|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-151 |
2.15e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.61 E-value: 2.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFLIEHP 72
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaevrrRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 73 KLYDNKSGLYNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:COG1131 83 ALYPDLTVRENLRFFARLYGlpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
.
gi 579496312 151 D 151
Cdd:COG1131 163 D 163
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-151 |
1.76e-47 |
|
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: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKVDIDNAD---NIGFLIEHP 72
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIkpdsgeITFDGKSYQKNIEalrRIGALIEAP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579496312 73 KLYDNKSGLYNLKLFAqvLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03268 82 GFYPNLTARENLRLLA--RLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-151 |
3.96e-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: 147.70 E-value: 3.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFLIEH 71
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkeprearrQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PKLYDNKSGLYNLKLFAQVLGKgFDKAY---TDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGL-FDEELkkrIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
...
gi 579496312 149 GMD 151
Cdd:COG4555 162 GLD 164
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-151 |
1.95e-40 |
|
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: 133.29 E-value: 1.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFLIEH 71
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDikkepeevkrRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PKLYDNKSGLYNLklfaqvlgkgfdkaytdkiidafgmrpyikkkvkKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03230 82 PSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1-151 |
3.19e-39 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 131.75 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-------NIGFLIEHPK 73
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwtrkdlhKIGSLIESPP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 74 LYDNKSGLYNLKLFAQVLGkgFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLG--LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-151 |
1.11e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.84 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK-VDIDNADNIGFLIEhpkl 74
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILapdsgeVLWDGEpLDPEDRRRIGYLPE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 75 ydnKSGLY-NLKLFAQV--LG--KGFDKAYTDKIIDA----FGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:COG4152 79 ---ERGLYpKMKVGEQLvyLArlKGLSKAEAKRRADEwlerLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:COG4152 156 PFSGLD 161
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-151 |
2.04e-33 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 117.08 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSN----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFL 68
Cdd:cd03266 4 ADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDvvkepaearrRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQVLG-KGFD-KAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGlKGDElTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
....*
gi 579496312 147 TNGMD 151
Cdd:cd03266 164 TTGLD 168
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-151 |
2.23e-32 |
|
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: 113.91 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK-VDIDNADNIGFLIEHPK 73
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlpdsgeVLFDGKpLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 74 LYDNKSGLYNLKLFAQVlgKGFDKAYTDKIID----AFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNG 149
Cdd:cd03269 81 LYPKMKVIDQLVYLAQL--KGLKKEEARRRIDewleRLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
..
gi 579496312 150 MD 151
Cdd:cd03269 159 LD 160
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-151 |
1.11e-31 |
|
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: 112.19 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFLIE 70
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 HPKLYDNKSGLYNLKLFAQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
.
gi 579496312 151 D 151
Cdd:COG4133 163 D 163
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-148 |
2.19e-30 |
|
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: 106.96 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGFLIEHPKLYDNKSGLYNL 84
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 85 KLFAQV--LGKGFDKAYTDKIIDAFGMRPYIKKKVKKY----SMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:pfam00005 81 RLGLLLkgLSKREKDARAEEALEKLGLGDLADRPVGERpgtlSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-151 |
5.80e-30 |
|
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: 107.98 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGS--NVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFL 68
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQVLGKGFDKAY--TDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKeeVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
....*
gi 579496312 147 TNGMD 151
Cdd:cd03263 161 TSGLD 165
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-151 |
1.81e-28 |
|
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: 103.81 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSrIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKVDIDNADN----IGFLIEH 71
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTppssgtIRIDGQDVLKQPQKlrrrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PKLYDNKSGLYNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNG 149
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGipSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
..
gi 579496312 150 MD 151
Cdd:cd03264 161 LD 162
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-151 |
4.63e-27 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 98.86 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADnigfliehpklydnksgl 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD------------------ 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 82 ynlklfaqvLGKGFDKAYTDKIidafGMRPyikkkvkKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd00267 63 ---------IAKLPLEELRRRI----GYVP-------QLSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2-151 |
1.39e-26 |
|
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: 99.08 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGS--NVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGFL 68
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLY--------DNKSGLYNLKLfaqvlGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKF 140
Cdd:cd03225 81 FQNPDDQffgptveeEVAFGLENLGL-----PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170
....*....|.
gi 579496312 141 LILDEPTNGMD 151
Cdd:cd03225 156 LLLDEPTAGLD 166
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-151 |
3.43e-26 |
|
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: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFLIEHPK 73
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvreprevrrRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 74 LYDNKSGLYNLKLFAQVLGKGFDKA--YTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAERreRIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-149 |
2.34e-25 |
|
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: 95.96 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMK-------VMNGNIIkFDGKvDIDNA-------DNIGF 67
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtimgllpPRSGSIR-FDGR-DITGLppherarAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNKSGLYNLKLFAQVLGKGFDKAYTDKIIDAFgmrPYIKKKVKKY----SMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELF---PRLKERRKQLagtlSGGEQQMLAIARALMSRPKLLLL 156
|
....*.
gi 579496312 144 DEPTNG 149
Cdd:cd03224 157 DEPSEG 162
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-151 |
4.61e-24 |
|
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: 92.78 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKY-GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGFLI 69
Cdd:COG1122 2 ELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 EHP-------KLYDNKS-GLYNLKL-FAQVlgkgfdKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKF 140
Cdd:COG1122 82 QNPddqlfapTVEEDVAfGPENLGLpREEI------RERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170
....*....|.
gi 579496312 141 LILDEPTNGMD 151
Cdd:COG1122 156 LVLDEPTAGLD 166
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-145 |
6.37e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 6.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 8 KKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGnIIKFD-GKVDIDnaDNIGFLIE-----HPKLydnkSGL 81
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG-ILEPTsGRVEVN--GRVSALLElgagfHPEL----TGR 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 82 YNLKLFAQVLgkGFDKAYTDKIID---AF-GMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:COG1134 107 ENIYLNGRLL--GLSRKEIDEKFDeivEFaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-151 |
6.87e-24 |
|
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: 91.34 E-value: 6.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADnigflIEHpklydnksgl 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD-----LAS---------- 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 82 YNLKLFAQVLgkgfdkAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03214 66 LSPKELARKI------AYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-150 |
1.56e-23 |
|
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: 91.73 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKvDIDNADN-------IG-- 66
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrptsgsVLFDGE-DITGLPPheiarlgIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FliEHPKLYDNKSGLYNLKLFAQVLGKGFD------------KAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSL 134
Cdd:cd03219 81 F--QIPRLFPELTVLENVMVAAQARTGSGLllararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170
....*....|....*.
gi 579496312 135 MNKPKFLILDEPTNGM 150
Cdd:cd03219 159 ATDPKLLLLDEPAAGL 174
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-146 |
1.73e-23 |
|
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: 91.04 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD---------NIGFLIEH 71
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgvpperrNIGMVFQD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579496312 72 PKLYDNKSGLYNLK--LFAQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:cd03259 81 YALFPHLTVAENIAfgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-151 |
6.80e-23 |
|
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: 89.87 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD--------------NIGFL 68
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaelyrlrrRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQVLGKGFDKAYTDKI---IDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:cd03261 163 PTAGLD 168
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-151 |
2.31e-22 |
|
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: 87.97 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKVDIDNADNIGFLiehPKLY 75
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkptsgsIRVFGKPLEKERKRIGYV---PQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 76 DN------------KSGLYNLKLFAQVLGKGfDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:cd03235 78 SIdrdfpisvrdvvLMGLYGHKGLFRRLSKA-DKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
....*...
gi 579496312 144 DEPTNGMD 151
Cdd:cd03235 157 DEPFAGVD 164
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-151 |
2.93e-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: 88.37 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGnIIKFD-GKVDIDNAD------------NIGFL 68
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVG-LVKPDsGKILLDGQDitklpmhkrarlGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQVLGKgfDKAYTDKIIDA----FGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILD 144
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGL--SKKEREEKLEElleeFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
....*..
gi 579496312 145 EPTNGMD 151
Cdd:cd03218 159 EPFAGVD 165
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-151 |
3.63e-22 |
|
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: 86.86 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-------------NIGF 67
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNKSGLYNLklfaqvlgkgfdkaytdkiidAFGMrpyikkkvkkySMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:cd03229 81 VFQDFALFPHLTVLENI---------------------ALGL-----------SGGQQQRVALARALAMDPDVLLLDEPT 128
|
....
gi 579496312 148 NGMD 151
Cdd:cd03229 129 SALD 132
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-147 |
7.40e-22 |
|
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: 86.77 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSN----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG------NIIKFDGKvDIDN---------- 61
Cdd:cd03255 2 ELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldrptsGEVRVDGT-DISKlsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 62 ADNIGFLIEHPKLYDNKSGLYNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPK 139
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
....*...
gi 579496312 140 FLILDEPT 147
Cdd:cd03255 161 IILADEPT 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-147 |
1.32e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK-VDIDN-----ADNIGFLIE 70
Cdd:COG3845 8 LRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqpdsgeILIDGKpVRIRSprdaiALGIGMVHQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 HPKLYDNKSGLYNLKLFAQVLGKGF---DKAYTD--KIIDAFGMR--PYikKKVKKYSMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:COG3845 88 HFMLVPNLTVAENIVLGLEPTKGGRldrKAARARirELSERYGLDvdPD--AKVEDLSVGEQQRVEILKALYRGARILIL 165
|
....
gi 579496312 144 DEPT 147
Cdd:COG3845 166 DEPT 169
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-151 |
1.57e-21 |
|
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: 84.04 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFliehpklydnksgl 81
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGY-------------- 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 82 ynlklFAQvlgkgfdkaytdkiidafgmrpyikkkvkkYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03221 68 -----FEQ------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-151 |
1.75e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIEHPKLYDNKS--- 79
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 80 -------GLYNL-KLFAQVLGKGFDK------------------AYT-----DKIIDAFGMRP-YIKKKVKKYSMGMKQK 127
Cdd:COG0488 81 tvldgdaELRALeAELEELEAKLAEPdedlerlaelqeefealgGWEaearaEEILSGLGFPEeDLDRPVSELSGGWRRR 160
|
170 180
....*....|....*....|....
gi 579496312 128 LAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLD 184
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-150 |
1.77e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 86.63 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKvDIDN--ADNI---G---- 66
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYrptsgrILFDGR-DITGlpPHRIarlGiart 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FliEHPKLYDNKSGLYNLKLFAQV-LGKGF------------------DKAytDKIIDAFGMRPYIKKKVKKYSMGMKQK 127
Cdd:COG0411 85 F--QNPRLFPELTVLENVLVAAHArLGRGLlaallrlprarreerearERA--EELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180
....*....|....*....|...
gi 579496312 128 LAIAVSLMNKPKFLILDEPTNGM 150
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGL 183
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-151 |
1.95e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDF--GDsrIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFL-IEHPKLYDNKS 79
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIdrGD--RIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFdQHQEELDPDKT 395
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 80 GLynlklfaQVLGKGFDKAYTDKIID---AFGMRP-YIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG0488 396 VL-------DELRDGAPGGTEQEVRGylgRFLFSGdDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-147 |
3.57e-21 |
|
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: 83.63 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK-VDIDNADNigfliehpkl 74
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYkpdsgeILVDGKeVSFASPRD---------- 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579496312 75 ydnksglynlklfAQVLGKGFdkaytdkiidafgmrpyikkkVKKYSMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:cd03216 72 -------------ARRAGIAM---------------------VYQLSVGERQMVEIARALARNARLLILDEPT 110
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-147 |
9.02e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK-VDIDN------------- 61
Cdd:COG1129 6 EMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYqpdsgeILLDGEpVRFRSprdaqaagiaiih 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 62 -----------ADNIgFLIEHPKlydnKSGLYNLK-LFAQvlgkgfdkayTDKIIDAFGMR--PyiKKKVKKYSMGMKQK 127
Cdd:COG1129 86 qelnlvpnlsvAENI-FLGREPR----RGGLIDWRaMRRR----------ARELLARLGLDidP--DTPVGDLSVAQQQL 148
|
170 180
....*....|....*....|
gi 579496312 128 LAIAVSLMNKPKFLILDEPT 147
Cdd:COG1129 149 VEIARALSRDARVLILDEPT 168
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-151 |
1.48e-20 |
|
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: 84.32 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGFLI 69
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 EHPKLYDNKS-------GLYN-LKLFAQVLGKgfDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFL 141
Cdd:COG1120 82 QEPPAPFGLTvrelvalGRYPhLGLFGRPSAE--DREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170
....*....|
gi 579496312 142 ILDEPTNGMD 151
Cdd:COG1120 160 LLDEPTSHLD 169
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-151 |
3.63e-20 |
|
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: 82.58 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN-------GNIIkFDG-KVDIDNAD------NIGF 67
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINlleepdsGTII-IDGlKLTDDKKNinelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNKSGLYNLKLfAQVLGKGFDKAYTDKI----IDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL-APIKVKGMSKAEAEERalelLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
....*...
