|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-221 |
6.32e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 226.10 E-value: 6.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLD 83
Cdd:COG1131 1 IEVRGLTKRYGDKtALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEMKNIIAPSY---TDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTS 158
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTdaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 159 GLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDSH 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-242 |
6.49e-63 |
|
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: 198.16 E-value: 6.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVL 82
Cdd:COG4555 1 MIEVENLSKKYgKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDELTLKEMKNIIAPSYTDWDE---PVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEelkKRIEELIELLGLEefLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 158 SGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLidshalikgSNRFINEQTKN 237
Cdd:COG4555 161 NGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL---------REEIGEENLED 230
|
....*
gi 1261293288 238 LFLNL 242
Cdd:COG4555 231 AFVAL 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-208 |
2.64e-62 |
|
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: 194.15 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLD 83
Cdd:cd03230 1 IEVRNLSKRYgKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEmkniiapsytdwdepvfqdyikqfnlNLKqkistLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPL 163
Cdd:cd03230 81 EPSLYENLTVRE--------------------------NLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1261293288 164 VRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03230 130 SRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-209 |
9.77e-46 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 153.14 E-value: 9.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHErKSKNKIGIVLD 83
Cdd:cd03268 1 LKTNDLTKTYgKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELT----LKEMKNIIAPSYTDWDEPVfqDYIKQFNLNlKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSG 159
Cdd:cd03268 80 APGFYPNLTarenLRLLARLLGIRKKRIDEVL--DVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261293288 160 LDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:cd03268 157 LDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-211 |
3.04e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 146.79 E-value: 3.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERkskNKIGIVL 82
Cdd:COG4152 1 MLELKGLTKRFGDKtAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR---RRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DE-GYF-----YDELT----LKEMKNIIAPSYTDwdepvfqDYIKQFNL--NLKQKISTLSKGM--RMKFAVALAlsHHA 148
Cdd:COG4152 78 EErGLYpkmkvGEQLVylarLKGLSKAEAKRRAD-------EWLERLGLgdRANKKVEELSKGNqqKVQLIAALL--HDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 149 DLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVN 211
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-282 |
1.95e-39 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 139.45 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 12 KCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLDEGYFYDE 90
Cdd:TIGR01188 1 KVYGDFkAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 91 LTLKEMKNIIAPSY---TDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVR 165
Cdd:TIGR01188 81 LTGRENLEMMGRLYglpKDEAEERAEELLELFELGeaADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 166 SELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL----VNDEKDMLIDSHALIKGSN-RFINEQTKNLFL 240
Cdd:TIGR01188 161 RAIWDYIRA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIaegtPEELKRRLGKDTLESRPRDiQSLKVEVSMLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 241 NLHQTHYGFEGITNKKDDVR-------RLMPDVL--------------MERPTIEDIMLSYIG 282
Cdd:TIGR01188 240 ELGETGLGLLAVTVDSDRIKilvpdgdETVPEIVeaairngirirsisTERPSLDDVFLKLTG 302
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-209 |
5.16e-39 |
|
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: 135.96 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKI 78
Cdd:cd03266 1 MITADALTKRFRDVKktvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 GIVLDEGYFYDELTLKEMKNIIAPSY---TDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLM 153
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYglkGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261293288 154 DEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-207 |
4.46e-36 |
|
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: 126.92 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE---RKSKNKIGI 80
Cdd:cd03229 1 LELKNVSKRYgQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VldegyfydeltlkemkniiapsytdwdepvFQDYIKQFNLNLKQKIS-TLSKGMRMKFAVALALSHHADLLLMDEPTSG 159
Cdd:cd03229 81 V------------------------------FQDFALFPHLTVLENIAlGLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1261293288 160 LDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:cd03229 131 LDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-208 |
7.84e-36 |
|
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: 127.40 E-value: 7.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERkskNKIGIVLD 83
Cdd:cd03269 1 LEVENVTKRFgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR---NRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEM-----------KNIIAPSYTDWdepvfqdyIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:cd03269 78 ERGLYPKMKVIDQlvylaqlkglkKEEARRRIDEW--------LERLELSeyANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 151 LLMDEPTSGLDPlVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03269 150 LILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-208 |
1.33e-35 |
|
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: 127.10 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLD 83
Cdd:cd03265 1 IEVENLVKKYGDFeAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEMKNIIAPSY----TDWDEPVfQDYIKQFNL-NLKQKI-STLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYgvpgAERRERI-DELLDFVGLlEAADRLvKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 158 SGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-209 |
2.26e-35 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 126.47 E-value: 2.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS---LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYDELTLKEMKNIIAP--SYTDWDEPVFQD-YIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEP 156
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARlkGLPKSEIKEEVElLLRVLGLTdkANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 157 TSGLDPLVRSELMDILLnFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:cd03263 161 TSGLDPASRRAIWDLIL-EVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-207 |
1.75e-34 |
|
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: 122.35 E-value: 1.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 6 EVNNLNK-CYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVld 83
Cdd:cd00267 1 EIENLSFrYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 egyfydeltlkemkniiapsytdwdepvFQdyikqfnlnlkqkistLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPL 163
Cdd:cd00267 79 ----------------------------PQ----------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1261293288 164 VRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-209 |
4.84e-34 |
|
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: 122.69 E-value: 4.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYEN-FSLKDVTFRISNDcITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLD 83
Cdd:cd03264 1 LQLENLTKRYGKkRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEMKNIIA-----PSyTDWDEPVfQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEP 156
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAwlkgiPS-KEVKARV-DEVLELVNLGdrAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 157 TSGLDPLVRSELMDILLNFMKEpgKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-220 |
5.07e-34 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 123.38 E-value: 5.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND---MDKHE-RKSKNKIG 79
Cdd:cd03261 1 IELRGLTKSFGGRTvLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAElYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IVLDEGYFYDELTLKEmkNIIAP--SYTDWDEPVFQDYIKQFnLNL-------KQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:cd03261 81 MLFQSGALFDSLTVFE--NVAFPlrEHTRLSEEEIREIVLEK-LEAvglrgaeDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 151 LLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDS 220
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-207 |
1.60e-33 |
|
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: 121.42 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 6 EVNNLNKCYENFS---LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNK-IGIV 81
Cdd:cd03225 1 ELKNLSFSYPDGArpaLDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LD--EGYF-----YDE---------LTLKEMKNIIApsytdwdepvfqDYIKQFNLN--LKQKISTLSKGMRMKFAVALA 143
Cdd:cd03225 81 FQnpDDQFfgptvEEEvafglenlgLPEEEIEERVE------------EALELVGLEglRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 144 LSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-209 |
9.26e-33 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 120.13 E-value: 9.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY--ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIV 81
Cdd:COG1122 1 IELENLSFSYpgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 L---DEGYF----YDE---------LTLKEMKNIIapsytdwdepvfQDYIKQFNL-NLKQK-ISTLSKGMRMKFAVALA 143
Cdd:COG1122 81 FqnpDDQLFaptvEEDvafgpenlgLPREEIRERV------------EEALELVGLeHLADRpPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261293288 144 LSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-215 |
1.28e-31 |
|
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: 116.73 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDkheRKSKNKIGIVLD 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTaVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT---RKDLHKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEMKNIIApSYTDWDEPVFQDYIKQFNLNL--KQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLD 161
Cdd:TIGR03740 78 SPPLYENLTARENLKVHT-TLLGLPDSRIDEVLNIVDLTNtgKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 162 PLVRSELMDILLNFmKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKD 215
Cdd:TIGR03740 157 PIGIQELRELIRSF-PEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKIN 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-208 |
1.73e-31 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 116.45 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSK--- 75
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 -NKIGIVldegyFYDELT-----------LKEMKNIIAPSYTDWDEPVFQDYI-KQFNLN---LKQKISTLSKGMRMKFA 139
Cdd:cd03257 81 rKEIQMV-----FQDPMSslnprmtigeqIAEPLRIHGKLSKKEARKEAVLLLlVGVGLPeevLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 140 VALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFsthITSDLD---KIADMIILIDDGKI 208
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLF---ITHDLGvvaKIADRVAVMYAGKI 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-209 |
2.21e-31 |
|
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: 114.84 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 6 EVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKherksknkigivlde 84
Cdd:cd03214 1 EVENLSVGYgGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 85 gyfydeLTLKEMKNIIApsYtdwdepVFQdYIKQFNL-NLKQK-ISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:cd03214 66 ------LSPKELARKIA--Y------VPQ-ALELLGLaHLADRpFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261293288 163 LVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKIL 209
Cdd:cd03214 131 AHQIELLELLRRLARERGKTVVMVLH---DLNlaaRYADRVILLKDGRIV 177
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
3.45e-31 |
|
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: 116.23 E-value: 3.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND---MDKHERKS-K 75
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 NKIGIVLDEGYFYDELTLKEmkNIIAP--SYTDWDEPVFQD----YIKQFNLN--LKQKISTLSKGMRMKFAVALALSHH 147
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFE--NVAFPlrEHTDLSEAEIRElvleKLELVGLPgaADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 148 ADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDS-HALIK 225
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASdDPWVR 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-222 |
4.13e-31 |
|
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: 115.86 E-value: 4.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND-MDKHERKSKNKIGIV 81
Cdd:cd03295 1 IEFENVTKRYGGgkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYDELTLKEmkNI-IAPSYTDWDEPVFQDYIKQF----NL---NLKQKI-STLSKGMRMKFAVALALSHHADLLL 152
Cdd:cd03295 81 IQQIGLFPHMTVEE--NIaLVPKLLKWPKEKIRERADELlalvGLdpaEFADRYpHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 153 MDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKILVNDEKDMLIDSHA 222
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTH---DIDeafRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-277 |
9.45e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 117.11 E-value: 9.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS----------------------LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKIN 61
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 62 FLGNDMDKHERKSKNKIGIV------LdegyFYD-------ELtLKEMKNIiapsytdwDEPVFQDYIKQFN--LNLKQK 126
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVVfgqrsqL----WWDlpaidsfRL-LKAIYRI--------PDAEYKKRLDELVelLDLGEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 127 IST----LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIIL 202
Cdd:COG4586 148 LDTpvrqLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 203 IDDGKILVNDEKDMLIDSHalikGSNRFINEQTKNLFLNLHQTHYG-------------FEGITNKKDDVRRLMP----- 264
Cdd:COG4586 228 IDHGRIIYDGSLEELKERF----GPYKTIVLELAEPVPPLELPRGGevieregnrvrleVDPRESLAEVLARLLArypvr 303
|
330
....*....|...
