|
170 180
....*....|....*....|..
gi 1391525485 149 TAFVRPKKLLVLDEPEQRLDQE 170
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-163 |
2.69e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTeiSFRRNVATVI 86
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA--RHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 --------DDLdfFPDLSVVEHLDLLAR--AHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:NF033858 79 aympqglgKNL--YPTLSVFENLDFFGRlfGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
....*..
gi 1391525485 157 LLVLDEP 163
Cdd:NF033858 157 LLILDEP 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
36-168 |
2.84e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 57.56 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVG--SDKPTEGTIEVLGEkaKDTEISFRRNVATVIDDLDFFPDLSVVEHLDLLARAHGledt 113
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGR--PLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLRG---- 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 114 delvdsileevqlvpqsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:cd03213 112 -----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-198 |
3.31e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 9 KISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVIDD 88
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 89 LdFFPDLSVVEHLDL-----LARAHGLEDTDELVDSILEEVQLVPQSGQLPGT-----LSSGQRRRLALATAFVRPKKLL 158
Cdd:PLN03211 150 I-LYPHLTVRETLVFcsllrLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1391525485 159 VLDEPEQRLDQEGIDWLGKRLRhEKEHNGLAIIMASHEPS 198
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLG-SLAQKGKTIVTSMHQPS 267
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
37-226 |
4.10e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.26 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 37 ALTGRNGSGKSTVLRCIVGSDKPTEGTIeVLGEKAKDTEIS--FRRNVATVIDDLDFFPDLSVVEHLDL--------LAR 106
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEI-LLDAQPLESWSSkaFARKVAYLPQQLPAAEGMTVRELVAIgrypwhgaLGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 107 aHGLEDTdELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD---QEGIDWLGKRLRHEK 183
Cdd:PRK10575 120 -FGAADR-EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiahQVDVLALVHRLSQER 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391525485 184 ehnGLAIIMASHEPSLVEAVGARIVRIGGGleETQSLAEPEQL 226
Cdd:PRK10575 198 ---GLTVIAVLHDINMAARYCDYLVALRGG--EMIAQGTPAEL 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-170 |
4.35e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKYGDhtvidhFNL-----QVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEV----------LG 68
Cdd:COG1245 338 EETLVEYPDLTKSYGG------FSLeveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEdlkisykpqyIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 69 EKAKDTEISFRRNVATviddlDFFPDlSVVEHLdlLARAHGLEdtdELVDSILEEvqlvpqsgqlpgtLSSGQRRRLALA 148
Cdd:COG1245 412 PDYDGTVEEFLRSANT-----DDFGS-SYYKTE--IIKPLGLE---KLLDKNVKD-------------LSGGELQRVAIA 467
|
170 180
....*....|....*....|..
gi 1391525485 149 TAFVRPKKLLVLDEPEQRLDQE 170
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLDVE 489
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-213 |
4.49e-10 |
|
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: 57.48 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISF-RRNVATVIDDLDFF----- 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSKVSLVGQEPVLFarslq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 93 -------PDLSVVEHLDLLARAHGLEDTDELVDSILEEVqlvpqsGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:cd03248 106 dniayglQSCSFECVKEAAQKAHAHSFISELASGYDTEV------GEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1391525485 166 RLDQEGIDWLGKRLRHEKEHNGLAIImaSHEPSLVEAvGARIVRIGGG 213
Cdd:cd03248 180 ALDAESEQQVQQALYDWPERRTVLVI--AHRLSTVER-ADQILVLDGG 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-222 |
4.87e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.27 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 9 KISNLVKKY----GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE---KAKDTE-ISFRR 80
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKElRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 81 NVATViddldFfpdlsvvEHLDLLAR-------AHGLE-------DTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLA 146
Cdd:PRK11153 83 QIGMI-----F-------QHFNLLSSrtvfdnvALPLElagtpkaEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 147 LATAFV-RPKKLLVlDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG-LEETQSLAE 222
Cdd:PRK11153 151 IARALAsNPKVLLC-DEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGrLVEQGTVSE 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-199 |
6.56e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlgekAKDTEISF--RRNvatviddldFFPDLS 96
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR----PAGARVLFlpQRP---------YLPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 97 VvehLDLLARAHGLED-TDELVDSILEEVQLvpqsGQLPG----------TLSSGQRRRLALATAFV-RPkKLLVLDEPE 164
Cdd:COG4178 442 L---REALLYPATAEAfSDAELREALEAVGL----GHLAErldeeadwdqVLSLGEQQRLAFARLLLhKP-DWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|....*
gi 1391525485 165 QRLDQEGIDWLGKRLRHEKEhnGLAIIMASHEPSL 199
Cdd:COG4178 514 SALDEENEAALYQLLREELP--GTTVISVGHRSTL 546
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-170 |
7.55e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVATVIDDLDFFPDlSV 97
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLaSLRNQVALVSQNVHLFND-TI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 98 V-------------EHLDLLAR-AHGLEDTDEL---VDSILEEvqlvpqSGQLpgtLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:PRK11176 434 AnniayarteqysrEQIEEAARmAYAMDFINKMdngLDTVIGE------NGVL---LSGGQRQRIAIARALLRDSPILIL 504
|
170
....*....|
gi 1391525485 161 DEPEQRLDQE 170
Cdd:PRK11176 505 DEATSALDTE 514
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-195 |
7.89e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 57.30 E-value: 7.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHT-VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISFRRNVA- 83
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfSKLQGIRKLVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 -------------TVIDDLDFFPDLSVVEHLDLLARahgledtdelVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATA 150
Cdd:PRK13644 81 ivfqnpetqfvgrTVEEDLAFGPENLCLPPIEIRKR----------VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391525485 151 FVRPKKLLVLDEPEQRLDQEGIDWLGKRLR--HEKehnGLAIIMASH 195
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKklHEK---GKTIVYITH 194
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
8-212 |
8.80e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.00 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDK--PTEGTIEVLGEKAKDTEI--------- 76
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPderaragif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 77 -SFRRNVAtviddldfFPDLSVVEHLDLLARAHGLEDTD-----ELVDSILEEVQLVPQ--SGQLPGTLSSGQRRRLALA 148
Cdd:COG0396 81 lAFQYPVE--------IPGVSVSNFLRTALNARRGEELSareflKLLKEKMKELGLDEDflDRYVNEGFSGGEKKRNEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 149 TAFVRPKKLLVLDEPEQRLDqegIDWLG------KRLRheKEHNGLAIImaSHEPSLVEAVGA---------RIVRIGG 212
Cdd:COG0396 153 QMLLLEPKLAILDETDSGLD---IDALRivaegvNKLR--SPDRGILII--THYQRILDYIKPdfvhvlvdgRIVKSGG 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-163 |
1.07e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.08 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 18 GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEK----AKDTEISFRRNVATVIDDLDFFP 93
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipamSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 94 DLSVVEHLDLLARAHgLEDTDELVDSI----LEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:PRK11831 98 DMNVFDNVAYPLREH-TQLPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-196 |
2.00e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.25 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHT-----VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIE------VLGEKAKDTEI 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 77 -------------------SFRRNVATVIDDLDFFPDLSVVEHlDLL--ARAHGL--EDTDELVDSILEEVQLvPQS--G 131
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQFAEYQLFEQTIEK-DIIfgPVSMGVskEEAKKRAAKYIELVGL-DESylQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 132 QLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHE 196
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHD 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
37-200 |
2.30e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 37 ALTGRNGSGKSTVLRCIvgSDKPTEGTIE----VLGEKAKDTeiSFRRNVATVIDDLDFFPDLSVVEHLDLLARAH---- 108
Cdd:TIGR00956 793 ALMGASGAGKTTLLNVL--AERVTTGVITggdrLVNGRPLDS--SFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpks 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 109 -GLEDTDELVDSILEEVQL---------VPQSGqlpgtLSSGQRRRLALATAFV-RPKKLLVLDEPEQRLDQEGIdWLGK 177
Cdd:TIGR00956 869 vSKSEKMEYVEEVIKLLEMesyadavvgVPGEG-----LNVEQRKRLTIGVELVaKPKLLLFLDEPTSGLDSQTA-WSIC 942
|
170 180
....*....|....*....|...