gi 579496312 144 DEPTNGMD 151
Cdd:cd03262 160 DEPTSALD 167
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-151 |
5.37e-20 |
|
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: 82.62 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD--------------NIG 66
Cdd:cd03256 2 EVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPKLYDNKSGLYNL-------KLFAQVLGKGFDKAytDKII-----DAFGMRPYIKKKVKKYSMGMKQKLAIAVSL 134
Cdd:cd03256 82 MIFQQFNLIERLSVLENVlsgrlgrRSTWRSLFGLFPKE--EKQRalaalERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170
....*....|....*..
gi 579496312 135 MNKPKFLILDEPTNGMD 151
Cdd:cd03256 160 MQQPKLILADEPVASLD 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-146 |
1.64e-19 |
|
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: 80.98 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSN----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKVDIDNADNIGFLIE 70
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErptsgeVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 71 HPKLYDNKSGLYN--LKLFAQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:cd03293 81 QDALLPWLTVLDNvaLGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-151 |
2.13e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 80.38 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD--------NIGFLIEHPK 73
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 74 LYdnksgLYNLKLFAQVL----GKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNG 149
Cdd:cd03226 82 YQ-----LFTDSVREELLlglkELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
..
gi 579496312 150 MD 151
Cdd:cd03226 157 LD 158
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-145 |
2.27e-19 |
|
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: 80.65 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 8 KKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD------NIGFlieHPKLydnkSGL 81
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssllglGGGF---NPEL----TGR 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 82 YNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:cd03220 103 ENIYLNGRLLGlsRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-146 |
1.33e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 79.36 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKY----GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNA------DNIGFLIEHP 72
Cdd:COG1116 10 LRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgPDRGVVFQEP 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 73 KLYDNKSGLYNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:COG1116 90 ALLPWLTVLDNVALGLELRGvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEP 165
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-147 |
1.64e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 78.16 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSN----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGnIIKFD-GKVDIDNAD------------ 63
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LDRPTsGEVLIDGQDisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 ---NIGFLIEHPKLYDNKSGLYNLKLFAQVLGKGF--DKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKP 138
Cdd:COG1136 84 rrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRkeRRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
....*....
gi 579496312 139 KFLILDEPT 147
Cdd:COG1136 164 KLILADEPT 172
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-151 |
2.04e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.55 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIM-------KVMNGNIIKFDGkvDIDNAD-------NIGFL 68
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagarKIQQGRVEVLGG--DMADARhrravcpRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 iehPK-----LYDNKSGLYNLKLFAQVLGkgFDKAYTDKIID----AFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPK 139
Cdd:NF033858 82 ---PQglgknLYPTLSVFENLDFFGRLFG--QDAAERRRRIDellrATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170
....*....|..
gi 579496312 140 FLILDEPTNGMD 151
Cdd:NF033858 157 LLILDEPTTGVD 168
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-151 |
2.75e-18 |
|
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: 78.10 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKvDIDNAD---------NIG 66
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrpdsgeILVDGQ-DITGLSekelyelrrRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPKLYDNKSGLYNLKLFAQVLGKgFDKAYTDKI----IDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLI 142
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTD-LSEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
....*....
gi 579496312 143 LDEPTNGMD 151
Cdd:COG1127 165 YDEPTAGLD 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-151 |
5.48e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.01 E-value: 5.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD--------------NIG 66
Cdd:COG2884 3 RFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlkrreipylrrRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPKLYDNKSGLYNLKLFAQVLGKGfDKAYTDKIIDA---FGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:COG2884 83 VVFQDFRLLPDRTVYENVALPLRVTGKS-RKEIRRRVREVldlVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
....*...
gi 579496312 144 DEPTNGMD 151
Cdd:COG2884 162 DEPTGNLD 169
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-151 |
1.32e-17 |
|
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: 78.34 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYG--SNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM-------NGNIiKFDGkVDIDNAD------NIG 66
Cdd:COG2274 475 ELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlglyeptSGRI-LIDG-IDLRQIDpaslrrQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPKLYdnkSG-LY-NLKLFaqvlgkgfDKAYTD-KIIDA---FGMRPYIKKKVKKY-----------SMGMKQKLA 129
Cdd:COG2274 553 VVLQDVFLF---SGtIReNITLG--------DPDATDeEIIEAarlAGLHDFIEALPMGYdtvvgeggsnlSGGQRQRLA 621
|
170 180
....*....|....*....|..
gi 579496312 130 IAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG2274 622 IARALLRNPRILILDEATSALD 643
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-151 |
3.14e-17 |
|
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: 74.97 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKvDIDNAD------NIGF-- 67
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFEtptsgeILLDGK-DITNLPphkrpvNTVFqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 --LIEHPKLYDNKSglYNLKLfaQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:cd03300 81 yaLFPHLTVFENIA--FGLRL--KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:cd03300 157 PLGALD 162
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-151 |
4.28e-17 |
|
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: 74.68 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITK-KYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVD----------IDNADNIGFLI-E 70
Cdd:cd03267 23 LKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvaglvpwkrrKKFLRRIGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 HPKLYDNKSGLYNLKLFAQV--LGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAAIydLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
...
gi 579496312 149 GMD 151
Cdd:cd03267 183 GLD 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-151 |
4.73e-17 |
|
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: 74.52 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG-----NIIKFDGKVDIDNAD------------ 63
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDiydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 -NIGFLIEHPKL-----YDNKSglYNLKLFAQVLGKGFDKAYTDKIIDAfGMRPYIKKKVKKYSM--GMKQKLAIAVSLM 135
Cdd:cd03260 81 rRVGMVFQKPNPfpgsiYDNVA--YGLRLHGIKLKEELDERVEEALRKA-ALWDEVKDRLHALGLsgGQQQRLCLARALA 157
|
170
....*....|....*.
gi 579496312 136 NKPKFLILDEPTNGMD 151
Cdd:cd03260 158 NEPEVLLLDEPTSALD 173
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-151 |
9.31e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIEhpKLYDNKSGLY 82
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ--KLYLDTTLPL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579496312 83 NLKLFAQvLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK09544 85 TVNRFLR-LRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-149 |
2.74e-16 |
|
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: 72.71 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKvDIDNAD-------NIGFL 68
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLpprsgsIRFDGE-DITGLPphriarlGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQVLGkgfDKAYTDKIID-AFGMRPYIKKKVKKY----SMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:COG0410 84 PEGRRIFPSLTVEENLLLGAYARR---DRAEVRADLErVYELFPRLKERRRQRagtlSGGEQQMLAIGRALMSRPKLLLL 160
|
....*.
gi 579496312 144 DEPTNG 149
Cdd:COG0410 161 DEPSLG 166
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-151 |
3.31e-16 |
|
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: 72.42 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIK--------FD---GKVDIdnAD---NIGF 67
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtygndvrlFGerrGGEDV--WElrkRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LieHPKLYDN-----------KSGLYN-LKLFAQVLGKgfDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLM 135
Cdd:COG1119 83 V--SPALQLRfprdetvldvvLSGFFDsIGLYREPTDE--QRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170
....*....|....*.
gi 579496312 136 NKPKFLILDEPTNGMD 151
Cdd:COG1119 159 KDPELLILDEPTAGLD 174
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-151 |
4.13e-16 |
|
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: 71.90 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD---------NIGFLIEH 71
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlppkdrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PKLYDNKSGLYN----LKLfaqvlgKGFDKAYTDK----IIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:cd03301 81 YALYPHMTVYDNiafgLKL------RKVPKDEIDErvreVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
....*...
gi 579496312 144 DEPTNGMD 151
Cdd:cd03301 155 DEPLSNLD 162
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-151 |
7.30e-16 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 71.38 E-value: 7.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKY----GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTT----IM---KVMNGNIIkFDGKvDIDNADN------ 64
Cdd:cd03257 3 EVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTlaraILgllKPTSGSII-FDGK-DLLKLSRrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 65 --------------------IGFLIEHP---KLYDNKSGLYNLKLFAQVLGKGFDKAYtdkiidaFGMRPYikkkvkKYS 121
Cdd:cd03257 81 rkeiqmvfqdpmsslnprmtIGEQIAEPlriHGKLSKKEARKEAVLLLLVGVGLPEEV-------LNRYPH------ELS 147
|
170 180 190
....*....|....*....|....*....|
gi 579496312 122 MGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALD 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-151 |
2.88e-15 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 71.47 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSN-----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKvDIDNAD------- 63
Cdd:COG1123 262 EVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrptsgsILFDGK-DLTKLSrrslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 -------------------NIGFLIEHPklydnksglynLKLFaQVLGKGFDKAYTDKIIDAFGMRPYIKkkvKKY---- 120
Cdd:COG1123 341 rrrvqmvfqdpysslnprmTVGDIIAEP-----------LRLH-GLLSRAERRERVAELLERVGLPPDLA---DRYphel 405
|
170 180 190
....*....|....*....|....*....|.
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-151 |
4.43e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGF---- 67
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDvthrsiqqrdiCMVFqsya 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNKSglYNLKLfaQVLGKGFDKAYTD---KIIDAFGMRpyiKKKVKKYSMGMKQKLAIAVSLMNKPKFLILD 144
Cdd:PRK11432 89 LFPHMSLGENVG--YGLKM--LGVPKEERKQRVKealELVDLAGFE---DRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
....*..
gi 579496312 145 EPTNGMD 151
Cdd:PRK11432 162 EPLSNLD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-151 |
4.75e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 25 DSRIVGLIGKNGVGKTTIMKVMNGNII----KFDGKVDIDNadnigfLIEHPK---LYDNKSGLYNLKLFA--------- 88
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPSWDE------VLKRFRgteLQNYFKKLYNGEIKVvhkpqyvdl 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579496312 89 ----------QVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13409 172 ipkvfkgkvrELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-151 |
7.35e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKV----------DIDNADNIGFLIEHPK 73
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqpvdagDIATRRRVGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 74 LYDNKSGLYNLKLFAQV--LGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:NF033858 350 LYGELTVRQNLELHARLfhLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-151 |
7.84e-15 |
|
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: 67.41 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSN--VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGkVDIDNAD------NIG 66
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdptsgeILIDG-VDLRDLDleslrkNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPKLYdNKSGLYNLklfaqvlgkgfdkaytdkiidafgmrpyikkkvkkYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
....*
gi 579496312 147 TNGMD 151
Cdd:cd03228 124 TSALD 128
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-151 |
8.67e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 70.20 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDF-GDSRIvGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIEH--PKLYDN 77
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLvPGSRI-GLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqlEFLRAD 391
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 78 KSGLYNLKLFAqvlgkgfDKAYTDKIIDAFGMRPYIKKKV----KKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK10636 392 ESPLQHLARLA-------PQELEQKLRDYLGGFGFQGDKVteetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-151 |
1.79e-14 |
|
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: 69.43 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 27 RIVGLIGKNGVGKTTIMKVMNGNII----KFDGKVDIDNAdnigflIEHPK---LYDNKSGLYNLKLFA----------- 88
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKpnlgDYDEEPSWDEV------LKRFRgteLQDYFKKLANGEIKVahkpqyvdlip 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579496312 89 --------QVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG1245 174 kvfkgtvrELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-151 |
2.16e-14 |
|
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: 67.61 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSN----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-------------- 63
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllsgkelrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 NIGFLIEHPKLYDNKSGLYNLKLFAQVLGKgfDKAYTDKIIDAF----GMrpyiKKKVKKY----SMGMKQKLAIAVSLM 135
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENVALPLEIAGV--PKAEIEERVLELlelvGL----EDKADAYpaqlSGGQKQRVGIARALA 156
|
170
....*....|....*.