gi 1261293288 265 DVLMERPTIEDIM 277
Cdd:COG4586 304 DLTIEEPPIEEVI 316
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-209 |
1.13e-30 |
|
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: 115.14 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERK--SKnKIGI 80
Cdd:COG1120 1 MLEAENLSVGYGGRPvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelAR-RIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDELTLKEM--------KNIIAPsYTDWDEPVFQDYIKQFNL-NLKQK-ISTLSKGMRMKFAVALALSHHADL 150
Cdd:COG1120 80 VPQEPPAPFGLTVRELvalgryphLGLFGR-PSAEDREAVEEALERTGLeHLADRpVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 151 LLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKIL 209
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH---DLNlaaRYADRLVLLKDGRIV 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-208 |
5.23e-30 |
|
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: 112.58 E-value: 5.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYEN-----FSLKDVTFRISNDCITGFIGTNGSGKTTTIKaILGLILK-DSGKINFLGNDMDK--HERKSK- 75
Cdd:cd03255 1 IELKNLSKTYGGggekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRpTSGEVRVDGTDISKlsEKELAAf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 --NKIGIVLDEGYFYDELTLKEmkNIIAPSY-----TDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSH 146
Cdd:cd03255 80 rrRHIGFVFQSFNLLPDLTALE--NVELPLLlagvpKKERRERAEELLERVGLGdrLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 147 HADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHiTSDLDKIADMIILIDDGKI 208
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTH-DPELAEYADRIIELRDGKI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-208 |
9.95e-30 |
|
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: 111.76 E-value: 9.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK---HERkskNKIGI 80
Cdd:cd03224 1 LEVENLNAGYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppHER---ARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VL---DEGYFyDELTLKEmkNIIAPSYTDWDEPVFQDYIKQFNL------NLKQKISTLSKGMRMKFAVALALSHHADLL 151
Cdd:cd03224 78 GYvpeGRRIF-PELTVEE--NLLLGAYARRRAKRKARLERVYELfprlkeRRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 152 LMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFS-THITSDLdKIADMIILIDDGKI 208
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRE-LRDEGVTILLVeQNARFAL-EIADRAYVLERGRV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-209 |
1.22e-29 |
|
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: 116.93 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLNKCYENFS------LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKN 76
Cdd:COG1123 259 PLLEVRNLSKRYPVRGkggvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 77 ----KIGIV-----------------LDEGY-FYDELTLKEMKNIIApsytdwdepvfqDYIKQFNLNLKQK---ISTLS 131
Cdd:COG1123 339 elrrRVQMVfqdpysslnprmtvgdiIAEPLrLHGLLSRAERRERVA------------ELLERVGLPPDLAdryPHELS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 132 KGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKI 208
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH---DLAvvrYIADRVAVMYDGRI 483
|
.
gi 1261293288 209 L 209
Cdd:COG1123 484 V 484
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-212 |
2.36e-29 |
|
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: 111.27 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVL--DEGYFYDeLTLKEM 96
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgqKTQLWWD-LPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 97 KNIIAPSYtDWDEPVFQDYIKQFN--LN----LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMD 170
Cdd:cd03267 116 FYLLAAIY-DLPPARFKKRLDELSelLDleelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1261293288 171 ILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVND 212
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-208 |
1.91e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 108.59 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCY-----ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIkAILGLILK-DSGKINFLGND---MDKHE 71
Cdd:COG1136 1 MSPLLELRNLTKSYgtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-NILGGLDRpTSGEVLIDGQDissLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 72 RkSK---NKIGIVLDEGYFYDELTLKEmkNIIAPSY-----TDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVA 141
Cdd:COG1136 80 L-ARlrrRHIGFVFQFFNLLPELTALE--NVALPLLlagvsRKERRERARELLERVGLGdrLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 142 LALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD--KIADMIILIDDGKI 208
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTH---DPElaARADRVIRLRDGRI 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-208 |
2.99e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.64 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGndmdKHERKSKNKIG 79
Cdd:COG1121 3 MMPAIELENLTVSYGGRPvLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IV-----LDEGYFydeLTLKEM-------KNIIAPSYTDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALS 145
Cdd:COG1121 79 YVpqraeVDWDFP---ITVRDVvlmgrygRRGLFRRPSRADREAVDEALERVGLEdlADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261293288 146 HHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHitsDLDKI---ADMIILIDDGKI 208
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTH---DLGAVreyFDRVLLLNRGLV 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-208 |
5.53e-28 |
|
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: 106.85 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 6 EVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGndmdKHERKSKNKIGIV--- 81
Cdd:cd03235 1 EVEDLTVSYGGHPvLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIGYVpqr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 --LDEGYfydELTLKEM-------KNIIAPSYTDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:cd03235 77 rsIDRDF---PISVRDVvlmglygHKGLFRRLSKADKAKVDEALERVGLSelADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 151 LLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-208 |
6.70e-28 |
|
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: 111.92 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCY---ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLI---LKDSGKINFLGNDMDKH-ERK 73
Cdd:COG1123 1 MTPLLEVRDLSVRYpggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphgGRISGEVLLDGRDLLELsEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 74 SKNKIGIV----------------LDEGYFYDELTLKEMKNIIApsytdwdepvfqDYIKQFNLN--LKQKISTLSKGMR 135
Cdd:COG1123 81 RGRRIGMVfqdpmtqlnpvtvgdqIAEALENLGLSRAEARARVL------------ELLEAVGLErrLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 136 MKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-207 |
8.21e-28 |
|
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: 105.16 E-value: 8.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYEN---FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGI 80
Cdd:cd03228 1 IEFKNVSFSYPGrpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDElTLKEmkNIiapsytdwdepvfqdyikqfnlnlkqkistLSKGMRMKFAVALALSHHADLLLMDEPTSGL 160
Cdd:cd03228 81 VPQDPFLFSG-TIRE--NI------------------------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261293288 161 DPLVRSELMDILLNFMKepGKSVFFSTHITSDLDKiADMIILIDDGK 207
Cdd:cd03228 128 DPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-208 |
3.28e-27 |
|
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: 105.73 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF--SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM----DKHERKSKNKI 78
Cdd:cd03256 1 IEVENLSKTYPNGkkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 GIVLDEGYFYDELTLkeMKNI-------------IAPSYTDWDEPVFQDYIKQFNLNLK--QKISTLSKGMRMKFAVALA 143
Cdd:cd03256 81 GMIFQQFNLIERLSV--LENVlsgrlgrrstwrsLFGLFPKEEKQRALAALERVGLLDKayQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 144 LSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKI 208
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLH---QVDlarEYADRIVGLKDGRI 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-223 |
1.45e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 103.92 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND---MDKHE-RKSKNK 77
Cdd:TIGR02315 1 MLEVENLSKVYPNgkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitkLRGKKlRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIVLDEGYFYDELTLkeMKNIIAP--SYTDWDEPVF-----QDYIKQFNL----NLK----QKISTLSKGMRMKFAVAL 142
Cdd:TIGR02315 81 IGMIFQHYNLIERLTV--LENVLHGrlGYKPTWRSLLgrfseEDKERALSAlervGLAdkayQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 143 ALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIlVNDEKDMLIDSHA 222
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI-VFDGAPSELDDEV 237
|
.