gi 1391525485 178 RLRHEKEHNGLAIIMASHEPSLV 200
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIHQPSAI 965
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-208 |
2.46e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.17 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 23 IDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG-----SDKPTEGTIEVLGEKAKDTEIS-FRRNVATVIDdldfFPDLS 96
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliiseTGQTIVGDYAIPANLKKIKEVKrLRKEIGLVFQ----FPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 97 V----VEHLDLLARAHGLEDTDELVDSILEEVQLV--PQ--SGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK13645 103 LfqetIEKDIAFGPVNLGENKQEAYKKVPELLKLVqlPEdyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391525485 169 QEG-IDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARIV 208
Cdd:PRK13645 183 PKGeEDFINLFERLNKEY-KKRIIMVTHNMDQVLRIADEVI 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-212 |
2.71e-09 |
|
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: 54.84 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG--SDKPTEGTIEVLGEKAKDTEI--------- 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPeerarlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 77 -SFRRNVAtviddldfFPDLSVVEHldllarahgLEDTDElvdsileevqlvpqsgqlpgTLSSGQRRRLALATAFVRPK 155
Cdd:cd03217 81 lAFQYPPE--------IPGVKNADF---------LRYVNE--------------------GFSGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 156 KLLVLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGA---------RIVRIGG 212
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLRE-EGKSVLIITHYQRLLDYIKPdrvhvlydgRIVKSGD 188
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
40-195 |
3.47e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 40 GRNGSGKSTVLRCIVGSDKPTEGTIeVLGEKAK----------DTEISFRRNVatviddldffpDLSVVEHLDLLAR--- 106
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDKEFEGEA-RPAPGIKvgylpqepqlDPEKTVRENV-----------EEGVAEVKAALDRfne 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 107 -----AHGLEDTDEL------------------VDSILE---EVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:PRK11819 108 iyaayAEPDADFDALaaeqgelqeiidaadawdLDSQLEiamDALRCPPWDAKVTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190
....*....|....*....|....*....|....*
gi 1391525485 161 DEPEQRLDQEGIDWLGkrlRHEKEHNGlAIIMASH 195
Cdd:PRK11819 188 DEPTNHLDAESVAWLE---QFLHDYPG-TVVAVTH 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-195 |
4.32e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 54.34 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDH--TVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVAT 84
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLeDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFpDLSVVEHLDLLarahgledtDELVDSILEEVQLVPQSGQlpgTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:cd03369 87 IPQDPTLF-SGTIRSNLDPF---------DEYSDEEIYGALRVSEGGL---NLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190
....*....|....*....|....*....|.
gi 1391525485 165 QRLDQEGIDWLGKRLRheKEHNGLAIIMASH 195
Cdd:cd03369 154 ASIDYATDALIQKTIR--EEFTNSTILTIAH 182
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-202 |
5.76e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 9 KISNLVKKYGD---HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEkAKDTEISFRRNvatv 85
Cdd:PRK13545 23 KLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-AALIAISSGLN---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 iddldffPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:PRK13545 98 -------GQLTGIENIELKGLMMGLtkEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391525485 164 EQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEA 202
Cdd:PRK13545 171 LSVGDQTFTKKCLDKMNEFKE-QGKTIFFISHSLSQVKS 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-168 |
8.23e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.85 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 25 HFNLQVYESdaVALTGRNGSGKSTVLRCIVGSdKPTEGTIEVLGEKAKDTEI-SFRRNVATVIDDldffPDL---SVVEH 100
Cdd:PRK11174 370 NFTLPAGQR--IALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPeSWRKHLSWVGQN----PQLphgTLRDN 442
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 101 LdLLARAHGledTDELVDSILEEVQLVPQSGQLP-----------GTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK11174 443 V-LLGNPDA---SDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-195 |
9.41e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 9.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKA--KDTEISFRRNV 82
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDDLDFFPDLSVVEHLdLLAR----AHGLEDTDEL---VDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPK 155
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENI-FLGRefvnRFGRIDWKKMyaeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1391525485 156 KLLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASH 195
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISH 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-195 |
9.71e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 26 FNLQVYESDAVALTGRNGSGKSTVLRCIVGSdKPTEGTIEVLG---EKAKDTEISFRRnvATVIDDLDFFPDLSVVEHLD 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGqplEAWSAAELARHR--AYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 103 LLARAHGLEDTDE-LVDSILEEVQLVPQSGQLPGTLSSG--QRRRLALATAFVRPK-----KLLVLDEPEQRLD--QEGi 172
Cdd:PRK03695 92 LHQPDKTRTEAVAsALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVWPDinpagQLLLLDEPMNSLDvaQQA- 170
|
170 180
....*....|....*....|...