gi 579496312 136 NKPKFLILDEPTNGMD 151
Cdd:cd03258 157 NNPKVLLCDEATSALD 172
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-151 |
2.46e-14 |
|
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: 67.36 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD---------NIGFLIEH 71
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDatdvpvqerNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PKL------YDNKS-GLyNLKLFAQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILD 144
Cdd:cd03296 83 YALfrhmtvFDNVAfGL-RVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
....*..
gi 579496312 145 EPTNGMD 151
Cdd:cd03296 162 EPFGALD 168
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-151 |
3.04e-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: 66.84 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 13 NVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGFLIEHPKLYdnkSG- 80
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqldpadlrrNIGYVPQDVTLF---YGt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 81 LY-NLKLFAQVlgkgfdkAYTDKIIDAF---GMRPYIKKKVKKYSM-----------GMKQKLAIAVSLMNKPKFLILDE 145
Cdd:cd03245 94 LRdNITLGAPL-------ADDERILRAAelaGVTDFVNKHPNGLDLqigergrglsgGQRQAVALARALLNDPPILLLDE 166
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:cd03245 167 PTSAMD 172
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-151 |
5.07e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.59 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGnIIKFD-GKVDIDNAD------------NIGFL 68
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVG-LVKPDsGRIFLDGEDithlpmhkrarlGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHP----KL--YDnksglyNLKLFAQVLGKGFD--KAYTDKIIDAFGmrpyIKKKVKKYSM----GMKQKLAIAVSLMN 136
Cdd:COG1137 84 PQEAsifrKLtvED------NILAVLELRKLSKKerEERLEELLEEFG----ITHLRKSKAYslsgGERRRVEIARALAT 153
|
170
....*....|....*
gi 579496312 137 KPKFLILDEPTNGMD 151
Cdd:COG1137 154 NPKFILLDEPFAGVD 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-151 |
6.58e-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: 67.73 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVlNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFLIEHP 72
Cdd:TIGR01257 934 LVKIFEPSGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDietnldavrqSLGMCPQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 73 KLYDNKSGLYNLKLFAQVLGKGFDKAY--TDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKGRSWEEAQleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
.
gi 579496312 151 D 151
Cdd:TIGR01257 1093 D 1093
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-151 |
6.60e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFLIEHP 72
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPvpararlaraRIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 73 KLYDNKSGLYNLKLFAQVLGKGFDK--AYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:PRK13536 124 NLDLEFTVRENLLVFGRYFGMSTREieAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
.
gi 579496312 151 D 151
Cdd:PRK13536 204 D 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-151 |
7.95e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.03 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKV----DIDNADNIGFliehpkLYDNKSGLY--- 82
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILvptsgeVRVLGYVpfkrRKEFARRIGV------VFGQRSQLWwdl 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 83 ----NLKLFAQVLG---KGFDKAYtDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG4586 112 paidSFRLLKAIYRipdAEYKKRL-DELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-151 |
9.61e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----------NIGFLIE 70
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpsrarharqRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 HPKLYDNKSGLYNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGlsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
...
gi 579496312 149 GMD 151
Cdd:PRK13537 168 GLD 170
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-151 |
2.05e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYG--SNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDI----------DNADNIGFL 68
Cdd:TIGR01257 1938 LRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagksiltnisDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQVlgKGFDKAYTDKI----IDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILD 144
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARL--RGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
....*..
gi 579496312 145 EPTNGMD 151
Cdd:TIGR01257 2096 EPTTGMD 2102
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-151 |
2.22e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITkkyGSNVvlNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN------------ADNIGFL 68
Cdd:PRK10762 258 LKVDNLS---GPGV--NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdglANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPK---------LYDNKSgLYNLKLFAQVLGK---GFDKAYTDKIIDAFGMR-PYIKKKVKKYSMGMKQKLAIAVSLM 135
Cdd:PRK10762 333 SEDRKrdglvlgmsVKENMS-LTALRYFSRAGGSlkhADEQQAVSDFIRLFNIKtPSMEQAIGLLSGGNQQKVAIARGLM 411
|
170
....*....|....*.
gi 579496312 136 NKPKFLILDEPTNGMD 151
Cdd:PRK10762 412 TRPKVLILDEPTRGVD 427
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-150 |
2.75e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG--------NIIKFDGK----VDIDNADNIGFL 68
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdGEIYWSGSplkaSNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPK--LYDNKSGLYNLKLFAQVLGKGFDKAYTDKIIDAFGMRPYIK-------KKVKKYSMGMKQKLAIAVSLMNKPK 139
Cdd:TIGR02633 82 IIHQEltLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQldadnvtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170
....*....|.
gi 579496312 140 FLILDEPTNGM 150
Cdd:TIGR02633 162 LLILDEPSSSL 172
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-151 |
2.87e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 65.69 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 11 GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI---------IKFDGKvDIDNAD------NIGFLIEHPKLY 75
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggrisgeVLLDGR-DLLELSealrgrRIGMVFQDPMTQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579496312 76 DNKSGLYNLKLFAQVLGKGFDKAYTDKIIDAF---GMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG1123 96 LNPVTVGDQIAEALENLGLSRAEARARVLELLeavGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-151 |
3.43e-13 |
|
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: 64.43 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSN--VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGFLI 69
Cdd:cd03252 3 FEHVRFRYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlaladpawlrrQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 EHPKLYdNKSGLYNLKLfaqvlgkGFDKAYTDKIIDAF---GMRPYIKKKVKKY-----------SMGMKQKLAIAVSLM 135
Cdd:cd03252 83 QENVLF-NRSIRDNIAL-------ADPGMSMERVIEAAklaGAHDFISELPEGYdtivgeqgaglSGGQRQRIAIARALI 154
|
170
....*....|....*.
gi 579496312 136 NKPKFLILDEPTNGMD 151
Cdd:cd03252 155 HNPRILIFDEATSALD 170
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-151 |
3.71e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD------------NIGFL 68
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisllplhararrGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQV---LGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrddLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:PRK10895 164 PFAGVD 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-150 |
3.75e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD------------NIGFL 68
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhklaaqlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNL--------KLFA-QVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPK 139
Cdd:PRK09700 86 YQELSVIDELTVLENLyigrhltkKVCGvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170
....*....|.
gi 579496312 140 FLILDEPTNGM 150
Cdd:PRK09700 166 VIIMDEPTSSL 176
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-151 |
7.70e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.33 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLE--HITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM------NGNIIKFDGKvDIDNAD----NIGFL 68
Cdd:PRK10851 1 MSIEiaNIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqTSGHIRFHGT-DVSRLHardrKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLklfaqvlgkgfdkaytdkiidAFGM-------RP---YIKKKVKK-----------------YS 121
Cdd:PRK10851 80 FQHYALFRHMTVFDNI---------------------AFGLtvlprreRPnaaAIKAKVTQllemvqlahladrypaqLS 138
|
170 180 190
....*....|....*....|....*....|
gi 579496312 122 MGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-151 |
1.15e-12 |
|
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: 61.85 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYG--SNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADnigfliehpklydnkSG 80
Cdd:cd03246 3 VENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD---------------IS 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579496312 81 LYNLKLFAQVLG------KGFDKAYTDKIIdafgmrpyikkkvkkySMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03246 68 QWDPNELGDHVGylpqddELFSGSIAENIL----------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-151 |
1.87e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN-------GNII----KFDGKVDIDNAD------ 63
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNllemprsGTLNiagnHFDFSKTPSDKAirelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 NIGFLIEHPKLYDNKSGLYNL-KLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKF 140
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLiEAPCRVLGlsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170
....*....|.
gi 579496312 141 LILDEPTNGMD 151
Cdd:PRK11124 163 LLFDEPTAALD 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-151 |
1.94e-12 |
|
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: 62.32 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSN-VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKvDIDNAD------NIGFL 68
Cdd:cd03295 2 EFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIeptsgeIFIDGE-DIREQDpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPyiKKKVKKY----SMGMKQKLAIAVSLMNKPKFLI 142
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKwpKEKIRERADELLALVGLDP--AEFADRYphelSGGQQQRVGVARALAADPPLLL 158
|
....*....
gi 579496312 143 LDEPTNGMD 151
Cdd:cd03295 159 MDEPFGALD 167
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-151 |
2.17e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.42 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 6 ITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN-------GNIIkFDG-KVDIDNAD------NIGFLIEH 71
Cdd:PRK09493 7 VSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINkleeitsGDLI-VDGlKVNDPKVDerlirqEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PKLYDNKSGLYNLkLFAQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKY----SMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:PRK09493 86 FYLFPHLTALENV-MFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYpselSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
....
gi 579496312 148 NGMD 151
Cdd:PRK09493 165 SALD 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-147 |
2.30e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG--------NIIKFDGKV----DIDNADNIGFL 68
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyeGEIIFEGEElqasNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKL--YDNKSGLYNLKLFAQVLGKG---FDKAY--TDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFL 141
Cdd:PRK13549 86 IIHQELalVKELSVLENIFLGNEITPGGimdYDAMYlrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
....*.
gi 579496312 142 ILDEPT 147
Cdd:PRK13549 166 ILDEPT 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-151 |
2.32e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.04 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGF---- 67
Cdd:PRK09452 17 LRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvpaenrhvNTVFqsya 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNKSglYNLKLfaQVLGKgfdKAYTDKIIDAFGM---RPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILD 144
Cdd:PRK09452 97 LFPHMTVFENVA--FGLRM--QKTPA---AEITPRVMEALRMvqlEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
....*..
gi 579496312 145 EPTNGMD 151
Cdd:PRK09452 170 ESLSALD 176
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-150 |
2.51e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGN------IIKFDGKvDIDN-------ADNIGF 67
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDpratsgRIVFDGK-DITDwqtakimREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNKSGLYNLKL---FAQvlgkgfDKAYTDKIIDAFGMRPYI-KKKVKK---YSMGMKQKLAIAVSLMNKPKF 140
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMggfFAE------RDQFQERIKWVYELFPRLhERRIQRagtMSGGEQQMLAIGRALMSQPRL 158
|
170
....*....|
gi 579496312 141 LILDEPTNGM 150
Cdd:PRK11614 159 LLLDEPSLGL 168
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-151 |
2.55e-12 |
|
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: 62.28 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD---------------NIGFL 68
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrkelrelrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYN--LKLFAQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:cd03294 108 FQSFALLPHRTVLENvaFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
....*
gi 579496312 147 TNGMD 151
Cdd:cd03294 188 FSALD 192
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-151 |
3.23e-12 |
|
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: 62.65 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 5 HITKKYGSN-VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIEHPKLYDNKSGLYN 83
Cdd:TIGR03719 9 RVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 84 LKLFAQVLGKGFDK------AYTD----------------KIIDAFG--------------MR-PYIKKKVKKYSMGMKQ 126
Cdd:TIGR03719 89 VEEGVAEIKDALDRfneisaKYAEpdadfdklaaeqaelqEIIDAADawdldsqleiamdaLRcPPWDADVTKLSGGERR 168
|
170 180
....*....|....*....|....*
gi 579496312 127 KLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
11-151 |
3.34e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.43 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 11 GSNVVLNDIDFDFGDSRIVGLIGKNGVGKT-TIMKVM-----NGNI---IKFDGKvDIDN----------ADNIGFLIEH 71
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMgllaaNGRIggsATFNGR-EILNlpekelnklrAEQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PKLYDNKsglYnLKLFAQV-----LGKGFDK--AYTD--KIIDAFGMrPYIKKKVKKY----SMGMKQKLAIAVSLMNKP 138
Cdd:PRK09473 106 PMTSLNP---Y-MRVGEQLmevlmLHKGMSKaeAFEEsvRMLDAVKM-PEARKRMKMYphefSGGMRQRVMIAMALLCRP 180
|
170
....*....|...
gi 579496312 139 KFLILDEPTNGMD 151
Cdd:PRK09473 181 KLLIADEPTTALD 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-151 |
4.28e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.69 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN------GNIIKFdGKVDIDNA------------ 62
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeAGTIRV-GDITIDTArslsqqkglirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 63 --DNIGFLIEHPKLYDNKSGLYNLkLFAQVLGKGFDK----AYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMN 136
Cdd:PRK11264 83 lrQHVGFVFQNFNLFPHRTVLENI-IEGPVIVKGEPKeeatARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170
....*....|....*
gi 579496312 137 KPKFLILDEPTNGMD 151
Cdd:PRK11264 162 RPEVILFDEPTSALD 176
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-145 |
7.22e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.83 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGS--------------------NVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID 60
Cdd:PRK13545 5 VKFEHVTKKYKMynkpfdklkdlffrskdgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 61 NAdniGFLIEHPKLYDNK-SGLYNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNK 137
Cdd:PRK13545 85 GS---AALIAISSGLNGQlTGIENIELKGLMMGltKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHIN 161
|
....*...