gi 1261293288 223 L 223
Cdd:TIGR02315 238 L 238
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-209 |
1.75e-26 |
|
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: 102.98 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND---MDKHERKsknkIGI 80
Cdd:cd03259 1 LELKGLSKTYgSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgVPPERRN----IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDELT--------LKEMKniiaPSYTDWDEPVfQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:cd03259 77 VFQDYALFPHLTvaeniafgLKLRG----VPKAEIRARV-RELLELVGLEglLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 151 LLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-208 |
4.86e-26 |
|
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: 107.23 E-value: 4.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS---LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGI 80
Cdd:COG2274 474 IELENVSFRYPGDSppvLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGY-FYDelTLKEmkNII--APSYTdwDEPVFQ--------DYIKQFNLNLKQKI----STLSKGMRMKFAVALALS 145
Cdd:COG2274 554 VLQDVFlFSG--TIRE--NITlgDPDAT--DEEIIEaarlaglhDFIEALPMGYDTVVgeggSNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 146 HHADLLLMDEPTSGLDPLVRSELMDILLNFMKepGKSVFFSTHITSDLdKIADMIILIDDGKI 208
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-207 |
7.56e-26 |
|
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: 101.02 E-value: 7.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVL 82
Cdd:COG4133 2 MLEAENLSCRRGERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDELTLKEMKNIIAPSY-TDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSG 159
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYgLRADREAIDEALEAVGLAglADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1261293288 160 LDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDkiADMIILIDDGK 207
Cdd:COG4133 162 LDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-209 |
1.27e-24 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 99.45 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY------ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKN-- 76
Cdd:TIGR04521 1 IKLKNVSYIYqpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 77 --KIGIV-------LDEGYFYDE---------LTLKEMKNIIapsytdwdepvfQDYIKQFNLNLKQK-IS--TLSKGMR 135
Cdd:TIGR04521 81 rkKVGLVfqfpehqLFEETVYKDiafgpknlgLSEEEAEERV------------KEALELVGLDEEYLeRSpfELSGGQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 136 MKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-221 |
1.63e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.68 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKCYEN-FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGI 80
Cdd:PRK13536 39 TVAIDLAGVSKSYGDkAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDELTLKEmkNIIAPS-----YTDWDEPVFQDYIKQFNLNLKQ--KISTLSKGMRMKFAVALALSHHADLLLM 153
Cdd:PRK13536 119 VPQFDNLDLEFTVRE--NLLVFGryfgmSTREIEAVIPSLLEFARLESKAdaRVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 154 DEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDSH 221
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-158 |
1.75e-24 |
|
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: 95.79 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVLDEGYFYDELTLKEmk 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRE-- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 98 NIIAPS-----YTDWDEPVFQDYIKQFNLN------LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTS 158
Cdd:pfam00005 79 NLRLGLllkglSKREKDARAEEALEKLGLGdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-220 |
6.15e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.34 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLD 83
Cdd:PRK13537 8 IDFRNVEKRYgDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEmkNIIapsytdwdepVFQDYikqFNLNLKQ--------------------KISTLSKGMRMKFAVALA 143
Cdd:PRK13537 88 FDNLDPDFTVRE--NLL----------VFGRY---FGLSAAAaralvppllefaklenkadaKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 144 LSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDS 220
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-222 |
1.19e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.98 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFSLKdVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK---HERKsknkIGI 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlppAERP----VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDELTLKEmkNI---IAPS--YTDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLM 153
Cdd:COG3840 76 LFQENNLFPHLTVAQ--NIglgLRPGlkLTAEQRAQVEQALERVGLAglLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 154 DEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDSHA 222
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-208 |
3.04e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKInflgndmdkherksknKIGI 80
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLlDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------------KLGE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYF-------YDELTLKEmknIIAPSYTDWDEPVFQDYIKQFNLN---LKQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:COG0488 377 TVKIGYFdqhqeelDPDKTVLD---ELRDGAPGGTEQEVRGYLGRFLFSgddAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 151 LLMDEPTSGLDPLVRSELMDILLNFmkePGkSVFFSTHitsD---LDKIADMIILIDDGKI 208
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDF---PG-TVLLVSH---DryfLDRVATRILEFEDGGV 507
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-209 |
5.84e-23 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 96.85 E-value: 5.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND---MDKHERKS--KNKIGIVLDEGYFYDELTL 93
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENimkQSPVELREvrRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 KEmkNI-IAPSYTDWDEPVFQ----DYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRS 166
Cdd:TIGR01186 89 LQ--NTsLGPELLGWPEQERKekalELLKLVGLEeyEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1261293288 167 ELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKIL 209
Cdd:TIGR01186 167 SMQDELKKLQATLQKTIVFITH---DLDeaiRIGDRIVIMKAGEIV 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-194 |
6.60e-23 |
|
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: 93.69 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKsknkIG 79
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD----RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IVLDEGYFYDELTLkeMKNIIAP------SYTDWDEPVfQDYIKQFNL--NLKQKISTLSKGMRMKFAVALALSHHADLL 151
Cdd:cd03293 77 YVFQQDALLPWLTV--LDNVALGlelqgvPKAEARERA-EELLELVGLsgFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1261293288 152 LMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD 194
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTH---DID 193
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-208 |
2.47e-22 |
|
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: 92.40 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNkIGIVLDE 84
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-ISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 85 GYFYDELTLKE-----MKNIIAPSYTDwDEPVFQdyIKQFnLN----LKQKISTLSKGMRMKFAVALALSHHADLLLMDE 155
Cdd:cd03299 80 YALFPHMTVYKniaygLKKRKVDKKEI-ERKVLE--IAEM-LGidhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261293288 156 PTSGLDPLVRSELMDILLNFMKEPGKSVFfstHITSDLDKI---ADMIILIDDGKI 208
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVL---HVTHDFEEAwalADKVAIMLNGKL 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-194 |
5.70e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.07 E-value: 5.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGndmdKHERKSK 75
Cdd:COG1116 4 AAPALELRGVSKRFPTGGggvtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 NKIGIVLDEGYFYDELTLKEmkNIIAP------SYTDWDEPVfQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHH 147
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLD--NVALGlelrgvPKAERRERA-RELLELVGLAgfEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261293288 148 ADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD 194
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH---DVD 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-208 |
8.03e-22 |
|
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: 89.41 E-value: 8.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLd 83
Cdd:cd03216 1 LELRGITKRFGGVkALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 egyfydeltlkemkniiapsytdwdepVFQdyikqfnlnlkqkistLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPL 163
Cdd:cd03216 80 ---------------------------VYQ----------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1261293288 164 VRSELMDILLNFmKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03216 117 EVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-208 |
1.04e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 91.27 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE----RKSKNK 77
Cdd:COG3638 2 MLELRNLSKRYPGgtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgralRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIVLDEGYFYDELTLkeMKNIIA-------------PSYTDWDEPVFQDYIKQFNL--NLKQKISTLSKGMRMKFAVAL 142
Cdd:COG3638 82 IGMIFQQFNLVPRLSV--LTNVLAgrlgrtstwrsllGLFPPEDRERALEALERVGLadKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 143 ALSHHADLLLMDEPTSGLDPlVRSE-LMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKI 208
Cdd:COG3638 160 ALVQEPKLILADEPVASLDP-KTARqVMDLLRRIAREDGITVVVNLH---QVDlarRYADRIIGLRDGRV 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-209 |
1.32e-21 |
|
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: 90.29 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK---HERkSKNKIGI 80
Cdd:cd03218 1 LRAENLSKRYGKRKvVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHKR-ARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDELTLKEmkNIIA------PSYTDWDEPVfQDYIKQFNL--NLKQKISTLSKGMRMKFAVALALSHHADLLL 152
Cdd:cd03218 80 LPQEASIFRKLTVEE--NILAvleirgLSKKEREEKL-EELLEEFHIthLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 153 MDEPTSGLDPLVRSELMDIlLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKI-IKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVL 212
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-209 |
1.83e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 92.48 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 9 NLNKCYENFSLkDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERK-----SKNKIGIVLD 83
Cdd:TIGR02142 4 RFSKRLGDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiflppEKRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKE-----MKNIIAPSYTDWDEPVfqdyIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEP 156
Cdd:TIGR02142 83 EARLFPHLSVRGnlrygMKRARPSERRISFERV----IELLGIGhlLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 157 TSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-209 |
2.42e-21 |
|
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: 90.78 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-----KNKIGIVLDEGYFYDELTL 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 KEmkNI-----IAPSYTDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRS 166
Cdd:cd03294 120 LE--NVafgleVQGVPRAEREERAAEALELVGLEgwEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1261293288 167 ELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKIL 209
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITH---DLDealRLGDRIAIMKDGRLV 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-208 |
3.10e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 93.54 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 7 VNNLNKCYENFSLK-----DVTFRISNdcITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIV 81
Cdd:TIGR01257 931 VKNLVKIFEPSGRPavdrlNITFYENQ--ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYDELTLKEMKNIIAP-SYTDWDEPVFQ--DYIKQFNLNLK--QKISTLSKGMRMKFAVALALSHHADLLLMDEP 156
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQlKGRSWEEAQLEmeAMLEDTGLHHKrnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 157 TSGLDPLVRSELMDILLNFmkEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-208 |
4.13e-21 |
|