gi 1391525485 173 dWLgKRLRHEKEHNGLAIIMASH 195
Cdd:PRK03695 171 -AL-DRLLSELCQQGIAVVMSSH 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
36-213 |
1.26e-08 |
|
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: 53.24 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNvATVIDDLDFFPDL------SVVehldllaRAHG 109
Cdd:cd03250 34 VAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQN-GTIRENILFGKPFdeeryeKVI-------KACA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 110 LE-DTDELVDSILEEVqlvpqsGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP--------EQRLDQEGIdwlGKRLR 180
Cdd:cd03250 106 LEpDLEILPDGDLTEI------GEKGINLSGGQKQRISLARAVYSDADIYLLDDPlsavdahvGRHIFENCI---LGLLL 176
|
170 180 190
....*....|....*....|....*....|...
gi 1391525485 181 HEKehnglAIIMASHEPSLVEAVgARIVRIGGG 213
Cdd:cd03250 177 NNK-----TRILVTHQLQLLPHA-DQIVVLDNG 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-181 |
1.34e-08 |
|
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: 54.53 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKY--GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVgSDKPTEGTIEVLGEKAKDTEISFRRNVATV 85
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDLSVVEHLDLLARAhgledTDELVDSILEEVQLVPQSGQLPG-----------TLSSGQRRRLALATAFVRP 154
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLDPYEQW-----SDEEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSK 1371
|
170 180
....*....|....*....|....*..
gi 1391525485 155 KKLLVLDEPEQRLDQEGIDWLGKRLRH 181
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-168 |
1.44e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTeiSFRRNVatVID 87
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP--GAERGV--VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLAGVekMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
...
gi 1391525485 166 RLD 168
Cdd:PRK11248 158 ALD 160
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-168 |
1.68e-08 |
|
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: 53.00 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 17 YGDH-TVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVATVIDDLDFFPD 94
Cdd:cd03253 10 YDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLdSLRRAIGVVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 95 lsVVEHLDLLARahgLEDTDELVDS------ILEEVQLVPQS-----GQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP 163
Cdd:cd03253 90 --TIGYNIRYGR---PDATDEEVIEaakaaqIHDKIMRFPDGydtivGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
....*
gi 1391525485 164 EQRLD 168
Cdd:cd03253 165 TSALD 169
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-210 |
2.80e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlgekaKDTEIS-FRRNVATVI-DDLDFFPDLS 96
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINnIAKPYCTYIgHNLGLKLEMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 97 VVEHLDLLARAHgleDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLg 176
Cdd:PRK13541 87 VFENLKFWSEIY---NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL- 162
|
170 180 190
....*....|....*....|....*....|....
gi 1391525485 177 KRLRHEKEHNGLAIIMASHEPSLVEAvgARIVRI 210
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSHLESSIKS--AQILQL 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-184 |
3.58e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.41 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 22 VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVI--DDLDFFPDLSVve 99
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIpqDPVLFSGSLRM-- 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 100 HLDLLARAhgledTDELVDSILEEVQLVPQSGQLPG-----------TLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:TIGR00957 1379 NLDPFSQY-----SDEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170
....*....|....*.
gi 1391525485 169 QEGIDWLGKRLRHEKE 184
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFE 1469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-213 |
5.12e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 15 KKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEkakdteisfrrnVATVIDDLDFFPD 94
Cdd:PRK13546 32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------------VSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 95 LSVVEHLD--LLARAHGLEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEP----EQRLD 168
Cdd:PRK13546 100 LTGIENIEfkMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlsvgDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1391525485 169 QEGIDWLgkrlrHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:PRK13546 180 QKCLDKI-----YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
36-170 |
5.60e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.66 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKD-TEISFRRNVATVIDDLDFF------------PDLSVVEHLD 102
Cdd:PRK13657 364 VAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFnrsiednirvgrPDATDEEMRA 443
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 103 LLARAHGLedtdelvDSIL-EEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQE 170
Cdd:PRK13657 444 AAERAQAH-------DFIErKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-168 |
6.98e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNLVKKYGDHTVIDH-----------FNLQvyESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDT 74
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGWFRrqtveavkplsFTLR--EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 75 EISFRRNVATVIddldfFPDLS--------VVEHLDLLARAH---GLEDTDELVDSILEEVQLVP-QSGQLPGTLSSGQR 142
Cdd:PRK15112 81 DYSYRSQRIRMI-----FQDPStslnprqrISQILDFPLRLNtdlEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQK 155
|
170 180
....*....|....*....|....*.
gi 1391525485 143 RRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLD 181
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-207 |
8.21e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 2 ARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE--------KAKD 73
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpaKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 74 TEISFrrnvatVIDDLDFFPDLSVVEhlDLLARAHGLEDTDELVDSILEE--VQLVPQSgqLPGTLSSGQRRRLALATAF 151
Cdd:PRK15439 86 LGIYL------VPQEPLLFPNLSVKE--NILFGLPKRQASMQKMKQLLAAlgCQLDLDS--SAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 152 VRPKKLLVLDEPEQRLDQEGIDWLGKRLRhEKEHNGLAIIMASHEPSLVEAVGARI 207
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIR-ELLAQGVGIVFISHKLPEIRQLADRI 210
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-195 |
9.29e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.39 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKY--GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKpTEGTIEVLGEKAKDTEISFRRNVATV 85
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDLSVVEHLDLLARAhgledTDELVDSILEEVQLVPQSGQLPG-----------TLSSGQRRRLALATAFVRP 154
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGKW-----SDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1391525485 155 KKLLVLDEPEQRLDQEGIDWLGKRLRHekEHNGLAIIMASH 195
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEH 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-168 |
1.15e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.83 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 22 VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGekakdtEISFRRNVA-----TVIDDLDF----- 91
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------RISFSPQTSwimpgTIKDNIIFglsyd 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 92 -FPDLSVVehldllaRAHGLEdtdelvdsilEEVQLVPQSGQLP-----GTLSSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:TIGR01271 515 eYRYTSVI-------KACQLE----------EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
...
gi 1391525485 166 RLD 168
Cdd:TIGR01271 578 HLD 580
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-168 |
1.35e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.01 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 22 VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGekakdtEISFRRNVA-----TVIDDL------D 90
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------RISFSSQFSwimpgTIKENIifgvsyD 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 91 FFPDLSVVEHLDLlarahgledtDELVDSILEEVQLVPQSGQLpgTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:cd03291 126 EYRYKSVVKACQL----------EEDITKFPEKDNTVLGEGGI--TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-199 |
1.85e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 49.07 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLgekakdteisfrrnvatviddldffpdlsvv 98
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 99 EHLDLLarahgledtdelvdsileevqLVPQSGQLP-GTL------------SSGQRRRLALATAFVRPKKLLVLDEPEQ 165
Cdd:cd03223 62 EGEDLL---------------------FLPQRPYLPlGTLreqliypwddvlSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180 190
....*....|....*....|....*....|....