gi 579496312 138 PKFLILDE 145
Cdd:PRK13545 162 PDILVIDE 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-151 |
7.48e-12 |
|
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: 61.87 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIE-HPKLYDNKSgly 82
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsRDALDPNKT--- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 83 nlklFAQVLGKGFD-----------KAYtdkiIDAFGMR-PYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:TIGR03719 403 ----VWEEISGGLDiiklgkreipsRAY----VGRFNFKgSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
.
gi 579496312 151 D 151
Cdd:TIGR03719 475 D 475
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-151 |
8.86e-12 |
|
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: 61.36 E-value: 8.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGS---NVV--LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADN----------- 64
Cdd:TIGR03269 280 IKVRNVSKRYISvdrGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEwvdmtkpgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 65 -------IGFLIEHPKLYDNKSGLYNL---------------KLFAQVLGKGFDKAYTDKIIDafgmrpyikKKVKKYSM 122
Cdd:TIGR03269 360 rgrakryIGILHQEYDLYPHRTVLDNLteaiglelpdelarmKAVITLKMVGFDEEKAEEILD---------KYPDELSE 430
|
170 180
....*....|....*....|....*....
gi 579496312 123 GMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-151 |
8.98e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN-----GNIIKFDGKVDIDNAD------NIGFL- 68
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmnelESEVRVEGRVEFFNQNiyerrvNLNRLr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 ----IEHPK-------LYDNKSglYNLKLFAQVLGKGFDKAYTDKIIDAfGMRPYIKKKVKKYSM----GMKQKLAIAVS 133
Cdd:PRK14258 88 rqvsMVHPKpnlfpmsVYDNVA--YGVKIVGWRPKLEIDDIVESALKDA-DLWDEIKHKIHKSALdlsgGQQQRLCIARA 164
|
170
....*....|....*...
gi 579496312 134 LMNKPKFLILDEPTNGMD 151
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLD 182
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-151 |
1.09e-11 |
|
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: 60.11 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVV-LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD--------------NIGF 67
Cdd:cd03292 3 FINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrgraipylrrKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNKSGLYNLKLFAQVLGKGfDKAYTDKIIDAF---GMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILD 144
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVP-PREIRKRVPAALelvGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
....*..
gi 579496312 145 EPTNGMD 151
Cdd:cd03292 162 EPTGNLD 168
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-151 |
1.42e-11 |
|
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: 60.04 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGsNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGnIIKFD-GKVDIDNAD---------NIGF--- 67
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAG-FIKPDsGKILLNGKDitnlppekrDISYvpq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 ---LIEHPKLYDNKSglYNLKLfaQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILD 144
Cdd:cd03299 79 nyaLFPHMTVYKNIA--YGLKK--RKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
....*..
gi 579496312 145 EPTNGMD 151
Cdd:cd03299 155 EPFSALD 161
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-151 |
2.21e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 12 SNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD------------NIGFLIEHPklyDNK- 78
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirnKAGMVFQNP---DNQi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 79 ----------SGLYNLKLFAQVLGKGFDKAytdkiIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:PRK13633 99 vativeedvaFGPENLGIPPEEIRERVDES-----LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
...
gi 579496312 149 GMD 151
Cdd:PRK13633 174 MLD 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-151 |
5.11e-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: 58.57 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 22 DFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNaDNIGFLIEHPKLyDNKSGLYNLkLFAQVLGKGFDKAYTD 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL-DTVSYKPQYIKA-DYEGTVRDL-LSSITKDFYTHPYFKT 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 579496312 102 KIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03237 98 EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-151 |
6.06e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.46 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYG--SNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID----NADN-------IGFL 68
Cdd:PRK13632 9 KVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitiSKENlkeirkkIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPklyDNKS-----------GLYNLKLFAQVLgkgfdKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNK 137
Cdd:PRK13632 89 FQNP---DNQFigatveddiafGLENKKVPPKKM-----KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170
....*....|....
gi 579496312 138 PKFLILDEPTNGMD 151
Cdd:PRK13632 161 PEIIIFDESTSMLD 174
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-151 |
6.74e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 58.69 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGF-- 67
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlshvppyqrpiNMMFqs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 --LIEHPKLYDNKSglYNLKlfAQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:PRK11607 100 yaLFPHMTVEQNIA--FGLK--QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:PRK11607 176 PMGALD 181
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-151 |
1.07e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.94 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNA-------------DNIG 66
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklrESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHP-------KLYDNKS-GLYNLKLFAQVLGKgfdkaYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKP 138
Cdd:PRK13636 86 MVFQDPdnqlfsaSVYQDVSfGAVNLKLPEDEVRK-----RVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170
....*....|...
gi 579496312 139 KFLILDEPTNGMD 151
Cdd:PRK13636 161 KVLVLDEPTAGLD 173
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-151 |
1.41e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIE-HPKLYDNksgl 81
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDFEN---- 397
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 82 yNLKLF---AQVLGKGFDkaytDKIIDAFGMRPY-----IKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK15064 398 -DLTLFdwmSQWRQEGDD----EQAVRGTLGRLLfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-151 |
1.54e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 9 KYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKV-----DIDNA--------DNIGFLIEHPK-- 73
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkPLDYSkrgllalrQQVATVFQDPEqq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 74 -LY-----DNKSGLYNLKLFAQVLGKGFDKAYTdkIIDAFGMRpyiKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:PRK13638 90 iFYtdidsDIAFSLRNLGVPEAEITRRVDEALT--LVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
....
gi 579496312 148 NGMD 151
Cdd:PRK13638 165 AGLD 168
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
16-151 |
2.03e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 56.71 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDnadniGFLIEHPK-----LYDNKSGLYNLKLFAQV 90
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-----GKQITEPGpdrmvVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579496312 91 ----------LGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR01184 76 alavdrvlpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-151 |
5.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.85 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 14 VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAdnigfliehPKLYDNKSGLYNLK-------- 85
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE---------PIKYDKKSLLEVRKtvgivfqn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 86 ----LFAQV---------LGKGFDKAYTDK----IIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:PRK13639 87 pddqLFAPTveedvafgpLNLGLSKEEVEKrvkeALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
...
gi 579496312 149 GMD 151
Cdd:PRK13639 167 GLD 169
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-151 |
5.24e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.84 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNA------DNIGFLIEHPKLYD 76
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaearEDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579496312 77 NKSGLYNLKLfaQVLGKGFDKAYtdKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11247 95 WKKVIDNVGL--GLKGQWRDAAL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-145 |
5.38e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.98 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGkvDIDNADNIGFLIEHPKLYDNKSGLYNLKLfaQVLGKGF 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG--KVDRNGEVSVIAISAGLSGQLTGIENIEF--KMLCMGF 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 579496312 96 D----KAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:PRK13546 116 KrkeiKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-151 |
6.53e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK-VDIDNADNiGFLIEHPK 73
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVpyqhgsITLDGKpVEGPGAER-GVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 74 LYDNKSGLYNLKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-151 |
7.61e-10 |
|
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: 54.08 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 12 SNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIEHPKLYDNksglyNLKlfaQVL 91
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLG-----TLR---EQL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579496312 92 gkgfdkAYT-DKIIdafgmrpyikkkvkkySMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03223 85 ------IYPwDDVL----------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
15-151 |
8.42e-10 |
|
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: 55.44 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMK-VMN---------GNIIkFDGKvDIDNADN-------------------- 64
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARaILGllpppgitsGEIL-FDGE-DLLKLSEkelrkirgreiqmifqdpmt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 65 -------IGFLIEHPklydnksglynLKLFaQVLGKgfdKAYTDKIIDAF---GMrPYIKKKVKKY----SMGMKQKLAI 130
Cdd:COG0444 98 slnpvmtVGDQIAEP-----------LRIH-GGLSK---AEARERAIELLervGL-PDPERRLDRYphelSGGMRQRVMI 161
|
170 180
....*....|....*....|.
gi 579496312 131 AVSLMNKPKFLILDEPTNGMD 151
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD 182
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-151 |
9.10e-10 |
|
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: 54.97 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI---------IKFDGK-VDIDN-ADNIGFL----IEHPKLYDNKS 79
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegggttsgqILFNGQpRKPDQfQKCVAYVrqddILLPGLTVRET 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579496312 80 GLYNLKLfaqVLGKGFDKAYTDKIIDAFGMR-----PYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03234 102 LTYTAIL---RLPRKSSDAIRKKRVEDVLLRdlaltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-151 |
9.19e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 55.56 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGkVDIDNAD------NIGFLI 69
Cdd:COG1132 342 FENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYdptsgrILIDG-VDIRDLTleslrrQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 EHPKLYdnkSG--LYNLKLfaqvlgkGFDKAYTDKIIDAF---GMRPYIKKKVKKY-----------SMGMKQKLAIAVS 133
Cdd:COG1132 421 QDTFLF---SGtiRENIRY-------GRPDATDEEVEEAAkaaQAHEFIEALPDGYdtvvgergvnlSGGQRQRIAIARA 490
|
170
....*....|....*...
gi 579496312 134 LMNKPKFLILDEPTNGMD 151
Cdd:COG1132 491 LLKDPPILILDEATSALD 508
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-151 |
9.60e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 7 TKKYGSN-VVLNDIDFDF-GDSRIvGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIEHPKLYDNKSGLYN- 83
Cdd:PRK11819 13 SKVVPPKkQILKDISLSFfPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 84 ----------LKLFAQVLGK-GFDKAYTDK----------IIDAFG--------------MR-PYIKKKVKKYSMGMKQK 127
Cdd:PRK11819 92 eegvaevkaaLDRFNEIYAAyAEPDADFDAlaaeqgelqeIIDAADawdldsqleiamdaLRcPPWDAKVTKLSGGERRR 171
|
170 180
....*....|....*....|....
gi 579496312 128 LAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-151 |
1.00e-09 |
|
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: 54.24 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSN--VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN----------ADNIGFLIE 70
Cdd:cd03247 3 INNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 HPKLYDnksglynlklfaqvlgkgfdkaytDKIIDAFGMRpyikkkvkkYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:cd03247 83 RPYLFD------------------------TTLRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
.
gi 579496312 151 D 151
Cdd:cd03247 130 D 130
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-151 |
1.20e-09 |
|
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: 54.54 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGFLIEHPKLYdNKSGLYN 83
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdisrkslrsMIGVVLQDTFLF-SGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 84 LKLfaqvlgkGFDKAYTDKIIDAF---GMRPYIKKKVKKY-----------SMGMKQKLAIAVSLMNKPKFLILDEPTNG 149
Cdd:cd03254 97 IRL-------GRPNATDEEVIEAAkeaGAHDFIMKLPNGYdtvlgenggnlSQGERQLLAIARAMLRDPKILILDEATSN 169
|
..
gi 579496312 150 MD 151
Cdd:cd03254 170 ID 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-151 |
1.33e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG----------------NIIKFDGKV--DIDNA 62
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitgdksagshiellgRTVQREGRLarDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 63 D-NIGFLIEHPKLYDNKSGLYNLKL-------FAQVLGKGFDKAYTDKIIDAF---GMRPYIKKKVKKYSMGMKQKLAIA 131
Cdd:PRK09984 85 RaNTGYIFQQFNLVNRLSVLENVLIgalgstpFWRTCFSWFTREQKQRALQALtrvGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180
....*....|....*....|
gi 579496312 132 VSLMNKPKFLILDEPTNGMD 151
Cdd:PRK09984 165 RALMQQAKVILADEPIASLD 184
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-151 |
1.33e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 55.08 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSN----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN-------GNIIkFDGkVDIDNAD------- 63
Cdd:COG1135 3 ELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINllerptsGSVL-VDG-VDLTALSerelraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 --NIGFLIEHPKLYDNKSGLYN----LKLfaqvlgKGFDKAYtdkiidafgmrpyIKKKV-------------KKY---- 120
Cdd:COG1135 81 rrKIGMIFQHFNLLSSRTVAENvalpLEI------AGVPKAE-------------IRKRVaellelvglsdkaDAYpsql 141
|
170 180 190
....*....|....*....|....*....|.