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: 88.85 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNkIGIVLD 83
Cdd:cd03301 1 VELENVTKRFGNVtALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEmkNIIAP------SYTDWDEPVFQ-DYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEP 156
Cdd:cd03301 80 NYALYPHMTVYD--NIAFGlklrkvPKDEIDERVREvAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 157 TSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-208 |
1.32e-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: 87.20 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKN---KIGI 80
Cdd:cd03262 1 IEIKNLHKSFGDFHvLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDELTLKEmkNIIAPSYTDWDEPVFQ------DYIKQFNLNLKQK--ISTLSKGMRMKFAVALALSHHADLLL 152
Cdd:cd03262 81 VFQQFNLFPHLTVLE--NITLAPIKVKGMSKAEaeeralELLEKVGLADKADayPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261293288 153 MDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-208 |
1.43e-20 |
|
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: 86.93 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 16 NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKnkIGIVLDEGYF-------Y 88
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS--IGYVMQDVDYqlftdsvR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 89 DELTLKeMKNiiapsyTDWDEPVFQDYIKQFNLN-LKQKIS-TLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPlvrs 166
Cdd:cd03226 91 EELLLG-LKE------LDAGNEQAETVLKDLDLYaLKERHPlSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY---- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1261293288 167 ELMDILLNFMKE---PGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03226 160 KNMERVGELIRElaaQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-208 |
2.66e-20 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 86.39 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 31 ITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMdKHERKSKNKIGIVLDEGYFYDELTLKEmkNI---IAPSY--T 105
Cdd:cd03298 26 ITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQ--NVglgLSPGLklT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 106 DWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSV 183
Cdd:cd03298 103 AEDRQAIEVALARVGLAglEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTV 182
|
170 180
....*....|....*....|....*
gi 1261293288 184 FFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03298 183 LMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-220 |
3.40e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 88.67 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND----MDKHERksknKIG 79
Cdd:COG1118 3 IEVRNISKRFGSFTlLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnLPPRER----RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IVldegyF--YD---ELTLKEmkNI------IAPSYTDWDEPVfQDYIKQFNL-NL-KQKISTLSKGMRMKFAVALALSH 146
Cdd:COG1118 79 FV-----FqhYAlfpHMTVAE--NIafglrvRPPSKAEIRARV-EELLELVQLeGLaDRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 147 HADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKILVNDEKDMLIDS 220
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTH---DQEealELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-209 |
4.01e-20 |
|
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: 86.72 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND---MDKHERkskNKIGI 80
Cdd:cd03219 1 LEVRGLTKRFGGLVaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEI---ARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDegyF-----YDELTLKEmkNIIAP-----SYTDWDEPVFQ----------DYIKQFNLN--LKQKISTLSKGMRMKF 138
Cdd:cd03219 78 GRT---FqiprlFPELTVLE--NVMVAaqartGSGLLLARARReereareraeELLERVGLAdlADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 139 AVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKIL 209
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVLLVEH---DMDvvmSLADRVTVLDQGRVI 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
4-209 |
8.00e-20 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 85.42 E-value: 8.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNnLNKCYENFSLKdVTFRISNDcITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGN---------DMDKHERKs 74
Cdd:cd03297 1 MLCVD-IEKRLPDFTLK-IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkiNLPPQQRK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 75 knkIGIVLDEGYFYDELTLKEmkNII--APSYTDWDEPVFQDYIKQ-FNLN--LKQKISTLSKGMRMKFAVALALSHHAD 149
Cdd:cd03297 77 ---IGLVFQQYALFPHLNVRE--NLAfgLKRKRNREDRISVDELLDlLGLDhlLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 150 LLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-214 |
8.88e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 8.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS--LKDVTFRISndciTG----FIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS--- 74
Cdd:COG2884 1 MIRFENVSKRYPGGReaLSDVSLEIE----KGefvfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 75 -KNKIGIVLDEGYFYDELTLKEmkNIIAP------SYTDWDEPVfQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALS 145
Cdd:COG2884 77 lRRRIGVVFQDFRLLPDRTVYE--NVALPlrvtgkSRKEIRRRV-REVLDLVGLSdkAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 146 HHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHitsDLDKIADM---IILIDDGKIlVNDEK 214
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATH---DLELVDRMpkrVLELEDGRL-VRDEA 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-208 |
1.18e-19 |
|
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: 85.47 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNkIGIVLD 83
Cdd:cd03296 3 IEVRNVSKRFGDFvALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELT--------LKEMKNIIAPSYTDWDEPVfQDYIKQFNL-NLKQKI-STLSKGMRMKFAVALALSHHADLLLM 153
Cdd:cd03296 82 HYALFRHMTvfdnvafgLRVKPRSERPPEAEIRAKV-HELLKLVQLdWLADRYpAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 154 DEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-209 |
3.24e-19 |
|
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: 83.77 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLI-----LKDSGKINFLG---NDMDKHERKSK 75
Cdd:cd03260 1 IELRDLNVYYGDKHaLKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 NKIGIVLDE-----GYFYDELTL----------KEMKNIIAPSYTD---WDEpvfqdyikqfnLNLKQKISTLSKGMRMK 137
Cdd:cd03260 81 RRVGMVFQKpnpfpGSIYDNVAYglrlhgiklkEELDERVEEALRKaalWDE-----------VKDRLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 138 FAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPgkSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-208 |
3.47e-19 |
|
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: 82.75 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS---LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIV 81
Cdd:cd03247 1 LSINNVSFSYPEQEqqvLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYDElTLKEmkniiapsytdwdepvfqdyikqfNLNLKqkistLSKGMRMKFAVALALSHHADLLLMDEPTSGLD 161
Cdd:cd03247 81 NQRPYLFDT-TLRN------------------------NLGRR-----FSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261293288 162 PLVRSELMDILLNFMKEpgKSVFFSTHITSDLDKiADMIILIDDGKI 208
Cdd:cd03247 131 PITERQLLSLIFEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKI 174
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-209 |
3.66e-19 |
|
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: 82.98 E-value: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLI--LKDSGKInfLGNDMDKHERKSKNKIGIVLDEGYFYDELTLKEM 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEV--LINGRPLDKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 97 KniiapsytdwdepvfqdyikQFNLNLKQkistLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFM 176
Cdd:cd03213 103 L--------------------MFAAKLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA 158
|
170 180 190
....*....|....*....|....*....|....
gi 1261293288 177 KEpGKSVFFSTHITSDLD-KIADMIILIDDGKIL 209
Cdd:cd03213 159 DT-GRTIICSIHQPSSEIfELFDKLLLLSQGRVI 191
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-208 |
6.27e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCY-----------------------ENFSLKDVTFRI-SNDCItGFIGTNGSGKTTTIKAILGLILKD 56
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrrtrreEFWALKDVSFEVeRGESV-GIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 57 SGKInflgndmdkherKSKNKIGIVLDEGY-FYDELTLKEmkNII--------APSYTDwdePVFqDYIKQF-NLN--LK 124
Cdd:COG1134 80 SGRV------------EVNGRVSALLELGAgFHPELTGRE--NIYlngrllglSRKEID---EKF-DEIVEFaELGdfID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 125 QKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILID 204
Cdd:COG1134 142 QPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
....
gi 1261293288 205 DGKI 208
Cdd:COG1134 221 KGRL 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-208 |
9.22e-19 |
|
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: 82.63 E-value: 9.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMD----KHERKS 74
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 75 KNKIGIVLDEGYFYDELTLKEmkNIIAP------SYTDWDEPVfQDYIKQFNLNLKQKI--STLSKGMRMKFAVALALSH 146
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFE--NVALPleiagvPKAEIEERV-LELLELVGLEDKADAypAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 147 HADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-188 |
9.43e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 81.70 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDkHERKS----KNKIGIVLDEGyfyDEltlk 94
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGllerRQRVGLVFQDP---DD---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 95 emkNIIAPSytdwdepVFQDY-IKQFNLNL----------------------KQKISTLSKGMRMKFAVALALSHHADLL 151
Cdd:TIGR01166 80 ---QLFAAD-------VDQDVaFGPLNLGLseaeverrvrealtavgasglrERPTHCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 1261293288 152 LMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTH 188
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRR-LRAEGMTVVISTH 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-223 |
1.15e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE--RKSKNK 77
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtaKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIVLDEGYFYDELTLKE---MKNIIA--PSYTDWDEPVFQDYIKQFNLNLkQKISTLSKGMRMKFAVALALSHHADLLL 152
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEEnlaMGGFFAerDQFQERIKWVYELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 153 MDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDSHAL 223
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-207 |
2.90e-18 |
|
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: 79.03 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKInflgndmdkhERKSKNKIGivld 83
Cdd:cd03221 1 IELENLSKTYGGKLLlKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------TWGSTVKIG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 egyfydeltlkemkniiapsytdwdepvfqdYIKQfnlnlkqkistLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPL 163
Cdd:cd03221 67 -------------------------------YFEQ-----------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1261293288 164 VRSELMDILLNFmkePGkSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:cd03221 105 SIEALEEALKEY---PG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-208 |
2.96e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.35 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKCY---ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE-RKSKNK 77
Cdd:PRK13632 5 SVMIKVENVSFSYpnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIVL-------------DEGYFYDE---LTLKEMKNIIApsytdwdepvfqDYIKQFNLN--LKQKISTLSKGMRMKFA 139
Cdd:PRK13632 85 IGIIFqnpdnqfigatveDDIAFGLEnkkVPPKKMKDIID------------DLAKKVGMEdyLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 140 VALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFfstHITSDLDKI--ADMIILIDDGKI 208
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLI---SITHDMDEAilADKVIVFSEGKL 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-199 |
4.69e-18 |
|
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: 82.41 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCY--ENFSLK---DVTFRISNDCITGFIGTNGSGKTTTIKAILGLI---LKDSGKINFLGND---MDKHER 72