gi 1391525485 166 RLDQEGIDWLgkrLRHEKEHnGLAIIMASHEPSL 199
Cdd:cd03223 121 ALDEESEDRL---YQLLKEL-GITVISVGHRPSL 150
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
13-226 |
1.93e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.80 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 13 LVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG---EKAKDTEIS--FRRNVATVID 87
Cdd:PRK10070 34 ILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELRevRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 88 DLDFFPDLSVVEHLDL---LARAHGLEDTDELVDSiLEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:PRK10070 114 SFALMPHMTVLDNTAFgmeLAGINAEERREKALDA-LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 165 QRLDQEGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGGleETQSLAEPEQL 226
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG--EVVQVGTPDEI 252
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-195 |
2.73e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.09 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 12 NLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIE----VLGEKA----KDTeISFRRNVA 83
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvLLGGRSifnyRDV-LEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 TVIDDLDFFPdLSVVEHLDLLARAHGLEDTDE---LVDSILEEVQL----VPQSGQLPGTLSSGQRRRLALATAFVRPKK 156
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEfrgVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1391525485 157 LLVLDEPEQRLDQEGIDWLGKRLRHEKEHngLAIIMASH 195
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTH 220
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
8-210 |
2.81e-07 |
|
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: 49.14 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNlVKKYGDHTVIDhfnlqvYESDAVALTGRNGSGKSTVLRCIVGS---DKPT-----EGTIEVLGEKAKDTEIsfr 79
Cdd:cd03240 4 LSIRN-IRSFHERSEIE------FFSPLTLIVGQNGAGKTTIIEALKYAltgELPPnskggAHDPKLIREGEVRAQV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 rnvatvidDLDFFpdlsvvehldlLARAHGLEDTDELvdSILEEVQLVPQSG------QLPGTLSSGQRR------RLAL 147
Cdd:cd03240 74 --------KLAFE-----------NANGKKYTITRSL--AILENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLAL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 148 ATAFVRPKKLLVLDEPEQRLDQEGIDW-LGKRLRHEKEHNGLAIIMASHEPSLVEAVGaRIVRI 210
Cdd:cd03240 133 AETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHDEELVDAAD-HIYRV 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-207 |
3.87e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 23 IDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEIS----FRRNVATVIDD----LDffPD 94
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqaLRRDIQFIFQDpyasLD--PR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 95 LSVVEHLDLLARAHGLEDTDEL---VDSILEEVQLVPQSG-QLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQE 170
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAaarVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190
....*....|....*....|....*....|....*..
gi 1391525485 171 GIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARI 207
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-168 |
4.40e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVlgekAKDTEISFRRNvatvi 86
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGIKLGYFAQ----- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 87 DDLDFF-PDLSVVEHLDLLARAhglEDTDELVDSI----LEEVQLVPQSGQLPGtlssGQRRRLALATAFVRPKKLLVLD 161
Cdd:PRK10636 383 HQLEFLrADESPLQHLARLAPQ---ELEQKLRDYLggfgFQGDKVTEETRRFSG----GEKARLVLALIVWQRPNLLLLD 455
|
....*..
gi 1391525485 162 EPEQRLD 168
Cdd:PRK10636 456 EPTNHLD 462
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
36-198 |
5.16e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.39 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIvgSDKPTEGTIEvlGE---KAKDTEISFRRNVATViDDLD-FFPDLSVVEHLDLLARAHGle 111
Cdd:cd03232 36 TALMGESGAGKTTLLDVL--AGRKTAGVIT--GEiliNGRPLDKNFQRSTGYV-EQQDvHSPNLTVREALRFSALLRG-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 112 dtdelvdsileevqlvpqsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAII 191
Cdd:cd03232 109 -------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAIL 162
|
....*..
gi 1391525485 192 MASHEPS 198
Cdd:cd03232 163 CTIHQPS 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
12-177 |
5.31e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 12 NLVKKYGDHTVidHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIeVLGEKA-KDTE--ISF---RRNVATV 85
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRVlFDAEkgICLppeKRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDLSVVEHLdllarAHGLEDTD-ELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:PRK11144 82 FQDARLFPHYKVRGNL-----RYGMAKSMvAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170
....*....|....*..
gi 1391525485 165 QRLD----QEGIDWLGK 177
Cdd:PRK11144 157 ASLDlprkRELLPYLER 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-196 |
1.07e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 6 TVLKISNL-VKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRN--V 82
Cdd:COG3845 256 VVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDD-----LdfFPDLSVVEHLDL-------LARaHGLEDTD---ELVDSILEEVQLVPQSGQLP-GTLSSGQRRRLA 146
Cdd:COG3845 336 AYIPEDrlgrgL--VPDMSVAENLILgryrrppFSR-GGFLDRKairAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1391525485 147 LATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHE 196
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISED 461
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-222 |
1.89e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 11 SNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKA-----KDTEISFRRNVATV 85
Cdd:PRK10636 5 SSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQlawvnQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 86 IDDLDFFPDLS-----VVEHLD--LLARAHGLEDTDEL------VDSILEEVQLVPQSGQLP-GTLSSGQRRRLALATAF 151
Cdd:PRK10636 85 IDGDREYRQLEaqlhdANERNDghAIATIHGKLDAIDAwtirsrAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 152 VRPKKLLVLDEPEQRLDQEGIDWLGKRLrheKEHNGlAIIMASHEPSLVEAVGARIVRIgggleETQSLAE 222
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWL---KSYQG-TLILISHDRDFLDPIVDKIIHI-----EQQSLFE 226
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
36-201 |
2.44e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 47.38 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEISFRRNVATVIDDLDFFPDLSVVEHLDLLARAHGLEDTDE 115
Cdd:pfam13304 141 GLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 116 LVDSILEEVQLVPqsgqlPGTLSSGQRRRLALATAFVRPKK---LLVLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIM 192
Cdd:pfam13304 221 LILLENGGGGELP-----AFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSR-NGAQLIL 294
|
....*....
gi 1391525485 193 ASHEPSLVE 201
Cdd:pfam13304 295 TTHSPLLLD 303
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-175 |
2.70e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG--SDKPTEGTIEVLGEKAKDTEISF 78
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 79 RRNVATViddLDF-FP-DLSVVEHLDLLARAH-------GLEDTD-----ELVDSILEEVQLVPQ--SGQLPGTLSSGQR 142
Cdd:CHL00131 81 RAHLGIF---LAFqYPiEIPGVSNADFLRLAYnskrkfqGLPELDpleflEIINEKLKLVGMDPSflSRNVNEGFSGGEK 157
|
170 180 190
....*....|....*....|....*....|....