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-151 |
1.84e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 54.25 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKY--GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKV-------DI-------- 59
Cdd:PRK13635 8 VEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlpeagtITVGGMVlseetvwDVrrqvgmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 60 DNADN--IGFLIEHpklyDNKSGLYNLKLFAQVLGKGFDKAytdkiIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNK 137
Cdd:PRK13635 88 QNPDNqfVGATVQD----DVAFGLENIGVPREEMVERVDQA-----LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170
....*....|....
gi 579496312 138 PKFLILDEPTNGMD 151
Cdd:PRK13635 159 PDIIILDEATSMLD 172
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-151 |
1.91e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.65 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG--NI----IKFDGKV--DIDNAD-NIGF------ 67
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDItsgdLFIGEKRmnDVPPAErGVGMvfqsya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNKSglYNLKLfaqvlgKGFDKAYTDKIIDAFG----MRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:PRK11000 86 LYPHLSVAENMS--FGLKL------AGAKKEEINQRVNQVAevlqLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
....*...
gi 579496312 144 DEPTNGMD 151
Cdd:PRK11000 158 DEPLSNLD 165
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-151 |
2.00e-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: 53.57 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNV--VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADnigflIEHPKLYDNK 78
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID-----ISTIPLEDLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579496312 79 SGL----YNLKLFAQVLGKGFDK--AYTDKIIDAfGMRpyIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03369 82 SSLtiipQDPTLFSGTIRSNLDPfdEYSDEEIYG-ALR--VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-151 |
2.48e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 10 YGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN-----------------------ADNIG 66
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdpprnvegtvydfvAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPKLYDNKSGLY-------NLKLFAQVLGK-------GFDKAYTDkIIDAFGMRPyiKKKVKKYSMGMKQKLAIAV 132
Cdd:PRK11147 93 EQAEYLKRYHDISHLVetdpsekNLNELAKLQEQldhhnlwQLENRINE-VLAQLGLDP--DAALSSLSGGWLRKAALGR 169
|
170
....*....|....*....
gi 579496312 133 SLMNKPKFLILDEPTNGMD 151
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLD 188
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-63 |
2.83e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.62 E-value: 2.83e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD 63
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP 65
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-151 |
3.35e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 10 YGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN--GNI---------IKFDG------KVD-IDNADNIGFLIEH 71
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLnpevtitgsIVYNGhniyspRTDtVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PK-----LYDNKsgLYNLKLfaqvlgKGF-DKAYTDKIIDAFGMRPYIKKKVKKY--------SMGMKQKLAIAVSLMNK 137
Cdd:PRK14239 95 PNpfpmsIYENV--VYGLRL------KGIkDKQVLDEAVEKSLKGASIWDEVKDRlhdsalglSGGQQQRVCIARVLATS 166
|
170
....*....|....
gi 579496312 138 PKFLILDEPTNGMD 151
Cdd:PRK14239 167 PKIILLDEPTSALD 180
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-151 |
4.29e-09 |
|
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: 53.76 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKY--GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNgNIIKFDGKVDIDNA--DNIGFliehpKLYD 76
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVswNSVTL-----QTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 77 NKSGLYNLKLFaqVLGKGFDK------AYTD----KIIDAFGMRPYIKKKVKKY-----------SMGMKQKLAIAVSLM 135
Cdd:TIGR01271 1292 KAFGVIPQKVF--IFSGTFRKnldpyeQWSDeeiwKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSIL 1369
|
170
....*....|....*.
gi 579496312 136 NKPKFLILDEPTNGMD 151
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLD 1385
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-151 |
4.82e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.07 E-value: 4.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG------NIIKFDGKvdiDNADNIGFLI----- 69
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfykptgGTILLRGQ---HIEGLPGHQIarmgv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 ----EHPKLYDNKSGLYNLkLFAQ-------VLG-----KGFDKAYTDKI------IDAFGMRPYIKKKVKKYSMGMKQK 127
Cdd:PRK11300 83 vrtfQHVRLFREMTVIENL-LVAQhqqlktgLFSgllktPAFRRAESEALdraatwLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180
....*....|....*....|....
gi 579496312 128 LAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLN 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-151 |
5.65e-09 |
|
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: 52.62 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGS--NVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVmngnIIKF----DGKVDIDNADNIGF----LIEHP 72
Cdd:cd03251 3 FKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNL----IPRFydvdSGRILIDGHDVRDYtlasLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 73 KLYDNKSGLYNLKLFAQVLgKGFDKAYTDKIIDA--------FGMR------PYIKKKVKKYSMGMKQKLAIAVSLMNKP 138
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIA-YGRPGATREEVEEAaraanaheFIMElpegydTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170
....*....|...
gi 579496312 139 KFLILDEPTNGMD 151
Cdd:cd03251 158 PILILDEATSALD 170
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-151 |
7.00e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.10 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYgsnvVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK-VDIDN-----ADNIGFL 68
Cdd:COG1129 257 LEVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADpadsgeIRLDGKpVRIRSprdaiRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEhpklyDNKS-GL-------YNLKL--FAQVLGKGF-----DKAYTDKIIDAFGMR-PYIKKKVKKYSMGMKQKLAIAV 132
Cdd:COG1129 333 PE-----DRKGeGLvldlsirENITLasLDRLSRGGLldrrrERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAK 407
|
170
....*....|....*....
gi 579496312 133 SLMNKPKFLILDEPTNGMD 151
Cdd:COG1129 408 WLATDPKVLILDEPTRGID 426
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-151 |
7.99e-09 |
|
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: 52.37 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 25 DSRIVGLIGKNGVGKTTIMKVMNG----NIIKFDGKVDID------------------------------NADNIgflie 70
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpNLGKFDDPPDWDeildefrgselqnyftkllegdvkvivkpqYVDLI----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 hPKLYDNKSGlynlklfaQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:cd03236 100 -PKAVKGKVG--------ELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
.
gi 579496312 151 D 151
Cdd:cd03236 171 D 171
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-151 |
8.33e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKY--GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNgNIIKFD-GKVDIDNADNIGF---------- 67
Cdd:PLN03232 1235 IKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF-RIVELEkGRIMIDDCDVAKFgltdlrrvls 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 -LIEHPKLYdnkSGL--YNLKLFAQV----LGKGFDKAYTDKIID--AFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKP 138
Cdd:PLN03232 1314 iIPQSPVLF---SGTvrFNIDPFSEHndadLWEALERAHIKDVIDrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
170
....*....|...
gi 579496312 139 KFLILDEPTNGMD 151
Cdd:PLN03232 1391 KILVLDEATASVD 1403
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-151 |
9.50e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.54 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 10 YGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID-------NADNIGFLIEH-PKlydNKSGL 81
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealSARAASRRVASvPQ---DTSLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 82 YNLKLFAQV-LGK-----------GFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNG 149
Cdd:PRK09536 90 FEFDVRQVVeMGRtphrsrfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
..
gi 579496312 150 MD 151
Cdd:PRK09536 170 LD 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-151 |
1.23e-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: 51.85 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM------NGNIIKFDGkVDIDNAD------NIGFLI 69
Cdd:cd03253 3 FENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrfydvSSGSILIDG-QDIREVTldslrrAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 EHPKLYdNKSGLYNLKLfaqvlgkGFDKAYTDKIIDAF---GMRPYIKKKVKKY-----------SMGMKQKLAIAVSLM 135
Cdd:cd03253 82 QDTVLF-NDTIGYNIRY-------GRPDATDEEVIEAAkaaQIHDKIMRFPDGYdtivgerglklSGGEKQRVAIARAIL 153
|
170
....*....|....*.
gi 579496312 136 NKPKFLILDEPTNGMD 151
Cdd:cd03253 154 KNPPILLLDEATSALD 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-151 |
1.23e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.94 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN-----------ADNIGFLI 69
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 EHP---------KLYDNKSGLYnLKLFAQVLGKgfDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKF 140
Cdd:PRK11231 83 QHHltpegitvrELVAYGRSPW-LSLWGRLSAE--DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170
....*....|.
gi 579496312 141 LILDEPTNGMD 151
Cdd:PRK11231 160 VLLDEPTTYLD 170
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-151 |
1.36e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 52.11 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG---------NIIKFDG-----KVDIDNADNIGFLIEHPklyDNKS- 79
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpnSKITVDGitltaKTVWDIREKVGIVFQNP---DNQFv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 80 ----------GLYNLKLFAQVLGKGFDKAYTDkiidaFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNG 149
Cdd:PRK13640 99 gatvgddvafGLENRAVPRPEMIKIVRDVLAD-----VGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
..
gi 579496312 150 MD 151
Cdd:PRK13640 174 LD 175
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-151 |
1.36e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.77 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 10 YGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN-----GNIIKFDGKV-----DIDNAD--------NIGFLIEH 71
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVrlfgrNIYSPDvdpievrrEVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PK------LYDNKSglYNLKLFAQVLGKGFDKAYTDKIIDAFGMRPYIKKKVKKY----SMGMKQKLAIAVSLMNKPKFL 141
Cdd:PRK14267 94 PNpfphltIYDNVA--IGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDYpsnlSGGQRQRLVIARALAMKPKIL 171
|
170
....*....|
gi 579496312 142 ILDEPTNGMD 151
Cdd:PRK14267 172 LMDEPTANID 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-151 |
1.47e-08 |
|
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: 51.34 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 11 GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN----------ADNIGFLIEHPKLYDNKSG 80
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqrdsiARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579496312 81 LYNLKLFAQVLGkgfdkayTDKIIDAF---GMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03231 91 LENLRFWHADHS-------DEQVEEALarvGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-151 |
1.74e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID----NADN-------IGFLIEHPKLY--------D 76
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDgellTAENvwnlrrkIGMVFQNPDNQfvgatvedD 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579496312 77 NKSGLYNLKLFAQVLGKGFDKAytdkiIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEA-----LLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-151 |
1.86e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKV-----DIDNADNI------GFLIEHPKLYDN 77
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVlyfgkDIFQIDAIklrkevGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 78 KSGLYNLKLFAQVLGKGfDKAYTDKIIDAFGMRPYIKKKV--------KKYSMGMKQKLAIAVSLMNKPKFLILDEPTNG 149
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIK-EKREIKKIVEECLRKVGLWKEVydrlnspaSQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
..
gi 579496312 150 MD 151
Cdd:PRK14246 184 ID 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-151 |
1.86e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIE-HPKLYDNKS--- 79
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQsRDALDPNKTvwe 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 80 ----GLYNLKlfaqvLGKgFD---KAYtdkiIDAFGMR-PYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11819 408 eisgGLDIIK-----VGN-REipsRAY----VGRFNFKgGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-151 |
1.88e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.59 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKY--GS---NVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGfliEHPKLY 75
Cdd:PRK13637 3 IKIENLTHIYmeGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD---KKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 76 D--NKSGLY----NLKLFAQVLGKGFdkaytdkiidAFGMRPY------IKKKVKK-------------------YSMGM 124
Cdd:PRK13637 80 DirKKVGLVfqypEYQLFEETIEKDI----------AFGPINLglseeeIENRVKRamnivgldyedykdkspfeLSGGQ 149
|
170 180
....*....|....*....|....*..
gi 579496312 125 KQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-151 |
1.95e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNadnigfliEHPKLYDNKSGLYN 83
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG--------EHIQHYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 84 LKLFAQ------------VLGKGF-------------DKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKP 138
Cdd:PRK10253 83 IGLLAQnattpgditvqeLVARGRyphqplftrwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170
....*....|...
gi 579496312 139 KFLILDEPTNGMD 151
Cdd:PRK10253 163 AIMLLDEPTTWLD 175
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
11-151 |
2.08e-08 |
|
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: 50.82 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 11 GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN----------ADNIGFLIEHPKLYDNKSG 80
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579496312 81 LYNLKLFAQVLGkgfdkaYTDKII----DAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR01189 91 LENLHFWAAIHG------GAQRTIedalAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-151 |
2.25e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.03 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKY-GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKV-----DIDNADN---------I 65
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITRLKNrevpflrrqI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 66 GFLIEHPKLYDNKSGLYNLKLFAQVLGKGFD--KAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLIL 143
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDdiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
....*...