Cdd:COG0444 1 LLEVRNLKVYFptRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDllkLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 73 KS--KNKIGIVldegyFYDELT----LKEMKNIIA--------PSYTDWDEPVfQDYIKQFNLNLKQKI-----STLSKG 133
Cdd:COG0444 81 RKirGREIQMI-----FQDPMTslnpVMTVGDQIAeplrihggLSKAEARERA-IELLERVGLPDPERRldrypHELSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 134 MRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDL-------DKIADM 199
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH---DLgvvaeiaDRVAVM 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
4-209 |
4.89e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 82.84 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNnLNKCYENFSLkDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGN---DMDK------HERKs 74
Cdd:COG4148 2 MLEVD-FRLRRGGFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgiflppHRRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 75 knkIGIVLDEGYFYDELTLKE-----MKNIIAPSytdwDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHH 147
Cdd:COG4148 79 ---IGYVFQEARLFPHLSVRGnllygRKRAPRAE----RRISFDEVVELLGIGhlLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 148 ADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLDKI---ADMIILIDDGKIL 209
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSH---SLDEVarlADHVVLLEQGRVV 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-209 |
5.60e-18 |
|
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: 80.73 E-value: 5.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 6 EVNNLNKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVL 82
Cdd:cd03254 4 EFENVNFSYDEkkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDElTLKEmkNIIAPSYTDWDEPV--------FQDYIKQ----FNLNLKQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:cd03254 84 QDTFLFSG-TIME--NIRLGRPNATDEEVieaakeagAHDFIMKlpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 151 LLMDEPTSGLDPLVRSELMDILLNFMKepGKSVFFSTHITSDLdKIADMIILIDDGKIL 209
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDDGKII 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-208 |
5.74e-18 |
|
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: 80.27 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGndmdkherksknKIGIVLDEGYFYD-ELTLKEmk 97
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGLGGGFNpELTGRE-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 98 NII------APSYTDWDEpvFQDYIKQFN-LN--LKQKISTLSKGMRMK--FAVALALSHhaDLLLMDEPTSGLDPLVRs 166
Cdd:cd03220 104 NIYlngrllGLSRKEIDE--KIDEIIEFSeLGdfIDLPVKTYSSGMKARlaFAIATALEP--DILLIDEVLAVGDAAFQ- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1261293288 167 ELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-209 |
6.83e-18 |
|
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: 80.39 E-value: 6.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKCYEnfSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKD---SGKINFLGNDMDKHerKSKNKI 78
Cdd:cd03234 8 DVGLKAKNWNKYAR--ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPD--QFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 GIVLDEGYFYDELTLKE----MKNIIAPSYTDWDEPVFQDYIKQFN-LNLKQ----KISTLSKGMRMKFAVALALSHHAD 149
Cdd:cd03234 84 AYVRQDDILLPGLTVREtltyTAILRLPRKSSDAIRKKRVEDVLLRdLALTRiggnLVKGISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 150 LLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHI-TSDLDKIADMIILIDDGKIL 209
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-208 |
7.85e-18 |
|
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: 79.94 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY---ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK-HERKSKNKIGI 80
Cdd:cd03245 3 IEFRNVSFSYpnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGY-FYDelTLKEMKNIIAPSYTDWD----------EPVFQDYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHAD 149
Cdd:cd03245 83 VPQDVTlFYG--TLRDNITLGAPLADDERilraaelagvTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 150 LLLMDEPTSGLDplVRSELMdiLLNFMKE--PGKSVFFSTHITSDLDkIADMIILIDDGKI 208
Cdd:cd03245 161 ILLLDEPTSAMD--MNSEER--LKERLRQllGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-208 |
1.06e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 82.51 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYEN---FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGI 80
Cdd:COG4987 334 LELEDVSFRYPGagrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDElTLKEmkNI-IA-PSYTD---WD-------EPVFQDYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHA 148
Cdd:COG4987 414 VPQRPHLFDT-TLRE--NLrLArPDATDeelWAalervglGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 149 DLLLMDEPTSGLDPLVRSELMDILLNFMKepGKSVFFSTHITSDLDKiADMIILIDDGKI 208
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRI 547
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-209 |
1.64e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.06 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYEN---FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE----RK 73
Cdd:PRK13635 2 KEEIIRVEHISFRYPDaatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 74 sknKIGIVL-------------DEGYFYDEltlkemkNIIAPSytdwDEPV--FQDYIKQFNLN--LKQKISTLSKGMRM 136
Cdd:PRK13635 82 ---QVGMVFqnpdnqfvgatvqDDVAFGLE-------NIGVPR----EEMVerVDQALRQVGMEdfLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 137 KFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFfstHITSDLDKIA--DMIILIDDGKIL 209
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVL---SITHDLDEAAqaDRVIVMNKGEIL 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-225 |
2.22e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDS---GKINFLGNDM-DKHERKSKNKIGIVL------------ 82
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLtAKTVWDIREKVGIVFqnpdnqfvgatv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 -DEGYFYDE---LTLKEMKNIIAPSYTDWDepvFQDYIKQfnlnlkqKISTLSKGMRMKFAVALALSHHADLLLMDEPTS 158
Cdd:PRK13640 103 gDDVAFGLEnraVPRPEMIKIVRDVLADVG---MLDYIDS-------EPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 159 GLDPLVRSELMDILLNFMKEPGKSVFfstHITSDLDK--IADMIILIDDGKILVNDEKDMLIDSHALIK 225
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVI---SITHDIDEanMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-199 |
3.29e-17 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 81.18 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS--LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNK-IGIV 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpaLRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYdELTLKEmkNII----APSYTDWDEPVFQDYIKQFNLNLKQKIST--------LSKGMRMKFAVALALSHHAD 149
Cdd:TIGR02857 402 PQHPFLF-AGTIAE--NIRlarpDASDAEIREALERAGLDEFVAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 150 LLLMDEPTSGLDPLVRSELMDILLNFMKepGKSVFFSTH---ITSDLDKIADM 199
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHrlaLAALADRIVVL 529
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-239 |
4.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.10 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 14 YENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLG-----NDMDKHERKSKNKIGIVLD--EGY 86
Cdd:PRK13641 18 MEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpETGNKNLKKLRKKVSLVFQfpEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 87 FYDELTLKEM----KNIiapSYTDwDEPVFQ--DYIKQFNLN---LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:PRK13641 98 LFENTVLKDVefgpKNF---GFSE-DEAKEKalKWLKKVGLSedlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 158 SGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKILVNDE-KDMLIDSHALIKgsnRFINEQTK 236
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASpKEIFSDKEWLKK---HYLDEPAT 249
|
...
gi 1261293288 237 NLF 239
Cdd:PRK13641 250 SRF 252
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
4.53e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.01 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYE--NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMD-KHERKSKNK 77
Cdd:PRK13647 1 MDNIIEVEDLHFRYKdgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIVL---DEGYFydeltlkemkniiapSYTDWDEPVF----------------QDYIKQFNL-NLKQKIST-LSKGMRM 136
Cdd:PRK13647 81 VGLVFqdpDDQVF---------------SSTVWDDVAFgpvnmgldkdeverrvEEALKAVRMwDFRDKPPYhLSYGQKK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 137 KFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHitsDLD---KIADMIILIDDGKILVNDE 213
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATH---DVDlaaEWADQVIVLKEGRVLAEGD 221
|
....*.
gi 1261293288 214 KDMLID 219
Cdd:PRK13647 222 KSLLTD 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-221 |
6.06e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.55 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 21 DVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGivldegY----F--YDELTLK 94
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVG------YmsqaFslYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 95 EmkNI--------IAPsyTDWDEPVfQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLV 164
Cdd:NF033858 358 Q--NLelharlfhLPA--AEIAARV-AEMLERFDLAdvADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 165 RSELMDILLNFMKEPGKSVFFSTHITSDldkiA---DMIILIDDGKILVNDEKDMLIDSH 221
Cdd:NF033858 433 RDMFWRLLIELSREDGVTIFISTHFMNE----AercDRISLMHAGRVLASDTPAALVAAR 488
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
19-223 |
1.11e-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: 77.43 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGK-INFLGNDMDKHE-RKSKNKIGIV---LDEgYFYDELTL 93
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDvWELRKRIGLVspaLQL-RFPRDETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 KEMknII---------APSYTDWDEPVFQDYIKQFNLN-LKQK-ISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:COG1119 98 LDV--VLsgffdsiglYREPTDEQRERARELLELLGLAhLADRpFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 163 LVRSELMDILLNFMKEPGKSVFFSTHitsDLDKIADMI---ILIDDGKILVNDEKDMLIDSHAL 223
Cdd:COG1119 176 GARELLLALLDKLAAEGAPTLVLVTH---HVEEIPPGIthvLLLKDGRVVAAGPKEEVLTSENL 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-209 |
1.73e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 78.22 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK---HERkskn 76
Cdd:COG3842 2 AMPALELENVSKRYGDVTaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEKR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 77 KIGIvldegyfydeltlkemkniiapsytdwdepVFQDY---------------------------------IKQFNLN- 122
Cdd:COG3842 78 NVGM------------------------------VFQDYalfphltvaenvafglrmrgvpkaeirarvaelLELVGLEg 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 123 -LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsdlDK-----I 196
Cdd:COG3842 128 lADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH-----DQeealaL 202
|
250
....*....|...
gi 1261293288 197 ADMIILIDDGKIL 209
Cdd:COG3842 203 ADRIAVMNDGRIE 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-209 |
2.45e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHER---KSKNKIGIVL---DEGYFYDEL- 91
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVATVFqdpEQQIFYTDId 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 92 -----TLKEMKNIIAPSYTDWDEPVFQDYIKQFNlnlKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRS 166
Cdd:PRK13638 97 sdiafSLRNLGVPEAEITRRVDEALTLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1261293288 167 ELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK13638 174 QMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-208 |
2.68e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 7 VNNLNKCYENFSL-KDVTFRIS-NDCItGFIGTNGSGKTTTIKAILGLILKDSGKINflgndMDKHERksknkIGIVLDE 84
Cdd:COG0488 1 LENLSKSFGGRPLlDDVSLSINpGDRI-GLVGRNGAGKSTLLKILAGELEPDSGEVS-----IPKGLR-----IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 85 GYFYDELT--------LKEMKNIIA--------PSYTDWDEPVFQDYIKQF-----------------NLNLK-----QK 126
Cdd:COG0488 70 PPLDDDLTvldtvldgDAELRALEAeleeleakLAEPDEDLERLAELQEEFealggweaearaeeilsGLGFPeedldRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 127 ISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDplvrselMD-I--LLNFMKEPGKSVFFSTHitsD---LDKIADMI 200
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LEsIewLEEFLKNYPGTVLVVSH---DryfLDRVATRI 219
|
....*...