gi 1391525485 143 RR-LALATAFVRPkKLLVLDEPEQRLDqegIDWL 175
Cdd:CHL00131 158 KRnEILQMALLDS-ELAILDETDSGLD---IDAL 187
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-204 |
2.72e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.15 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHT-----VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEV--------------- 66
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 67 ---LGEKAKDTEiSFRRNVA-------------TVIDDLDFFPDLSVVEHLDLLARAHGLEDTDELVDSILEevqlvpqs 130
Cdd:PRK13631 101 tnpYSKKIKNFK-ELRRRVSmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLE-------- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1391525485 131 gQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGiDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVG 204
Cdd:PRK13631 172 -RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG-EHEMMQLILDAKANNKTVFVITHTMEHVLEVA 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-203 |
3.83e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.88 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 37 ALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKA----KDTEISFRRNVATVIDD------------------LDFFPD 94
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadPEAQKLLRQKIQIVFQNpygslnprkkvgqileepLLINTS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 95 LSVVEhldllaRAhgledtdELVDSILEEVQLVP-QSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD---QE 170
Cdd:PRK11308 125 LSAAE------RR-------EKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvsvQA 191
|
170 180 190
....*....|....*....|....*....|...
gi 1391525485 171 GIDWLGKRLRHEKehnGLAIIMASHEPSLVEAV 203
Cdd:PRK11308 192 QVLNLMMDLQQEL---GLSYVFISHDLSVVEHI 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-168 |
3.92e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.44 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDH--TVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG-EKAKDTEISFRRNVAT 84
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 85 VIDDLDFFPDlSVVEHLDLLARAhgledTDELVDSILEEVQLVPQSGQLPGTL-----------SSGQRRRLALATAFVR 153
Cdd:cd03288 100 ILQDPILFSG-SIRFNLDPECKC-----TDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVR 173
|
170
....*....|....*
gi 1391525485 154 PKKLLVLDEPEQRLD 168
Cdd:cd03288 174 KSSILIMDEATASID 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-168 |
5.49e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVGSDKPTEGTIEvlGEKAKDTEISFRRNvaTVIddLDFFPDLS-----VV---EHLDLLARA 107
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYD--EEPSWDEVLKRFRG--TEL--QDYFKKLAngeikVAhkpQYVDLIPKV 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 108 HG------LEDTDE--LVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:COG1245 176 FKgtvrelLEKVDErgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
8-168 |
7.52e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSG--KSTVLRCIVGSD---KPTEGTIEVLGEKAKDTEISFRRNV 82
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVIDDldffpDLSVVEHLDLLARAHGL--EDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVL 160
Cdd:NF000106 94 R*GRRE-----SFSGRENLYMIGR*LDLsrKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
....*...
gi 1391525485 161 DEPEQRLD 168
Cdd:NF000106 169 DEPTTGLD 176
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-191 |
7.85e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKY--GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG-EKAKDTEISFRRNVA- 83
Cdd:PLN03232 1235 IKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcDVAKFGLTDLRRVLSi 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 84 ----------TVIDDLDFFPDLSVVEHLDLLARAHGLEDTDELVDSILEEVQlvpQSGQlpgTLSSGQRRRLALATAFVR 153
Cdd:PLN03232 1315 ipqspvlfsgTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVS---EGGE---NFSVGQRQLLSLARALLR 1388
|
170 180 190
....*....|....*....|....*....|....*...
gi 1391525485 154 PKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAII 191
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVI 1426
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-199 |
1.37e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.51 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 22 VIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG--------SDKPTEGTIEVLGEKAKDTEISFRRNVatviddldFFP 93
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGElwpvyggrLTKPAKGKLFYVPQRPYMTLGTLRDQI--------IYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 94 DLSvvehLDLLARahGLEDTDelVDSILEEVQL---VPQSGQLPGT------LSSGQRRRLALATAFVRPKKLLVLDEPE 164
Cdd:TIGR00954 539 DSS----EDMKRR--GLSDKD--LEQILDNVQLthiLEREGGWSAVqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|....*
gi 1391525485 165 QRLdqeGIDWLGKRLRHEKEHnGLAIIMASHEPSL 199
Cdd:TIGR00954 611 SAV---SVDVEGYMYRLCREF-GITLFSVSHRKSL 641
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-224 |
1.81e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.78 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 4 RSTVLKISNLVKKygDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTE--ISFRRN 81
Cdd:PRK09700 262 HETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VATVID---DLDFFPDLSVVEHLDLLA--RAHGLEDTDELVDSILEEVQLVPQSGQLP----------GTLSSGQRRRLA 146
Cdd:PRK09700 340 MAYITEsrrDNGFFPNFSIAQNMAISRslKDGGYKGAMGLFHEVDEQRTAENQRELLAlkchsvnqniTELSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 147 LATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEhNGLAIIMASHEPSLVEAVGARIV-----RIGGGLEETQSLA 221
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAvfcegRLTQILTNRDDMS 498
|
...