gi 579496312 144 DEPTNGMD 151
Cdd:PRK10908 162 DEPTGNLD 169
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-151 |
2.55e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 51.34 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSN----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN-------GNIIkFDGkVDI---DNAD---- 63
Cdd:PRK11153 3 ELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINllerptsGRVL-VDG-QDLtalSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 --NIGFLIEHPKL------YDNKSglynLKLFAQVLGKGFDKAYTDKIIDAFGmrpyIKKKVKKY----SMGMKQKLAIA 131
Cdd:PRK11153 81 rrQIGMIFQHFNLlssrtvFDNVA----LPLELAGTPKAEIKARVTELLELVG----LSDKADRYpaqlSGGQKQRVAIA 152
|
170 180
....*....|....*....|
gi 579496312 132 VSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11153 153 RALASNPKVLLCDEATSALD 172
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-151 |
2.55e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSN-----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKV---DIDNADNIGFliEHP 72
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgDIYIGDKKNN--HEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 73 KLYDNKSGLYNLKLFAQVLGKGFD-------KAYTDKIID----AFGMRPY-IKKKVKKY------------------SM 122
Cdd:PRK13631 100 ITNPYSKKIKNFKELRRRVSMVFQfpeyqlfKDTIEKDIMfgpvALGVKKSeAKKLAKFYlnkmglddsylerspfglSG 179
|
170 180
....*....|....*....|....*....
gi 579496312 123 GMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLD 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-151 |
3.04e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.89 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSN---VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN----ADN-------IG 66
Cdd:PRK13650 5 IEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdlltEENvwdirhkIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPklyDNKS-----------GLYNLKLFAQVLGKGFDKAytdkiIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLM 135
Cdd:PRK13650 85 MVFQNP---DNQFvgatveddvafGLENKGIPHEEMKERVNEA-----LELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170
....*....|....*.
gi 579496312 136 NKPKFLILDEPTNGMD 151
Cdd:PRK13650 157 MRPKIIILDEATSMLD 172
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-151 |
4.04e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.58 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG----------------NIIKFDGKVDIDNADnIGFLIEHPKLYDNK 78
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGldtptsgdvifngqpmSKLSSAAKAELRNQK-LGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579496312 79 SGLYNLKLFAQVLGKGFDKAYTD--KIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRalEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
79-151 |
5.20e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 5.20e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579496312 79 SGLYNLKLFAQVL--GKGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:NF000106 102 SGRENLYMIGR*LdlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-151 |
5.32e-08 |
|
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: 50.23 E-value: 5.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVmngnIIKF----DGKVDIDNADN-----------IGFLIEHPKLYDNkS 79
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSL----LERFydptSGEILLDGVDIrdlnlrwlrsqIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 80 GLYNLKLfaqvlgkGFDKAYTDKIIDAFGM---RPYIKKKVKKY-----------SMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:cd03249 93 IAENIRY-------GKPDATDEEVEEAAKKaniHDFIMSLPDGYdtlvgergsqlSGGQKQRIAIARALLRNPKILLLDE 165
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:cd03249 166 ATSALD 171
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1-151 |
5.41e-08 |
|
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: 49.80 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKY--GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGF 67
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskiglhdlrsRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYdnkSGL--YNLKLFAQvlgkgfdkaYTD-KIIDAF---GMRPYIKKKVKK-----------YSMGMKQKLAI 130
Cdd:cd03244 83 IPQDPVLF---SGTirSNLDPFGE---------YSDeELWQALervGLKEFVESLPGGldtvveeggenLSVGQRQLLCL 150
|
170 180
....*....|....*....|.
gi 579496312 131 AVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03244 151 ARALLRKSKILVLDEATASVD 171
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-151 |
8.06e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 9 KYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM----NGNIIKFD------GKVDIDNADNIGFL----IEHPKL 74
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervTTGVITGGdrlvngRPLDSSFQRSIGYVqqqdLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 75 YDNKSGLYN--LKLFAQVLGKGFDKaYTDKIIDAFGMRPYIKKKVKKYSMGM----KQKLAIAVSLMNKPKFLI-LDEPT 147
Cdd:TIGR00956 852 TVRESLRFSayLRQPKSVSKSEKME-YVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPT 930
|
....
gi 579496312 148 NGMD 151
Cdd:TIGR00956 931 SGLD 934
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-151 |
9.68e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.58 E-value: 9.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 8 KKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMK-------------VMNGNIIKF----DGKVDIDNADNIGFL-- 68
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRcinflekpsegsiVVNGQTINLvrdkDGQLKVADKNQLRLLrt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 -----IEHPKLYDNKSGLYN-LKLFAQVLG--KGFDKAYTDKIIDAFGMRPYIKKKVKKY-SMGMKQKLAIAVSLMNKPK 139
Cdd:PRK10619 93 rltmvFQHFNLWSHMTVLENvMEAPIQVLGlsKQEARERAVKYLAKVGIDERAQGKYPVHlSGGQQQRVSIARALAMEPE 172
|
170
....*....|..
gi 579496312 140 FLILDEPTNGMD 151
Cdd:PRK10619 173 VLLFDEPTSALD 184
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-151 |
1.08e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.40 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKV---MNGNIIKF--DGKV----------DIDNAD-- 63
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFrvEGKVtfhgknlyapDVDPVEvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 -NIGFLIEHPKLYDnKSGLYNLKLFAQVLG-KGFDKAYTDKIIDAFGMRPYIKKKVKK----YSMGMKQKLAIAVSLMNK 137
Cdd:PRK14243 91 rRIGMVFQKPNPFP-KSIYDNIAYGARINGyKGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQ 169
|
170
....*....|....
gi 579496312 138 PKFLILDEPTNGMD 151
Cdd:PRK14243 170 PEVILMDEPCSALD 183
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-151 |
1.20e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDI----------------DNADNIGFLIEHPKLYDNKS 79
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanlkkikevkRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 80 GLYNLKLFAQV-LGKGFDKAYTD--KIIDAFGM-RPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13645 107 TIEKDIAFGPVnLGENKQEAYKKvpELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-151 |
1.52e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDF--DFGDSRIVGliGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADN--------IGFLIEHPKLYDNKSGLYNL 84
Cdd:PRK13543 26 VFGPLDFhvDAGEALLVQ--GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgdrsrfMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579496312 85 KLFAQVLGKgFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13543 104 HFLCGLHGR-RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-151 |
1.69e-07 |
|
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: 49.03 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM---------NGNII---------------KFDG- 55
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptSGRIIyhvalcekcgyverpSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 56 ------------KVDIDNADN---------IGFLIEHP-KLYDNKSGLYN-LKLFAQVLGKGFDKAYTD-KIIDAFGMRP 111
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDklrrrirkrIAIMLQRTfALYGDDTVLDNvLEALEEIGYEGKEAVGRAvDLIEMVQLSH 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 579496312 112 YIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-147 |
1.91e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID----------NADNIGFLIE 70
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfasttAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 HPKLY----------------DNKSGLYNLKLFaqvlgkgfdKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSL 134
Cdd:PRK11288 85 YQELHlvpemtvaenlylgqlPHKGGIVNRRLL---------NYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170
....*....|...
gi 579496312 135 MNKPKFLILDEPT 147
Cdd:PRK11288 156 ARNARVIAFDEPT 168
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-151 |
2.61e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.03 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNigfliehpKLYDNKSGLYNlklfaqvLGKG 94
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN--------QFGREASLIDA-------IGRK 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 579496312 95 FDKAYTDKIIDAFGMR--PYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG2401 110 GDFKDAVELLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1-151 |
3.28e-07 |
|
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: 47.18 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDfDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDnadnigfliehpklydnksg 80
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-------------------- 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579496312 81 lynlklfaqvlgkgfdkaytdkiidafGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03222 60 ---------------------------GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-147 |
3.38e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN----------ADNIG-FLI 69
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarltpakAHQLGiYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 -EHPKLYDNKSGLYNLklfaqvlgkgfdkaytdkiidAFGM--RPYIKKKVKKY--SMGMKQKLAIAVS----------- 133
Cdd:PRK15439 92 pQEPLLFPNLSVKENI---------------------LFGLpkRQASMQKMKQLlaALGCQLDLDSSAGslevadrqive 150
|
170
....*....|....*...
gi 579496312 134 ----LMNKPKFLILDEPT 147
Cdd:PRK15439 151 ilrgLMRDSRILILDEPT 168
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-151 |
3.84e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.81 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNV-----VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNA------------- 62
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 63 --DNIGFLIEHP--KLYDnKSGLYNLKLFAQVLGkgFDKAYTDKI----IDAFGM-RPYIKKKVKKYSMGMKQKLAIAVS 133
Cdd:PRK13643 82 vrKKVGVVFQFPesQLFE-ETVLKDVAFGPQNFG--IPKEKAEKIaaekLEMVGLaDEFWEKSPFELSGGQMRRVAIAGI 158
|
170
....*....|....*...
gi 579496312 134 LMNKPKFLILDEPTNGMD 151
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLD 176
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-151 |
4.34e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKY--GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNgNIIKFDGKVDIDNAD-NIGFLIEHPKLYdn 77
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwNSVPLQKWRKAF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 78 ksGLYNLK--LFAQVLGKGFD--KAYTD----KIIDAFGMRPYIKKKVKK-----------YSMGMKQKLAIAVSLMNKP 138
Cdd:cd03289 80 --GVIPQKvfIFSGTFRKNLDpyGKWSDeeiwKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKA 157
|
170
....*....|...
gi 579496312 139 KFLILDEPTNGMD 151
Cdd:cd03289 158 KILLLDEPSAHLD 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-151 |
4.96e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.47 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN-----------ADNIGFLieh 71
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsskafARKVAYL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 PKLYDNKSGLYNLKLFA-------QVLGK--GFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLI 142
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAigrypwhGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
....*....
gi 579496312 143 LDEPTNGMD 151
Cdd:PRK10575 171 LDEPTSALD 179
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-151 |
5.19e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 47.34 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG-----NIIKFDGKVDIDNADnigfliehpkLY 75
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndliPGARVEGEILLDGED----------IY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 76 DNKSGLYNLKlfAQVlGKGFDKA-------YtDKIidAFGMRPY-IKKK-------------------VK--------KY 120
Cdd:COG1117 82 DPDVDVVELR--RRV-GMVFQKPnpfpksiY-DNV--AYGLRLHgIKSKseldeiveeslrkaalwdeVKdrlkksalGL 155
|
170 180 190
....*....|....*....|....*....|.
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-151 |
6.75e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.05 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSN--VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM-------NGNIIKFDGKVDIDN----ADNIGF 67
Cdd:PRK13648 8 IVFKNVSFQYQSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMigiekvkSGEIFYNNQAITDDNfeklRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPK--------LYDNKSGLYNLKLFAQVLGKGFDKAYTDkiidaFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPK 139
Cdd:PRK13648 88 VFQNPDnqfvgsivKYDVAFGLENHAVPYDEMHRRVSEALKQ-----VDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170
....*....|..
gi 579496312 140 FLILDEPTNGMD 151
Cdd:PRK13648 163 VIILDEATSMLD 174
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-151 |
7.29e-07 |
|
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: 46.70 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM------NGNIIKFDGKvDIDNADN------IGFLIEHPKLY-----DN 77
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpQGGQVLLDGK-PISQYEHkylhskVSLVGQEPVLFarslqDN 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 78 KSglYNL--KLFAQVLGKGfDKAYTDKIIDAFGMRPY--IKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03248 108 IA--YGLqsCSFECVKEAA-QKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-151 |
7.65e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.63 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM-------NGNIIkFDGKvDIDN------ADNIGF 67
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVaslisptSGTLL-FEGE-DISTlkpeiyRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKL-----YDNksglynLKLFAQVLGKGFDKAYTDKIIDAFGMRPYI-KKKVKKYSMGMKQKLAIAVSLMNKPKFL 141
Cdd:PRK10247 86 CAQTPTLfgdtvYDN------LIFPWQIRNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170
....*....|
gi 579496312 142 ILDEPTNGMD 151
Cdd:PRK10247 160 LLDEITSALD 169
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-151 |
9.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.90 E-value: 9.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADN------------IGF 67
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsklqgirklVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLY--------DNKSGLYNLKLFAQVLGKGFDKAYTDkiidaFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPK 139
Cdd:PRK13644 82 VFQNPETQfvgrtveeDLAFGPENLCLPPIEIRKRVDRALAE-----IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170
....*....|..
gi 579496312 140 FLILDEPTNGMD 151
Cdd:PRK13644 157 CLIFDEVTSMLD 168
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
123-151 |
1.08e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 46.82 E-value: 1.08e-06
10 20
....*....|....*....|....*....