gi 1261293288 201 ILIDDGKI 208
Cdd:COG0488 220 LELDRGKL 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-208 |
3.04e-16 |
|
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: 75.74 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRI-SNDCITgFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK---HERKsknkIG 79
Cdd:cd03300 1 IELENVSKFYGGFvALDGVSLDIkEGEFFT-LLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKRP----VN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IVLDEGYFYDELTLKEmkNIIAP------SYTDWDEPVfQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLL 151
Cdd:cd03300 76 TVFQNYALFPHLTVFE--NIAFGlrlkklPKAEIKERV-AEALDLVQLEgyANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 152 LMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-209 |
5.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 11 NKCYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINF-----LGNDMDKHERKSKNKIGIVLD-- 83
Cdd:PRK13643 14 NSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvSSTSKQKEIKPVRKKVGVVFQfp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEMKniIAPS----YTDWDEPVFQDYIKQFNLN---LKQKISTLSKGMRMKFAVALALSHHADLLLMDEP 156
Cdd:PRK13643 94 ESQLFEETVLKDVA--FGPQnfgiPKEKAEKIAAEKLEMVGLAdefWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 157 TSGLDPLVRSELMDiLLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK13643 172 TAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-208 |
5.39e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.24 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 14 YENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKN---KIGIVLDegyfYDE 90
Cdd:PRK13637 18 FEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirkKVGLVFQ----YPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 91 LTLKE---MKNI-IAPSYTDW-DEPVFQDYIKQFNL------NLKQKIS-TLSKGMRMKFAVALALSHHADLLLMDEPTS 158
Cdd:PRK13637 94 YQLFEetiEKDIaFGPINLGLsEEEIENRVKRAMNIvgldyeDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261293288 159 GLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-208 |
6.18e-16 |
|
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: 74.75 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS----KNKI 78
Cdd:cd03292 1 IEFINVTKTYPNgtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 GIVLDEGYFYDELTLKE-----MKnIIAPSYTDWDEPVfQDYIKQfnLNLKQKIST----LSKGMRMKFAVALALSHHAD 149
Cdd:cd03292 81 GVVFQDFRLLPDRNVYEnvafaLE-VTGVPPREIRKRV-PAALEL--VGLSHKHRAlpaeLSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 150 LLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-209 |
6.72e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.83 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 14 YENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINfLGNDMDKHERKSKN------KIGIVLD--EG 85
Cdd:PRK13634 18 FERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVITAGKKNKKlkplrkKVGIVFQfpEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 86 YFYDELTLKEM----KNIIAPsytdwDEPVFQDYIKQFNL-NLKQKIST-----LSKG-MRmKFAVALALSHHADLLLMD 154
Cdd:PRK13634 97 QLFEETVEKDIcfgpMNFGVS-----EEDAKQKAREMIELvGLPEELLArspfeLSGGqMR-RVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 155 EPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-206 |
1.08e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 18 SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK--HERKSKNKIGIVLDEGYFYDELTLKE 95
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldHKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 96 --------MKNIIAPSYTDWDEPVFQDYIKQFNLNLK----QKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPL 163
Cdd:PRK09700 100 nlyigrhlTKKVCGVNIIDWREMRVRAAMMLLRVGLKvdldEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1261293288 164 VRSELMDIlLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDG 206
Cdd:PRK09700 180 EVDYLFLI-MNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-208 |
1.35e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCY----ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM-DKHERKSK 75
Cdd:PRK13650 1 MSNIIEVKNLTFKYkedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 NKIGIVL-------------DEGYFYDE---LTLKEMKNIIAPSYTDWDEPVFQDyikqfnlnlkQKISTLSKGMRMKFA 139
Cdd:PRK13650 81 HKIGMVFqnpdnqfvgatveDDVAFGLEnkgIPHEEMKERVNEALELVGMQDFKE----------REPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 140 VALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFfstHITSDLDKIA--DMIILIDDGKI 208
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVI---SITHDLDEVAlsDRVLVMKNGQV 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-209 |
1.37e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 14 YENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKiNFLGN-------DMDKHERKSKNKIGIVLD--E 84
Cdd:PRK13645 22 FEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDyaipanlKKIKEVKRLRKEIGLVFQfpE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 85 GYFYDELTLKEMKniIAPSYTDWDE-------PVFQDYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:PRK13645 101 YQLFQETIEKDIA--FGPVNLGENKqeaykkvPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 158 SGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-208 |
1.56e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.40 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 15 ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE-RKSKNKIGIVLD--EGYF---- 87
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKHIGIVFQnpDNQFvgsi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 88 --YD--------ELTLKEMKNIIAPSYTDWDEPVFQDYIKQfnlnlkqkisTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:PRK13648 101 vkYDvafglenhAVPYDEMHRRVSEALKQVDMLERADYEPN----------ALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 158 SGLDPLVRSELMDiLLNFMKEPGKSVFFSthITSDLDKI--ADMIILIDDGKI 208
Cdd:PRK13648 171 SMLDPDARQNLLD-LVRKVKSEHNITIIS--ITHDLSEAmeADHVIVMNKGTV 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-209 |
1.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.82 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 14 YENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFlgNDM-------DKHERKSKNKIGIVLD--E 84
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDItithktkDKYIRPVRKRIGMVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 85 GYFYDELTLKEMknIIAPSYTDWDEPVFQDYIKQFNLNL-------KQKISTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:PRK13646 96 SQLFEDTVEREI--IFGPKNFKMNLDEVKNYAHRLLMDLgfsrdvmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 158 SGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-223 |
1.83e-15 |
|
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: 73.67 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVLDEGYFYDElTLKEmk 97
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWlRRQVGVVLQENVLFNR-SIRD-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 98 NIiapSYTDWDEPVFQ-----------DYIKQ----FNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDp 162
Cdd:cd03252 95 NI---ALADPGMSMERvieaaklagahDFISElpegYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD- 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 163 lVRSElmDILLNFMKE--PGKSVFFSTHITSDLdKIADMIILIDDGKILVNDEKDMLIDSHAL 223
Cdd:cd03252 171 -YESE--HAIMRNMHDicAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-208 |
1.89e-15 |
|
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: 72.46 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLNKcyeNFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVL 82
Cdd:cd03215 3 PVLEVRGLSV---KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 ------DEGYFyDELTLKEmkNIIAPSYtdwdepvfqdyikqfnlnlkqkistLSKGMRMKFAVALALSHHADLLLMDEP 156
Cdd:cd03215 80 vpedrkREGLV-LDLSVAE--NIALSSL-------------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 157 TSGLDPLVRSELMDILLNfMKEPGKSVFFsthITSDLDKI---ADMIILIDDGKI 208
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRE-LADAGKAVLL---ISSELDELlglCDRILVMYEGRI 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-210 |
2.03e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 73.52 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK---HERKSKnkiG 79
Cdd:COG1137 3 TLEAENLVKSYGKRTvVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRARL---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IvldeGYFYDE------LTLKEmkNIIA------PSYTDWDEPVfQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALS 145
Cdd:COG1137 80 I----GYLPQEasifrkLTVED--NILAvlelrkLSKKEREERL-EELLEEFGIThlRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 146 HHADLLLMDEPTSGLDPLVRSELMDILLnFMKEPGKSVFfsthITsdlD-------KIADMIILIDDGKILV 210
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIR-HLKERGIGVL----IT---DhnvretlGICDRAYIISEGKVLA 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-208 |
3.34e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.05 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKcyeNFS----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMD-KHERKSK 75
Cdd:COG1129 1 AEPLLEMRGISK---SFGgvkaLDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 NK-IGIVldegyfYDELTL-------------KEMKN--IIapsytDWDEPV--FQDYIKQFNLNL--KQKISTLSKGMR 135
Cdd:COG1129 78 AAgIAII------HQELNLvpnlsvaeniflgREPRRggLI-----DWRAMRrrARELLARLGLDIdpDTPVGDLSVAQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261293288 136 MKFAVALALSHHADLLLMDEPTSGLDPlvrSELmDILLNFM---KEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTE---REV-ERLFRIIrrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-207 |
3.57e-15 |
|
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: 72.50 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 16 NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGndmdkherksknKIGIVLDEGYFYDElTLKE 95
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 96 mkNIIAPSytDWDEPVFQDYIK--QFNLNLKQ-----------KISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:cd03250 85 --NILFGK--PFDEERYEKVIKacALEPDLEIlpdgdlteigeKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1261293288 163 LVRSELMD-ILLNFMKEpGKSVFFSTHITSDLDKiADMIILIDDGK 207
Cdd:cd03250 161 HVGRHIFEnCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
124-208 |
4.70e-15 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 74.37 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 124 KQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMI 200
Cdd:COG4175 158 DSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITH---DLDealRLGDRI 234
|
....*...
gi 1261293288 201 ILIDDGKI 208
Cdd:COG4175 235 AIMKDGRI 242
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-208 |
6.77e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.43 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVLDEGY-FYDelTLKEm 96
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlRRQIGVVPQDTFlFSG--TIRE- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 97 kNII--APSYTDwDEpVFQ--------DYIKQFNLNLKQKI----STLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:COG1132 433 -NIRygRPDATD-EE-VEEaakaaqahEFIEALPDGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDT 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261293288 163 LVRSELMDILLNFMKepGKSVFFSTH----ItsdldKIADMIILIDDGKI 208
Cdd:COG1132 510 ETEALIQEALERLMK--GRTTIVIAHrlstI-----RNADRILVLDDGRI 552
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-244 |
7.57e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDS---GKINFLGNDMDKHE----- 71
Cdd:PRK09984 1 MQTIIRVEKLAKTFnQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGrlard 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 72 -RKSKNKIGIVLDEGYFYDELTLKEMKNIIAPSYTdwdePVFQDYIKQFNLNLKQ-----------------KISTLSKG 133
Cdd:PRK09984 81 iRKSRANTGYIFQQFNLVNRLSVLENVLIGALGST----PFWRTCFSWFTREQKQralqaltrvgmvhfahqRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 134 MRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDe 213
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG- 235
|
250 260 270
....*....|....*....|....*....|.
gi 1261293288 214 kdmlidshalikGSNRFINEQTKNLFLNLHQ 244
Cdd:PRK09984 236 ------------SSQQFDNERFDHLYRSINR 254
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-240 |
8.77e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 8.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMD---KHERkSKNKIGI 80
Cdd:PRK10895 4 LTAKNLAKAYKGRRVvEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHAR-ARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDELT--------LKEMKNIIAPSYTDWDEPVFQDY-IKQFNLNLKQkisTLSKGMRMKFAVALALSHHADLL 151
Cdd:PRK10895 83 LPQEASIFRRLSvydnlmavLQIRDDLSAEQREDRANELMEEFhIEHLRDSMGQ---SLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 152 LMDEPTSGLDPLvrsELMDI--LLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDshalikgsnr 229
Cdd:PRK10895 160 LLDEPFAGVDPI---SVIDIkrIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ---------- 226
|
250
....*....|.