gi 1391525485 222 EPE 224
Cdd:PRK09700 499 EEE 501
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
13-212 |
2.19e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 13 LVKKYGDHtvidHFNLQ---VYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEvlgekakdteisfrrnvatviddl 89
Cdd:cd03222 6 CVKRYGVF----FLLVElgvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 90 dffpdlsvvehLDLLARAHGLEDTDelvdsileevqlvpqsgqlpgtLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQ 169
Cdd:cd03222 58 -----------WDGITPVYKPQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1391525485 170 EGIDWLGKRLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGG 212
Cdd:cd03222 105 EQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-168 |
2.33e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 27 NLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGT-IEVLGEKAKDTEISFRRNvATVIDDLDFFPDLSVVEH---LD 102
Cdd:PLN03232 637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRGSVAYVPQVSWIFN-ATVRENILFGSDFESERYwraID 715
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 103 LLARAHgleDTDELVDSILEEVqlvpqsGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PLN03232 716 VTALQH---DLDLLPGRDLTEI------GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-195 |
2.73e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 43.76 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-----SFRRNV 82
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 83 ATVidDLDFF---------PDLS----VVEHL-DLLARAHGleDTDELVDSILEEVQLVPQS-GQLPGTLSSGQRRRLAL 147
Cdd:PRK11701 87 LRT--EWGFVhqhprdglrMQVSaggnIGERLmAVGARHYG--DIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1391525485 148 ATAFVRPKKLLVLDEPEQRLD---QEGIDWLGKRLRHEKehnGLAIIMASH 195
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDvsvQARLLDLLRGLVREL---GLAVVIVTH 210
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-227 |
2.76e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 26 FNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGE--KAKDTEISFRRNVATVIDDLDF---FPDLSVVEH 100
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEDRKAegiIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 101 LDLLARAHGL--------EDTDELVDSILEEVQL-VPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQrldqeG 171
Cdd:PRK11288 352 INISARRHHLragclinnRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR-----G 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391525485 172 IDWLGK----RLRHEKEHNGLAIIMASHEPSLVEAVGARIV-----RIGGGLEETQ-------SLAEPEQLA 227
Cdd:PRK11288 427 IDVGAKheiyNVIYELAAQGVAVLFVSSDLPEVLGVADRIVvmregRIAGELAREQaterqalSLALPRTSA 498
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
15-168 |
3.40e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 43.07 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 15 KKYGDHTVI---DHFNlqvyesdavALTGRNGSGKSTVLRCIvgsdkptegtIEVLGEKAKDTeisfRRNvatviddldf 91
Cdd:cd03239 10 KSYRDETVVggsNSFN---------AIVGPNGSGKSNIVDAI----------CFVLGGKAAKL----RRG---------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 92 fpDLSVVEHLDLLARAhgledTDELVDSILEE-VQLVPQsGQLPGTLSSGQRRRLALATAF----VRPKKLLVLDEPEQR 166
Cdd:cd03239 57 --SLLFLAGGGVKAGI-----NSASVEITFDKsYFLVLQ-GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAA 128
|
..
gi 1391525485 167 LD 168
Cdd:cd03239 129 LD 130
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-162 |
3.44e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNLVKKYGDH--TVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLG-EKAKDTEISFRRN 81
Cdd:PLN03130 1235 SGSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcDISKFGLMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VA-----------TVIDDLDFFPDLSVVEHLDLLARAHgLEDTDELVDSILEEVqlVPQSGQlpgTLSSGQRRRLALATA 150
Cdd:PLN03130 1315 LGiipqapvlfsgTVRFNLDPFNEHNDADLWESLERAH-LKDVIRRNSLGLDAE--VSEAGE---NFSVGQRQLLSLARA 1388
|
170
....*....|..
gi 1391525485 151 FVRPKKLLVLDE 162
Cdd:PLN03130 1389 LLRRSKILVLDE 1400
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-213 |
3.67e-05 |
|
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: 44.05 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 23 IDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGS-DKPTEGTIEVLGEKA--KDTEISFRRNVATVIDDLD---FFPDLS 96
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdiRNPAQAIRAGIAMVPEDRKrhgIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 97 VVEHLDL--LARAHGLEDTDEL--VDSILEEVQ---LVPQSGQLP-GTLSSGQRRRLALATAFVRPKKLLVLDEPEQrld 168
Cdd:TIGR02633 356 VGKNITLsvLKSFCFKMRIDAAaeLQIIGSAIQrlkVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR--- 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391525485 169 qeGIDWLGK----RLRHEKEHNGLAIIMASHEPSLVEAVGARIVRIGGG 213
Cdd:TIGR02633 433 --GVDVGAKyeiyKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
80-195 |
6.16e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 80 RNVATVIDDLDFFPDLSVVEHLDLLARAHGLEDT---------DELVDSILEEVQlvPQSGQLPGTLSSGQRRRLALATA 150
Cdd:PTZ00265 1295 RNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVkrackfaaiDEFIESLPNKYD--TNVGPYGKSLSGGQKQRIAIARA 1372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1391525485 151 FVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHNGLAIIMASH 195
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-196 |
6.47e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.78 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 1 MARRSTVLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIevLGEKAKDTEIS--- 77
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL--LFEGEDISTLKpei 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 78 FRRNVA-----------TVIDDLdFFPDLSVVEHLDLLARAHGLEDTdELVDSILEevqlvpqsgQLPGTLSSGQRRRLA 146
Cdd:PRK10247 79 YRQQVSycaqtptlfgdTVYDNL-IFPWQIRNQQPDPAIFLDDLERF-ALPDTILT---------KNIAELSGGEKQRIS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 147 LATAFVRPKKLLVLDEPEQRLDQEgidwlGKRLRHEKEH-----NGLAIIMASHE 196
Cdd:PRK10247 148 LIRNLQFMPKVLLLDEITSALDES-----NKHNVNEIIHryvreQNIAVLWVTHD 197
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-199 |
6.50e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 37 ALTGRNGSGKSTVLRCIVGSDKP--TEGTIEVLG-EKAKDTeisFRRnVATVIDDLDFF-PDLSVVEHLDL-----LARA 107
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfPKKQET---FAR-ISGYCEQNDIHsPQVTVRESLIYsaflrLPKE 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 108 HGLEDTDELVDSILEEVQLVPQSGQ---LPGT--LSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHE 182
Cdd:PLN03140 986 VSKEEKMMFVDEVMELVELDNLKDAivgLPGVtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNT 1065
|
170
....*....|....*..
gi 1391525485 183 KEhNGLAIIMASHEPSL 199
Cdd:PLN03140 1066 VD-TGRTVVCTIHQPSI 1081
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
8-195 |
8.78e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNLvKKYGDHTVIDhFNLQVyesdaVALTGRNGSGKSTVLRCIV-----GSDKPTEGTIEVLGEKAKDTEISF---- 78
Cdd:COG0419 5 LRLENF-RSYRDTETID-FDDGL-----NLIVGPNGAGKSTILEAIRyalygKARSRSKLRSDLINVGSEEASVELefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 79 RRNVATVI---DDLDFFPDLSVVEHLDLLARAHGLEDTDELVDSI-------------------LEEVQLVPQSGQLP-G 135
Cdd:COG0419 78 GGKRYRIErrqGEFAEFLEAKPSERKEALKRLLGLEIYEELKERLkeleealesaleelaelqkLKQEILAQLSGLDPiE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 136 TLSSGQRRRLALATAFVrpkklLVLDepEQRLDQEGIDWLGKRLRHekehngLAIImaSH 195
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEE------LAII--TH 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-193 |
8.78e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVL-GEKAKDTEISF-RRNVATVIDDLDFFPD-- 94
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWwRSKIGVVSQDPLLFSNsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 95 -----LSVVEHLDLLARAHGLE-------------------------------DTDELVD-----SILEEVQLVPQSGQ- 132
Cdd:PTZ00265 477 knnikYSLYSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndmsnttDSNELIEmrknyQTIKDSEVVDVSKKv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 133 --------LP-----------GTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKRLRHEK-EHNGLAIIM 192
Cdd:PTZ00265 557 lihdfvsaLPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIII 636
|
.