gi 579496312 123 GMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAME 190
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-151 |
1.32e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM----------NGNIIKFDGKVDID---------N 61
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMamhaidgipkNCQILHVEQEVVGDdttalqcvlN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 62 AD--NIGFLIEHPKLYDNKSGLYNLKLFAQvlGKGFDKAYTDK---------------IIDAFGMRPYI----------- 113
Cdd:PLN03073 258 TDieRTQLLEEEAQLVAQQRELEFETETGK--GKGANKDGVDKdavsqrleeiykrleLIDAYTAEARAasilaglsftp 335
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 579496312 114 ---KKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PLN03073 336 emqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-68 |
1.34e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579496312 6 ITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFL 68
Cdd:PRK15064 7 ITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKL 69
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-151 |
1.47e-06 |
|
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: 45.62 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI--------IKFDGK-VDIDN-ADNIGFLIEHPKLYDNKSGLYNL 84
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtglgvsgeVLINGRpLDKRSfRKIIGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579496312 85 KLFAqvlgkgfdkaytdkiidafgmrpyikkKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03213 104 MFAA---------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-151 |
1.50e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 46.33 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 6 ITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID----NADNI-------GFLIEHPK 73
Cdd:PRK13652 9 LCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRgepiTKENIrevrkfvGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 74 --------LYDNKSGLYNLKLFAQVLGKGFDKAytdkiIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:PRK13652 89 dqifsptvEQDIAFGPINLGLDEETVAHRVSSA-----LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:PRK13652 164 PTAGLD 169
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-151 |
1.66e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.07 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNI--------------- 65
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQlrdlyalseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 66 -----GFLIEHPK--LYDNKSGLYNL--KLFAQvlgkgfdkaytdkiidafGMRPY--------------------IKKK 116
Cdd:PRK11701 87 lrtewGFVHQHPRdgLRMQVSAGGNIgeRLMAV------------------GARHYgdiratagdwlerveidaarIDDL 148
|
170 180 190
....*....|....*....|....*....|....*
gi 579496312 117 VKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
101-151 |
2.15e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.81 E-value: 2.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 579496312 101 DKIIDAFGMRPY------IKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR00955 142 DEVLQALGLRKCantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-147 |
2.57e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 5 HITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG--------NIIKFDGKV----DIDNADNIGFLIEH- 71
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvyphgsyeGEILFDGEVcrfkDIRDSEALGIVIIHq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 72 -----PKLydnkSGLYNLKLFAQVLGKGF---DKAY--TDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFL 141
Cdd:NF040905 86 elaliPYL----SIAENIFLGNERAKRGVidwNETNrrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
....*.
gi 579496312 142 ILDEPT 147
Cdd:NF040905 162 ILDEPT 167
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-151 |
2.69e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.51 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID---------NAD------NIGFLIEHP--KLYDnK 78
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstskNKDikqirkKVGLVFQFPesQLFE-E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 79 SGLYNLKLFAQVLGKGFDKAYT---DKII------DAFGMRPYikkkvkKYSMGMKQKLAIAVSLMNKPKFLILDEPTNG 149
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEAlarEKLAlvgiseSLFEKNPF------ELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
..
gi 579496312 150 MD 151
Cdd:PRK13649 176 LD 177
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-151 |
2.81e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 11 GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTT----IMKVMN--GNIIkFDGKvDIDNADNIGFLIEHPKLY----DNKSG 80
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIW-FDGQ-PLHNLNRRQLLPVRHRIQvvfqDPNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 81 LyNLKL-FAQVLGKGFD--------KAYTDKIIDAF---GMRPYIKKKV-KKYSMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:PRK15134 375 L-NPRLnVLQIIEEGLRvhqptlsaAQREQQVIAVMeevGLDPETRHRYpAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
....
gi 579496312 148 NGMD 151
Cdd:PRK15134 454 SSLD 457
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
11-151 |
2.85e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 44.86 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 11 GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKvDIDNADNIG---FLIEHPKLYDNKSGL 81
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLppaagtIKLDGG-DIDDPDVAEachYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 82 YNLKLFAQVLGKgfDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13539 92 ENLEFWAAFLGG--EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-151 |
4.02e-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: 45.16 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 28 IVGLIGKNGVGKTTIMKVMNGnIIKFD-GKVDID----------NADNIGFLIEhpklydnksglynlkLFAQVLGKGFD 96
Cdd:COG1245 368 VLGIVGPNGIGKTTFAKILAG-VLKPDeGEVDEDlkisykpqyiSPDYDGTVEE---------------FLRSANTDDFG 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 97 -KAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG1245 432 sSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-151 |
6.22e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 18 DIDFDFGDSRIVGLIGKNGVGKTT-------IMKVMNGNIIkFDGKvDIdNADNI------------------GFLIEHP 72
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTElaetlygLRPARGGRIM-LNGK-EI-NALSTaqrlarglvylpedrqssGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 73 kLYDNKSGL-YNLKLFAQVLGKgfDKAYTDKIIDAFGMR-PYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:PRK15439 358 -LAWNVCALtHNRRGFWIKPAR--ENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
.
gi 579496312 151 D 151
Cdd:PRK15439 435 D 435
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-151 |
6.90e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 10 YGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK-VDIDNA---DNIGFLIE----HPKLY 75
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnpekgeILFERQsIKKDLCtyqKQLCFVGHrsgiNPYLT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 76 DNKSGLYNLKLFAQVLGkgfdkayTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13540 91 LRENCLYDIHFSPGAVG-------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-151 |
7.07e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 44.31 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNV-----VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDI------DNADNIGFLI 69
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdekNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 70 EHPKLYDNKSGLYNLK-------------------LFAQVLGK---------GFDKAYTD----KIIDAFGM-RPYIKKK 116
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKkikeirrrvgvvfqfaeyqLFEQTIEKdiifgpvsmGVSKEEAKkraaKYIELVGLdESYLQRS 162
|
170 180 190
....*....|....*....|....*....|....*
gi 579496312 117 VKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-151 |
7.95e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.93 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMN------------GNIIK-----FDGKVDIDNAD 63
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmndkvsgyrysGDVLLggrsiFNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 64 NIGFLIEHPK-----LYDNK-SGLYNLKLFAQVLGKGFDKAYTDKIidafGMRPYIKKKVK----KYSMGMKQKLAIAVS 133
Cdd:PRK14271 102 RVGMLFQRPNpfpmsIMDNVlAGVRAHKLVPRKEFRGVAQARLTEV----GLWDAVKDRLSdspfRLSGGQQQLLCLART 177
|
170
....*....|....*...
gi 579496312 134 LMNKPKFLILDEPTNGMD 151
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALD 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-151 |
8.24e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 44.33 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 12 SNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD----NIGFLIEHPKLYDNKSGLYNlKLF 87
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlvqyDHHYLHRQVALVGQEPVLFS-GSV 571
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 88 AQVLGKGFDKAYTDKIIDAF---GMRPYIKKKVKKY-----------SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR00958 572 RENIAYGLTDTPDEEIMAAAkaaNAHDFIMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-151 |
1.16e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.60 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 11 GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGK---------------------------V 57
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIapdhgeILFDGEnipamsrsrlytvrkrmsmlfqsgalfT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 58 DIDNADNIGF-LIEHPKLYDNksglynlKLFAQVLGKgfdkaytdkiIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMN 136
Cdd:PRK11831 98 DMNVFDNVAYpLREHTQLPAP-------LLHSTVMMK----------LEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170
....*....|....*
gi 579496312 137 KPKFLILDEPTNGMD 151
Cdd:PRK11831 161 EPDLIMFDEPFVGQD 175
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-146 |
1.81e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.29 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG--NI----IKFDGKV--DIDNAD-NIG--F-- 67
Cdd:PRK11650 5 KLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRItsgeIWIGGRVvnELEPADrDIAmvFqn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 --LIEHPKLYDNKSglYNLKLfaqvlgKGFDKAYTDKIIDA----FGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFL 141
Cdd:PRK11650 85 yaLYPHMSVRENMA--YGLKI------RGMPKAEIEERVAEaariLELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
....*
gi 579496312 142 ILDEP 146
Cdd:PRK11650 157 LFDEP 161
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
121-151 |
1.93e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 43.26 E-value: 1.93e-05
10 20 30
....*....|....*....|....*....|.
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-148 |
2.21e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 27 RIVGLIGKNGVGKTTIMKVM-------------NGNIIKFDGKVDIDNAdNIGFLIEHPKLYDNKSGLYNLKL---FAQV 90
Cdd:PRK10762 31 RVMALVGENGAGKSTMMKVLtgiytrdagsilyLGKEVTFNGPKSSQEA-GIGIIHQELNLIPQLTIAENIFLgreFVNR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579496312 91 LGK-GFDKAY--TDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:PRK10762 110 FGRiDWKKMYaeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-147 |
2.58e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 28 IVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID----------NADNIG----FLIEHPKLYDnksglynlklfaqvlgk 93
Cdd:PRK13409 367 VIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyiKPDYDGtvedLLRSITDDLG----------------- 429
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 579496312 94 gfDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:PRK13409 430 --SSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
81-151 |
2.67e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 2.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 81 LYNLKLFAQvlGKGFDKAYTDKIIDAFGMRPYIKK-----KVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13549 364 LAALDRFTG--GSRIDDAAELKTILESIQRLKVKTaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
126-151 |
3.19e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 3.19e-05
10 20
....*....|....*....|....*.
gi 579496312 126 QKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK15093 165 QKVMIAIALANQPRLLIADEPTNAME 190
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-151 |
3.26e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 41.65 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD------------NIGFLIEHPKlydnKSGLy 82
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvtrrsprdairaGIAYVPEDRK----REGL- 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 579496312 83 nlklfaqVLGKGfdkaytdkIIDAFGMRPYIkkkvkkySMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03215 90 -------VLDLS--------VAENIALSSLL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-151 |
3.33e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.40 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 3 LEHITKKYGS-NVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNA-----------DNIGFLIE 70
Cdd:PRK10790 343 IDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvlrQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 HPK-LYDNksglynlkLFAQV-LGKGFDKAYTDKIIDAF-----------GMRPYIKKKVKKYSMGMKQKLAIAVSLMNK 137
Cdd:PRK10790 423 DPVvLADT--------FLANVtLGRDISEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170
....*....|....
gi 579496312 138 PKFLILDEPTNGMD 151
Cdd:PRK10790 495 PQILILDEATANID 508
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-151 |
4.34e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.12 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDI------DNADN---------IGFLIEHP--KLYDNk 78
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitPETGNknlkklrkkVSLVFQFPeaQLFEN- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 79 SGLYNLKLFAQVLGKGFDKAYTD--KIIDAFGMRP-YIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13641 102 TVLKDVEFGPKNFGFSEDEAKEKalKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-151 |
4.45e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 42.07 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 14 VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD---------------NIGFLIEHP--KLYD 76
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyirpvrkRIGMVFQFPesQLFE 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 77 N---KSGLYNLKLFAQVLGKGFDKAYtDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13646 101 DtveREIIFGPKNFKMNLDEVKNYAH-RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-50 |
4.99e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 41.74 E-value: 4.99e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI 50
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL 51
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-146 |
4.99e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.78 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 18 DIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNI------IKFDGKVDIDNAD---------NIGFLIEHPKLYDNKSGLY 82
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTrpqkgrIVLNGRVLFDAEKgiclppekrRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579496312 83 NLKLfaqvlG-KGFDKAYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:PRK11144 96 NLRY-----GmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
31-145 |
7.20e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 31 LIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN----ADNIGfliEHPKLYdnkSGLY-NLKLFAQVLG-KGFDKAytDKII 104
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpvtAEQPE---DYRKLF---SAVFtDFHLFDQLLGpEGKPAN--PALV 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 579496312 105 DAFGMRPYIKKKVK---------KYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:PRK10522 426 EKWLERLKMAHKLEledgrisnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-151 |
7.69e-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: 41.35 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNII-KFDGKVDID----NADNIGFLIEH---------------PKLY 75
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINgkpvDIRNPAQAIRAgiamvpedrkrhgivPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 76 DNKS-GLYNLKLFAqvlGKG-FDKAYTDKIIDAFGMRPYIKK-----KVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:TIGR02633 356 VGKNiTLSVLKSFC---FKMrIDAAAELQIIGSAIQRLKVKTaspflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
...