gi 1261293288 230 fiNEQTKNLFL 240
Cdd:PRK10895 227 --DEHVKRVYL 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
15-215 |
1.10e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 15 ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNK-IGIVLDEGYFYDELtl 93
Cdd:PRK10522 335 NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKlFSAVFTDFHLFDQL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 kemkniIAPSYTDWDEPVFQDYIKQFNLNLK-----QKIST--LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRS 166
Cdd:PRK10522 413 ------LGPEGKPANPALVEKWLERLKMAHKleledGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 167 ELMDILLNFMKEPGKSVFFSTHITSDLDKiADMIILIDDGKI--LVNDEKD 215
Cdd:PRK10522 487 EFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLseLTGEERD 536
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-201 |
1.12e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKInflgndmdkherksknKIGI 80
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI----------------EIGE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYfydeltLKEMKNIIAPSYTDWDE-----PVFQ---------DYIKQFNL---NLKQKISTLSKGMRMKFAVALA 143
Cdd:TIGR03719 384 TVKLAY------VDQSRDALDPNKTVWEEisgglDIIKlgkreipsrAYVGRFNFkgsDQQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 144 LSHHADLLLMDEPTSGLDPLVRSELMDILLNFmkePGKSVFFStHITSDLDKIADMII 201
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVIS-HDRWFLDRIATHIL 511
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-209 |
1.15e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDkHERKS----KNK 77
Cdd:PRK13636 5 ILKVEELNYNYSDgtHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGlmklRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIVL---DEGYF----YDELTLKEMkNIIAPSyTDWDEPVFQDYIKQFNLNLKQKIS-TLSKGMRMKFAVALALSHHAD 149
Cdd:PRK13636 84 VGMVFqdpDNQLFsasvYQDVSFGAV-NLKLPE-DEVRKRVDNALKRTGIEHLKDKPThCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 150 LLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLDKIA---DMIILIDDGKIL 209
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATH---DIDIVPlycDNVFVMKEGRVI 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-224 |
1.16e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS------LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND---MDKHERKSK 75
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 NKIGIVLDEGYFYDELTLKEM---------------------KNII--APSYTDWDEPVFQ---DYIKQFNLN---LKQK 126
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIrrrvgvvfqfaeyqlfeqtieKDIIfgPVSMGVSKEEAKKraaKYIELVGLDesyLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 127 ISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHitsDLDKI---ADMIILI 203
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTH---DLDNVlewTKRTIFF 238
|
250 260
....*....|....*....|..
gi 1261293288 204 DDGKILVN-DEKDMLIDSHALI 224
Cdd:PRK13651 239 KDGKIIKDgDTYDILSDNKFLI 260
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-201 |
1.22e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLNKCYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINflgndmdkherkSKNKIG--- 79
Cdd:PRK13409 339 TLVEYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------------PELKISykp 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 --IVLDegyfYD---ELTLKEMKNIIAPSYtdwdepVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLL 152
Cdd:PRK13409 407 qyIKPD----YDgtvEDLLRSITDDLGSSY------YKSEIIKPLQLErlLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1261293288 153 MDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMII 201
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-208 |
1.54e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLNKcyeNFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKH------------ 70
Cdd:COG1129 255 VVLEVEGLSV---GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRsprdairagiay 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 71 ---ERKSKnkiGIVLDegyfydeLTLKEmkNIIAPS---YTDW---DEP----VFQDYIKQFNL---NLKQKISTLSKGM 134
Cdd:COG1129 332 vpeDRKGE---GLVLD-------LSIRE--NITLASldrLSRGgllDRRreraLAEEYIKRLRIktpSPEQPVGNLSGGN 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 135 RMKfaVALA--LSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFsthITSDLD---KIADMIILIDDGKI 208
Cdd:COG1129 400 QQK--VVLAkwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIV---ISSELPellGLSDRILVMREGRI 472
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-209 |
3.20e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.41 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE---RKSKNKIG 79
Cdd:COG1126 1 MIEIENLHKSFGDLEvLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKkdiNKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IVldegyfydeltlkemkniiapsytdwdepvFQdyikQFNL--------NLkqkisTLS----KGMRMKFAVALA---- 143
Cdd:COG1126 81 MV------------------------------FQ----QFNLfphltvleNV-----TLApikvKKMSKAEAEERAmell 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 144 ----LSHHAD-------------------------LLLMDEPTSGLDPlvrsELMDILLNFMKE---PGKSVFFSTHits 191
Cdd:COG1126 122 ervgLADKADaypaqlsggqqqrvaiaralamepkVMLFDEPTSALDP----ELVGEVLDVMRDlakEGMTMVVVTH--- 194
|
250 260
....*....|....*....|.
gi 1261293288 192 DLD---KIADMIILIDDGKIL 209
Cdd:COG1126 195 EMGfarEVADRVVFMDGGRIV 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
128-229 |
3.80e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.48 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 128 STLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:PRK11247 132 AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
90 100
....*....|....*....|...
gi 1261293288 208 ILVndekDMLID-SHALIKGSNR 229
Cdd:PRK11247 212 IGL----DLTVDlPRPRRRGSAR 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-210 |
5.00e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFlgndmdkherksknkigiVLDEGYFYDELTLKEmkN 98
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------------------DVPDNQFGREASLID--A 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 99 IiaPSYTDWDEPVfqDYIKQFNLN----LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLN 174
Cdd:COG2401 106 I--GRKGDFKDAV--ELLNAVGLSdavlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1261293288 175 FMKEPGKSVFFSTH---ITSDLdkIADMIILIDDGKILV 210
Cdd:COG2401 182 LARRAGITLVVATHhydVIDDL--QPDLLIFVGYGGVPE 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-214 |
5.16e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.11 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCY------ENFSLKDVTFRI-SNDCITgFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK---HERk 73
Cdd:COG1101 1 MLELKNLSKTFnpgtvnEKRALDGLNLTIeEGDFVT-VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpeYKR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 74 SKNkIGIVldegyFYD-------ELTLKE---------MKNIIAPSYTDWDEPVFQDYIKQFNLNL----KQKISTLSKG 133
Cdd:COG1101 79 AKY-IGRV-----FQDpmmgtapSMTIEEnlalayrrgKRRGLRRGLTKKRRELFRELLATLGLGLenrlDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 134 MRMkfAVAL--ALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILV- 210
Cdd:COG1101 153 QRQ--ALSLlmATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILd 230
|
....*.
gi 1261293288 211 --NDEK 214
Cdd:COG1101 231 vsGEEK 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-209 |
5.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 14 YENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHerkSKNK--------IGIVLD-- 83
Cdd:PRK13649 18 FEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITST---SKNKdikqirkkVGLVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 EGYFYDELTLKEMkniiapSYTDWDEPVFQDYIKQF---NLNL--------KQKISTLSKGMRMKFAVALALSHHADLLL 152
Cdd:PRK13649 95 ESQLFEETVLKDV------AFGPQNFGVSQEEAEALareKLALvgiseslfEKNPFELSGGQMRRVAIAGILAMEPKILV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 153 MDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-209 |
5.54e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.76 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 22 VTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINF-LGN---DMDK---HER-KSKNKIGIVLDEGYFY----- 88
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDewvDMTKpgpDGRgRAKRYIGILHQEYDLYphrtv 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 89 -DELT----------LKEMKNIIAPSYTDWDEpvfqDYIKQFnlnLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:TIGR03269 383 lDNLTeaiglelpdeLARMKAVITLKMVGFDE----EKAEEI---LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 158 SGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKIL 209
Cdd:TIGR03269 456 GTMDPITKVDVTHSILKAREEMEQTFIIVSH---DMDfvlDVCDRAALMRDGKIV 507
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-208 |
6.60e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.88 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK-HERksKNKIGIVL 82
Cdd:PRK10851 3 IEIANIKKSFGRTQvLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHAR--DRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDELTLKEmkNI-----IAPSYtdwdEPVFQDYIKQFNLNLKQKI----------STLSKGMRMKFAVALALSHH 147
Cdd:PRK10851 81 QHYALFRHMTVFD--NIafgltVLPRR----ERPNAAAIKAKVTQLLEMVqlahladrypAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 148 ADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-207 |
7.04e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 7.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNdmdKHERKS----- 74
Cdd:COG3845 2 MPPALELRGITKRFGGVvANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRSprdai 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 75 KNKIGIV-----LdegyfYDELTLKEmkNII------APSYTDWDEPV--FQDYIKQFNL--NLKQKISTLSKGMRMKFA 139
Cdd:COG3845 79 ALGIGMVhqhfmL-----VPNLTVAE--NIVlgleptKGGRLDRKAARarIRELSERYGLdvDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 140 VALALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHitsDLD---KIADMIILIDDGK 207
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRR-LAAEGKSIIFITH---KLRevmAIADRVTVLRRGK 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-219 |
8.28e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.35 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLG---NDMDKHERKSKNKIG 79
Cdd:PRK09493 1 MIEFKNVSKHFgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IVLDEGYFYDELTLKEmkNII-APSYTdwdEPVFQDYIKQFNLNLKQKI----------STLSKGMRMKFAVALALSHHA 148
Cdd:PRK09493 81 MVFQQFYLFPHLTALE--NVMfGPLRV---RGASKEEAEKQARELLAKVglaerahhypSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 149 DLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLID 219
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-201 |
1.76e-13 |
|
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: 70.20 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLNKCYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKIN----------FLGNDMDKH-E 71
Cdd:COG1245 340 TLVEYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisykpqYISPDYDGTvE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 72 RKSKNKIGIVLDEGYFYDELtlkemkniiapsytdwdepvfqdyIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHAD 149
Cdd:COG1245 420 EFLRSANTDDFGSSYYKTEI------------------------IKPLGLEklLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 150 LLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMII 201
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-209 |
1.90e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMD-------KHERKSKN 76
Cdd:COG4161 3 IQLKNINCFYGSHqALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpseKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 77 KIGIVLDEGYFYDELTLkeMKNII-APsytdwdepvfqdyIKQFNLNLKQKIST--------------------LSKGMR 135
Cdd:COG4161 83 KVGMVFQQYNLWPHLTV--MENLIeAP-------------CKVLGLSKEQAREKamkllarlrltdkadrfplhLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 136 MKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-208 |