gi 1391525485 193 A 193
Cdd:PTZ00265 637 A 637
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-168 |
1.11e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 41.97 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVGSDKPTEGTIEvlGEKAKDTEISFRRNVATviddLDFFP-----DLSVV---EHLDLLARA 107
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFD--DPPDWDEILDEFRGSEL----QNYFTkllegDVKVIvkpQYVDLIPKA 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1391525485 108 ------HGLEDTDEL--VDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:cd03236 103 vkgkvgELLKKKDERgkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
40-168 |
1.27e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 40 GRNGSGKSTVLRCI----VGSDKPTEGTIEVLGEKAKDTEISFRRNVATVIDDLDFFPDLSVVEHLDLLARAHGLEDTDE 115
Cdd:TIGR00956 94 GRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNRPD 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1391525485 116 LVDS---ILEEVQLVPQSGQLPGT------------LSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:TIGR00956 174 GVSReeyAKHIADVYMATYGLSHTrntkvgndfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-200 |
2.37e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVGSDKPTEGTIevlGEKAKDTEISFRRNVatvIDDLDffpdLSVVEhldLLARAHGLEDTDE 115
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV---FRSAKVRMAVFSQHH---VDGLD----LSSNP---LLYMMRCFPGVPE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 116 lvDSILEEVQLVPQSGQLP----GTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWLGKrlrhekehnGLA-- 189
Cdd:PLN03073 605 --QKLRAHLGSFGVTGNLAlqpmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ---------GLVlf 673
|
170
....*....|....
gi 1391525485 190 ---IIMASHEPSLV 200
Cdd:PLN03073 674 qggVLMVSHDEHLI 687
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
38-217 |
4.37e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.13 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 38 LTGRNGSGKSTVLRCI-VGSDKPTEG-----------TIEVLGE---------KAKDTeiSFRR-----NVATVIDDLDF 91
Cdd:COG3910 42 FVGENGSGKSTLLEAIaVAAGFNPEGgsknfrfstreSESALGEylrlsrglpKPRDG--FFLRaesffNVATYLDELAA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 92 FPDLSVVEHL--DLLARAHGledtdelvDSILeevqlvpqsgqlpgtlssgqrrrlALATAFVRPKKLLVLDEPEQRLDQ 169
Cdd:COG3910 120 EGPGILDSYGgrSLHEQSHG--------ESFL------------------------ALFENRFRGNGLYLLDEPEAALSP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1391525485 170 EGIDWLGKRLrHEKEHNGLAIIMASHEPSLVEAVGARIVRIG-GGLEET 217
Cdd:COG3910 168 SRQLALLALI-HDLVREGSQFIIATHSPILMAYPGATIYEFDeDGIREV 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-198 |
4.64e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.28 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLgekakdteisfrrnvatviddldffpdlsvvehldllarahgleDTDE 115
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------------DGED 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 116 LVDSILEEVQLVPQSGQlPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEGIDWL-----GKRLRHEKEHNGLAI 190
Cdd:smart00382 41 ILEEVLDQLLLIIVGGK-KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLLLKSEKNLTV 119
|
....*...
gi 1391525485 191 IMASHEPS 198
Cdd:smart00382 120 ILTTNDEK 127
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-200 |
5.05e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.48 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 18 GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG---SDKPTEGT-----IEVLGEKAKDTEISFRRNVATVIDD- 88
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGllaANGRIGGSatfngREILNLPEKELNKLRAEQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 89 -LDFFPDLSVVEHL-DLLARAHGLEDTDELVDSI--LEEVQLvPQS----GQLPGTLSSGQRRRLALATAFV-RPKkLLV 159
Cdd:PRK09473 107 mTSLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVrmLDAVKM-PEArkrmKMYPHEFSGGMRQRVMIAMALLcRPK-LLI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1391525485 160 LDEPEQRLD---QEGIDWLGKRLRHEkehNGLAIIMASHEPSLV 200
Cdd:PRK09473 185 ADEPTTALDvtvQAQIMTLLNELKRE---FNTAIIMITHDLGVV 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
40-213 |
5.14e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 40 GRNGSGKSTVLRCIVGSDKPTEGtiEVLGEK--AKDTEISFRRNvATVIDDLDFFPDlsvvehldllarahglEDTDELV 117
Cdd:PTZ00243 693 GATGSGKSTLLQSLLSQFEISEG--RVWAERsiAYVPQQAWIMN-ATVRGNILFFDE----------------EDAARLA 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 118 DSIlEEVQLVPQSGQLPG-----------TLSSGQRRRLALATAFVRPKKLLVLDEPEQRLDQEgidwLGKRLRHEKEHN 186
Cdd:PTZ00243 754 DAV-RVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH----VGERVVEECFLG 828
|
170 180 190
....*....|....*....|....*....|
gi 1391525485 187 GLA---IIMASHEPSLVeAVGARIVRIGGG 213
Cdd:PTZ00243 829 ALAgktRVLATHQVHVV-PRADYVVALGDG 857
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
36-201 |
5.19e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRcivgsdkptEGTIEVLGEKAKDTEISFRRNVATVIDDLDFfpdlsvvehldllarahgledtde 115
Cdd:cd03238 24 VVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQLQF------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 116 LVDSILEEVQLvpqsGQLPGTLSSGQRRRLALAT-AFVRPKK-LLVLDEPEQRLDQEGIDWLGKRLRhEKEHNGLAIIMA 193
Cdd:cd03238 71 LIDVGLGYLTL----GQKLSTLSGGELQRVKLASeLFSEPPGtLFILDEPSTGLHQQDINQLLEVIK-GLIDLGNTVILI 145
|
....*...