gi 579496312 149 GMD 151
Cdd:TIGR02633 433 GVD 435
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-151 |
8.03e-05 |
|
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: 40.69 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 9 KYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVM-----NGNI---IKFDGK-VDIDNADNIGFlIEHPKLYDNKS 79
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVItgeILINGRpLDKNFQRSTGY-VEQQDVHSPNL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579496312 80 GLYNLKLFAQVLgKGFdkaytdkiidafgmrpyikkkvkkySMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:cd03232 95 TVREALRFSALL-RGL-------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-151 |
8.04e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 40.97 E-value: 8.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 2 KLEHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGN--------IIKFDGKvDIDNAD-------NIG 66
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkyevtegEILFKGE-DITDLPpeerarlGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPKLYdnkSGLyNLKLFAQVLGKGFdkaytdkiidafgmrpyikkkvkkySMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:cd03217 81 LAFQYPPEI---PGV-KNADFLRYVNEGF-------------------------SGGEKKRNEILQLLLLEPDLAILDEP 131
|
....*
gi 579496312 147 TNGMD 151
Cdd:cd03217 132 DSGLD 136
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
10-151 |
9.13e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 40.78 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 10 YGSNV-VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIEHPKLYDNKSGLYNLK--- 85
Cdd:cd03290 10 WGSGLaTLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQkpw 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 86 -LFAQV-----LGKGFDKAYTDKIIDA-----------FGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTN 148
Cdd:cd03290 90 lLNATVeenitFGSPFNKQRYKAVTDAcslqpdidllpFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
...
gi 579496312 149 GMD 151
Cdd:cd03290 170 ALD 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-151 |
1.04e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.53 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSN----VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDN--------------- 61
Cdd:PRK10584 7 VEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 62 ADNIGFLIEHPKLYDNKSGLYNLKLFAQVLGKGFDKAYTDKI--IDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPK 139
Cdd:PRK10584 87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170
....*....|..
gi 579496312 140 FLILDEPTNGMD 151
Cdd:PRK10584 167 VLFADEPTGNLD 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-151 |
1.14e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 41.10 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKY-GSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMkvmngNIIK--FD---GKVDIDNAD-----------NIG 66
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-----NLLQrvFDpqsGRILIDGTDirtvtraslrrNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 67 FLIEHPKLYdNKSGLYNLKLfaqvlgkGFDKAYTDKIIDAFGM---RPYIKKKVKKY-----------SMGMKQKLAIAV 132
Cdd:PRK13657 413 VVFQDAGLF-NRSIEDNIRV-------GRPDATDEEMRAAAERaqaHDFIERKPDGYdtvvgergrqlSGGERQRLAIAR 484
|
170
....*....|....*....
gi 579496312 133 SLMNKPKFLILDEPTNGMD 151
Cdd:PRK13657 485 ALLKDPPILILDEATSALD 503
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-151 |
1.27e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.79 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 4 EHITKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD---------------NIGFL 68
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakisdaelrevrrkKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 69 IEHPKLYDNKSGLYNLKLFAQVLGKGFDKAyTDKIIDAF---GMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGINAEER-REKALDALrqvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
....*.
gi 579496312 146 PTNGMD 151
Cdd:PRK10070 191 AFSALD 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-151 |
2.21e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 39.72 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDID----NADN-------IGFLIEHP--KLY------D 76
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMgrevNAENekwvrskVGLVFQDPddQVFsstvwdD 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579496312 77 NKSGLYNLKLFAQVLGKGFDKAytdkiIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK13647 101 VAFGPVNMGLDKDEVERRVEEA-----LKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
107-151 |
2.80e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 2.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 579496312 107 FGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK10938 123 FGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-151 |
2.82e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNG------NIIKFDGKV----DIDNADNIGF------------------ 67
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGireksaGTITLHGKKinnhNANEAINHGFalvteerrstgiyayldi 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 ----LIEHPKLYDNKSGLYNLKLFaqvlgkgfdKAYTDKIIDAFGMR-PYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLI 142
Cdd:PRK10982 344 gfnsLISNIRNYKNKVGLLDNSRM---------KSDTQWVIDSMRVKtPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILM 414
|
....*....
gi 579496312 143 LDEPTNGMD 151
Cdd:PRK10982 415 LDEPTRGID 423
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
121-151 |
2.90e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 39.83 E-value: 2.90e-04
10 20 30
....*....|....*....|....*....|.
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
121-151 |
2.96e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 2.96e-04
10 20 30
....*....|....*....|....*....|.
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-151 |
3.22e-04 |
|
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: 39.93 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 16 LNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDnadniGFLIEHPKlydnKSGLYNLKLFAQVL-GKG 94
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK-----GSVAYVPQ----QAWIQNDSLRENILfGKA 724
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 579496312 95 FDKAYTDKIIDAF-----------GMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:TIGR00957 725 LNEKYYQQVLEACallpdleilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-146 |
3.60e-04 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 38.99 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 7 TKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVD-------------IDNA---DNIgflie 70
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSvpgsiayvsqepwIQNGtirENI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 71 hpklydnksglynlkLFaqvlGKGFDKAYTDKIIDAFGMRPYIKKKVKK-----------YSMGMKQKLAIAVSLMNKPK 139
Cdd:cd03250 87 ---------------LF----GKPFDEERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDAD 147
|
....*..
gi 579496312 140 FLILDEP 146
Cdd:cd03250 148 IYLLDDP 154
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
121-147 |
3.89e-04 |
|
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: 39.28 E-value: 3.89e-04
10 20
....*....|....*....|....*..
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPT 184
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
121-147 |
4.00e-04 |
|
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: 39.28 E-value: 4.00e-04
10 20
....*....|....*....|....*..
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPT 453
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
120-151 |
4.41e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 39.18 E-value: 4.41e-04
10 20 30
....*....|....*....|....*....|..
gi 579496312 120 YSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-151 |
4.89e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 38.92 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 15 VLNDIDFDFGDSRIVGLIGKNGVGKT-TIMKVMN----------GNIIKFDGKvDIDNAD----------NIGFLIEHPK 73
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRllpsppvvypSGDIRFHGE-SLLHASeqtlrgvrgnKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 74 LYDNKsgLYNL-KLFAQVL----GKGFDKAYTDKI--IDAFGMRpYIKKKVKKY----SMGMKQKLAIAVSLMNKPKFLI 142
Cdd:PRK15134 103 VSLNP--LHTLeKQLYEVLslhrGMRREAARGEILncLDRVGIR-QAAKRLTDYphqlSGGERQRVMIAMALLTRPELLI 179
|
....*....
gi 579496312 143 LDEPTNGMD 151
Cdd:PRK15134 180 ADEPTTALD 188
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-44 |
6.97e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.44 E-value: 6.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 579496312 1 MKLEHIT-KKYGSnvvLNDIDFDFgDSRIVGLIGKNGVGKTTIMK 44
Cdd:COG3593 1 MKLEKIKiKNFRS---IKDLSIEL-SDDLTVLVGENNSGKSSILE 41
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-148 |
7.04e-04 |
|
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: 38.58 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNVVL-NDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNADNIGFLIEHPklYDNKS 79
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRP--YMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 80 GLYNLKLFAQVLGKGFDKAYTDK----IIDAFGMRPYIKKKV---------KKYSMGMKQKLAIAVSLMNKPKFLILDEP 146
Cdd:TIGR00954 530 TLRDQIIYPDSSEDMKRRGLSDKdleqILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
..
gi 579496312 147 TN 148
Cdd:TIGR00954 610 TS 611
|
|
| PLN03210 |
PLN03210 |
Resistant to P. syringae 6; Provisional |
27-128 |
7.94e-04 |
|
Resistant to P. syringae 6; Provisional
Pssm-ID: 215633 [Multi-domain] Cd Length: 1153 Bit Score: 38.70 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 27 RIVGLIGKNGVGKTTIMKVMNGNI-IKFDGKVDIDNAdnigFLIEHPKLYDN-KSGLYNLKLFAQvlgkgfdKAYTDKII 104
Cdd:PLN03210 208 RMVGIWGSSGIGKTTIARALFSRLsRQFQSSVFIDRA----FISKSMEIYSSaNPDDYNMKLHLQ-------RAFLSEIL 276
|
90 100
....*....|....*....|....*
gi 579496312 105 DafgmrpyiKKKVKKYSMG-MKQKL 128
Cdd:PLN03210 277 D--------KKDIKIYHLGaMEERL 293
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
118-151 |
8.27e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.47 E-value: 8.27e-04
10 20 30
....*....|....*....|....*....|....
gi 579496312 118 KKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-151 |
9.21e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 38.32 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 7 TKKYGSNVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIK--FDGKVDIDNAD-------NIGFLIEHPKLYDN 77
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGnnFTGTILANNRKptkqilkRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 78 KSGLYNLKLFA-----QVLGKGFDKAYTDKIIDAFGM----RPYIKKK-VKKYSMGMKQKLAIAVSLMNKPKFLILDEPT 147
Cdd:PLN03211 155 LTVRETLVFCSllrlpKSLTKQEKILVAESVISELGLtkceNTIIGNSfIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
....
gi 579496312 148 NGMD 151
Cdd:PLN03211 235 SGLD 238
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-151 |
1.17e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.09 E-value: 1.17e-03
10 20 30
....*....|....*....|....*....|...
gi 579496312 119 KYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
121-151 |
1.27e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 37.76 E-value: 1.27e-03
10 20 30
....*....|....*....|....*....|.
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-145 |
1.28e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.54 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 13 NVVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNA--DNI-----GFLIEHPKLYDNKSGLYNLK 85
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCniNNIakpycTYIGHNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579496312 86 LFAQVlgkgFDKAYT-DKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDE 145
Cdd:PRK13541 93 FWSEI----YNSAETlYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-151 |
1.37e-03 |
|
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: 37.58 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 1 MKLEHITKKYGSNV--VLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGNIIKFDGKVDIDNAD-----------NIGF 67
Cdd:cd03288 20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklplhtlrsRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 68 LIEHPKLYDNkSGLYNL----KLFAQVLGKGFDKAYTDKIIDAF--GMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFL 141
Cdd:cd03288 100 ILQDPILFSG-SIRFNLdpecKCTDDRLWEALEIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170
....*....|
gi 579496312 142 ILDEPTNGMD 151
Cdd:cd03288 179 IMDEATASID 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
121-151 |
1.56e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 37.53 E-value: 1.56e-03
10 20 30
....*....|....*....|....*....|.
gi 579496312 121 SMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALD 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
97-151 |
1.72e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 37.31 E-value: 1.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 579496312 97 KAYTDKIIDAFGMR-PYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG3845 379 RAFAEELIEEFDVRtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
111-151 |
2.90e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 36.69 E-value: 2.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 579496312 111 PYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:NF040905 396 PSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-43 |
5.10e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 35.76 E-value: 5.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 579496312 2 KLEHIT-KKYGSNVVLNDIDFDFGdsrIVGLIGKNGVGKTTIM 43
Cdd:COG0419 1 KLLRLRlENFRSYRDTETIDFDDG---LNLIVGPNGAGKSTIL 40
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
14-144 |
7.88e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 35.04 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 14 VVLNDIDFDFGDSRIVGLIGKNGVGKTTIMKVMNGniikFDGKvdiDNADNIGFLIEHPKLYDNK------SGLYNLKLF 87
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCG----LDAP---DEGDFIGLRGDALPLGANSfilpglTGEENARMM 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 579496312 88 AQVLGKGFDKaYTDKIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILD 144
Cdd:PRK15177 74 ASLYGLDGDE-FSHFCYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIAD 129
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-150 |
8.17e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 35.48 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579496312 31 LIGKNGVGKTTIMKVMNGNIIKfdgkvdidNADNIGFLIEHPKLYDNKSGLYN--------LKLFAQV-------LG--- 92
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQK--------DSGSILFQGKEIDFKSSKEALENgismvhqeLNLVLQRsvmdnmwLGryp 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579496312 93 -KGF----DKAYTD--KIIDAFGMRPYIKKKVKKYSMGMKQKLAIAVSLMNKPKFLILDEPTNGM 150
Cdd:PRK10982 101 tKGMfvdqDKMYRDtkAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
119-151 |
9.43e-03 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 35.18 E-value: 9.43e-03
10 20 30
....*....|....*....|....*....|...
gi 579496312 119 KYSMGMKQKLAIAVSLMNKPKFLILDEPTNGMD 151
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| |