gi 1391525485 194 SHEPSLVE 201
Cdd:cd03238 146 EHNLDVLS 153
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-207 |
5.37e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSdKPT---EGTIEVLGEKA--KDTEISFRRN 81
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCrfKDIRDSEALG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VATVIDDLDFFPDLSVVEHLDL-LARAHG--------LEDTDELvdsiLEEVQLVPQSGQLPGTLSSGQRRRLALATAFV 152
Cdd:NF040905 80 IVIIHQELALIPYLSIAENIFLgNERAKRgvidwnetNRRAREL----LAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 153 RPKKLLVLDEPEQRLDQEGIDWLGKRLRHEKEHnGLAIIMASHEPSLVEAVGARI 207
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSI 209
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
8-87 |
6.23e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 8 LKISNlVKKYGDHTVidHFNLQVyesdaVALTGRNGSGKSTVLRCIV---GSDKPTEGTIEVLGEKAKDTEISFRRNVAT 84
Cdd:pfam13476 1 LTIEN-FRSFRDQTI--DFSKGL-----TLITGPNGSGKTTILDAIKlalYGKTSRLKRKSGGGFVKGDIRIGLEGKGKA 72
|
...
gi 1391525485 85 VID 87
Cdd:pfam13476 73 YVE 75
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-168 |
7.67e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 12 NLVKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGsDKPT------------EGTIEVL-------GEKAK 72
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrRGSGETIwdikkhiGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 73 DTEISFRRN--VATVI-----DDLDFFPDLS------VVEHLDLLarahGLedTDELVDSILEevqlvpqsgqlpgTLSS 139
Cdd:PRK10938 344 SLHLDYRVStsVRNVIlsgffDSIGIYQAVSdrqqklAQQWLDIL----GI--DKRTADAPFH-------------SLSW 404
|
170 180
....*....|....*....|....*....
gi 1391525485 140 GQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-202 |
8.65e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 40.08 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 19 DHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVLGEKAKDTEI-SFRRNVATVIDDLDFFPDlSV 97
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 98 ---------------VEHLDLLARAHglEDTDELVDSILEEVqlvpqsGQLPGTLSSGQRRRLALATAFVRPKKLLVLDE 162
Cdd:PRK10789 406 annialgrpdatqqeIEHVARLASVH--DDILRLPQGYDTEV------GERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1391525485 163 PEQRLDqegidwlgKRLRHEKEHN------GLAIIMASHEPS-LVEA 202
Cdd:PRK10789 478 ALSAVD--------GRTEHQILHNlrqwgeGRTVIISAHRLSaLTEA 516
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-168 |
9.66e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.79 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 36 VALTGRNGSGKSTVLRCIVGSDKP------TEGTI-EVLgEKAKDTEIsfrrnvatviddLDFFPDLS-----VV---EH 100
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPnlgdyeEEPSWdEVL-KRFRGTEL------------QNYFKKLYngeikVVhkpQY 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1391525485 101 LDLLARA-HG-----LEDTDE--LVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PRK13409 169 VDLIPKVfKGkvrelLKKVDErgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-168 |
2.08e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.14 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 7 VLKISNLVKkYGDHTVIDHFNLQVYESDAVALTGRNGSGKStvLRCIVGSDKPTEGTIEVLGEKAKDTE----ISFR-RN 81
Cdd:PRK10418 4 QIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKpvapCALRgRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 82 VATVIDD--LDFFPDLSVVEHLDLLARAHGLEDTDELVDSILEEVQL-----VPQSgqLPGTLSSGQRRRLALATAFVRP 154
Cdd:PRK10418 81 IATIMQNprSAFNPLHTMHTHARETCLALGKPADDATLTAALEAVGLenaarVLKL--YPFEMSGGMLQRMMIALALLCE 158
|
170
....*....|....
gi 1391525485 155 KKLLVLDEPEQRLD 168
Cdd:PRK10418 159 APFIIADEPTTDLD 172
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
136-175 |
3.08e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.30 E-value: 3.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1391525485 136 TLSSGQRRRLALATA-FVRPKkLLVLDEPEQRLDQEGIDWL 175
Cdd:PLN03073 344 TFSGGWRMRIALARAlFIEPD-LLLLDEPTNHLDLHAVLWL 383
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
8-54 |
4.33e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.28 E-value: 4.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1391525485 8 LKISNlVKKYGDHTVidHFNLqvyESDAVALTGRNGSGKSTVLRCIV 54
Cdd:COG3950 6 LTIEN-FRGFEDLEI--DFDN---PPRLTVLVGENGSGKTTLLEAIA 46
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-213 |
4.40e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 37.50 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 20 HTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVG--SDKPTEGTIEVLGEKAKDTE---------ISFRRNVATVIDD 88
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEplaaidaprLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 89 LDFfpDLSVVEHLDL----LARAHG--LEDTDELVDSILEEVQLVPQSGQLPGTLSSGQRRRLALATAF---------VR 153
Cdd:PRK13547 94 PAF--AFSAREIVLLgrypHARRAGalTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1391525485 154 PKKLLVLDEPEQRLD---QEGIDWLGKRLRHEKEHNGLAIImasHEPSLVEAVGARIVRIGGG 213
Cdd:PRK13547 172 PPRYLLLDEPTAALDlahQHRLLDTVRRLARDWNLGVLAIV---HDPNLAARHADRIAMLADG 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-168 |
5.05e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 37.80 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 18 GDHTVIDHFNLQVYESDAVALTGRNGSGKSTVLRCIVGSDKPTEGTIEVL-GEKAKDTEISFRRNvATVIDDLDFFPDLS 96
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIrGTVAYVPQVSWIFN-ATVRDNILFGSPFD 706
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391525485 97 VVEH---LDLLARAHgleDTDELVDSILEEVqlvpqsGQLPGTLSSGQRRRLALATAFVRPKKLLVLDEPEQRLD 168
Cdd:PLN03130 707 PERYeraIDVTALQH---DLDLLPGGDLTEI------GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-208 |
6.11e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 37.36 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 5 STVLKISNL----VKKYGDHTVIDHFNLQVYESDAVALTGRNGSGKS----TVLRCIVGSDKPTEGTIEVLGE---KAKD 73
Cdd:COG4172 4 MPLLSVEDLsvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdllGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 74 TEI-SFRRNVATVIddldfF--PDLS----------VVEHLDL---LARAHGLEDTDELvdsiLEEVQLV-PQS--GQLP 134
Cdd:COG4172 84 RELrRIRGNRIAMI-----FqePMTSlnplhtigkqIAEVLRLhrgLSGAAARARALEL----LERVGIPdPERrlDAYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391525485 135 GTLSSGQRRR----LALATafvRPkKLLVLDEPEQRLD---QEGIDWLGKRLRHEkehNGLAIIMASHEPSLVEAVGARI 207
Cdd:COG4172 155 HQLSGGQRQRvmiaMALAN---EP-DLLIADEPTTALDvtvQAQILDLLKDLQRE---LGMALLLITHDLGVVRRFADRV 227
|
.
gi 1391525485 208 V 208
Cdd:COG4172 228 A 228
|
|
| |