2.37e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.68 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHerksknkigiv 81
Cdd:PRK13652 3 LIETRDLCYSYSGskEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 ldegyfydelTLKEMKNIIAPSYTDWDEPVFQDYIKQ------FNLNL-----KQKIST-----------------LSKG 133
Cdd:PRK13652 72 ----------NIREVRKFVGLVFQNPDDQIFSPTVEQdiafgpINLGLdeetvAHRVSSalhmlgleelrdrvphhLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 134 MRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK13652 142 EKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-209 |
2.40e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLI-LKDSGKI---------NFLGNDMDK 69
Cdd:PRK14267 1 MKFAIETVNLRVYYgSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLeLNEEARVegevrlfgrNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 70 HErkSKNKIGIVLD------EGYFYDELTLKEMKNIIAPSYTDWDEPV--------FQDYIKQfnlNLKQKISTLSKGMR 135
Cdd:PRK14267 81 IE--VRREVGMVFQypnpfpHLTIYDNVAIGVKLNGLVKSKKELDERVewalkkaaLWDEVKD---RLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 136 MKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpgKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-209 |
2.47e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 2.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKCY------ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSG-----------KINFLG 64
Cdd:PRK13631 19 DIILRVKNLYCVFdekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 65 NDMDKHERKSKN------KIGIVL---DEGYFYDELTLKEMKNIIA---PSYTDWDEPVFqdYIKQFNLN---LKQKIST 129
Cdd:PRK13631 99 LITNPYSKKIKNfkelrrRVSMVFqfpEYQLFKDTIEKDIMFGPVAlgvKKSEAKKLAKF--YLNKMGLDdsyLERSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 130 LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-208 |
2.53e-13 |
|
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: 66.47 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY---ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNK-IGI 80
Cdd:cd03246 1 LEVENVSFRYpgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEgyfyDEL---TLKEmkNIiapsytdwdepvfqdyikqfnlnlkqkistLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:cd03246 81 LPQD----DELfsgSIAE--NI------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 158 SGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLdKIADMIILIDDGKI 208
Cdd:cd03246 125 SHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
130-208 |
3.47e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.08 E-value: 3.47e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 130 LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKepGKSVFFSTHITSDLDKIaDMIILIDDGKI 208
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-222 |
3.60e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 68.91 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 10 LNKCYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM----DKHERK-SKNKIGIVLDE 84
Cdd:PRK10070 35 LEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREvRRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 85 GYFYDELTLKE-----MKNIIAPSYTDWDEPVfqDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:PRK10070 115 FALMPHMTVLDntafgMELAGINAEERREKAL--DALRQVGLEnyAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 158 SGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDSHA 222
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-209 |
4.15e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS--LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMdKHERKS----KNK 77
Cdd:PRK13639 1 ILETRDLKYSYPDGTeaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSllevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIV------------LDEGYFYDELTLKEMKNIIAPSYTDWDEPV-FQDYikqfnlnLKQKISTLSKGMRMKFAVALAL 144
Cdd:PRK13639 80 VGIVfqnpddqlfaptVEEDVAFGPLNLGLSKEEVEKRVKEALKAVgMEGF-------ENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 145 SHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-207 |
6.81e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 18 SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLdegyFYDELTL---- 93
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISM----VHQELNLvlqr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 KEMKNIIAPSY------TDWDEpVFQDYIKQF-----NLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:PRK10982 89 SVMDNMWLGRYptkgmfVDQDK-MYRDTKAIFdeldiDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1261293288 163 LVRSELMDIlLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:PRK10982 168 KEVNHLFTI-IRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-209 |
6.83e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.96 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVL 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRiLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDE-LTLKEMkniIA----PSYTDW------DEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHAD 149
Cdd:PRK11231 82 PQHHLTPEgITVREL---VAygrsPWLSLWgrlsaeDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 150 LLLMDEPTSGLDPLVRSELMDiLLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKIL 209
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMR-LMRELNTQGKTVVTVLH---DLNqasRYCDHLVVLANGHVM 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-209 |
8.88e-13 |
|
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: 66.10 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 15 ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVLDEGYFYDElTL 93
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlRRQIGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 KEmkNII--APSYTDwDEPVF-------QDYIKQFNLNLKQKI----STLSKGMRMKFAVALALSHHADLLLMDEPTSGL 160
Cdd:cd03251 93 AE--NIAygRPGATR-EEVEEaaraanaHEFIMELPEGYDTVIgergVKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 161 DplVRSE--LMDILLNFMKepGKSVFFSTHITSDLDKiADMIILIDDGKIL 209
Cdd:cd03251 170 D--TESErlVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-209 |
9.39e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVL 82
Cdd:PRK10253 8 LRGEQLTLGYGKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDELTLKEM----KNIIAPSYTDW---DEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLM 153
Cdd:PRK10253 88 QNATTPGDITVQELvargRYPHQPLFTRWrkeDEEAVTKAMQATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1261293288 154 DEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-188 |
1.36e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.04 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK--HERkskn 76
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 77 kiGIVldegyFYDE---------------LTLKEMKNI----IApsyTDWDEPV-FQDYIKQFnlnlkqkISTLSKGMRM 136
Cdd:COG4525 79 --GVV-----FQKDallpwlnvldnvafgLRLRGVPKAerraRA---EELLALVgLADFARRR-------IWQLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 137 KFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTH 188
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-219 |
1.39e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDS--GKINFLGNDMDKHERKSKNK 77
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVkALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIVLdegyFYDELTL-KEM---KNI-----IAPS-YTDWDEPVF--QDYIKQFNL--NLKQKISTLSKGMRMKFAVALA 143
Cdd:PRK13549 82 AGIAI----IHQELALvKELsvlENIflgneITPGgIMDYDAMYLraQKLLAQLKLdiNPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 144 LSHHADLLLMDEPTSgldPLVRSE---LMDILLNFmKEPGKSVFFSTHITSDLDKIADMIILIDDGK-ILVNDEKDMLID 219
Cdd:PRK13549 158 LNKQARLLILDEPTA---SLTESEtavLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRhIGTRPAAGMTED 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-222 |
1.89e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.37 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFSLKdVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDmdkHERK--SKNKIGIV 81
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTppSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYDELTLKEmkNI---IAPSY--TDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMD 154
Cdd:PRK10771 77 FQENNLFSHLTVAQ--NIglgLNPGLklNAAQREKLHAIARQMGIEdlLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 155 EPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMLIDSHA 222
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-200 |
1.94e-12 |
|
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: 67.12 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 31 ITGFIGTNGSGKTTTIKailglILkdSGKI--NfLGNdmdkHERK-SKNKI-----GIVLDEgYFYDeLTLKEMKNIIAP 102
Cdd:COG1245 101 VTGILGPNGIGKSTALK-----IL--SGELkpN-LGD----YDEEpSWDEVlkrfrGTELQD-YFKK-LANGEIKVAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 103 SYTDW----------------DEP-VFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDpl 163
Cdd:COG1245 167 QYVDLipkvfkgtvrellekvDERgKLDELAEKLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-- 244
|
170 180 190
....*....|....*....|....*....|....*...
gi 1261293288 164 VRSEL-MDILLNFMKEPGKSVFFSTHITSDLDKIADMI 200
Cdd:COG1245 245 IYQRLnVARLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-208 |
4.41e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKcyENFslKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIV-LD 83
Cdd:PRK15439 269 LTVEDLTG--EGF--RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVyLP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 E-----GYFYDE--------LTLKEMKNIIAPSYtdwDEPVFQDYIKQFNL---NLKQKISTLSKGMRMKFAVALALSHH 147
Cdd:PRK15439 345 EdrqssGLYLDAplawnvcaLTHNRRGFWIKPAR---ENAVLERYRRALNIkfnHAEQAARTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 148 ADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFsthITSDLDKI---ADMIILIDDGKI 208
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLF---ISSDLEEIeqmADRVLVMHQGEI 481
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-209 |
5.65e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.30 E-value: 5.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLI------LKDSGKINFLGNDMDKHER-KSKNKIGIVLDEGYFYDEL 91
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAiKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 92 TLKEmkNIIAP--SYTDWD----EPVFQDYIKQFNL------NLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSG 159
Cdd:PRK14246 106 SIYD--NIAYPlkSHGIKEkreiKKIVEECLRKVGLwkevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261293288 160 LDpLVRSELMDILLNFMKEPGKSVFFStHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK14246 184 ID-IVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVADYVAFLYNGELV 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-209 |
5.91e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.25 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE-RKSKNKIGIV 81
Cdd:PRK09536 3 MIDVSDLSVEFGDTTvLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSaRAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDE---GYFYDELTLKEMKNiiAP------SYTDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:PRK09536 83 PQDtslSFEFDVRQVVEMGR--TPhrsrfdTWTETDRAAVERAMERTGVAqfADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 151 LLMDEPTSGLD--PLVRS-ELMDILLnfmkEPGKSVFFSTHitsDLDKIA---DMIILIDDGKIL 209
Cdd:PRK09536 161 LLLDEPTASLDinHQVRTlELVRRLV----DDGKTAVAAIH---DLDLAArycDELVLLADGRVR 218
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-200 |
1.12e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.54 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 31 ITGFIGTNGSGKTTTIKailglILKDSGKINfLGNDMDKHERKS--KNKIGIVLDEgyFYDELTLKEMKNIIAPSYTDW- 107
Cdd:cd03236 28 VLGLVGPNGIGKSTALK-----ILAGKLKPN-LGKFDDPPDWDEilDEFRGSELQN--YFTKLLEGDVKVIVKPQYVDLi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 108 ---------------DEP-VFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDplVRSEL- 168
Cdd:cd03236 100 pkavkgkvgellkkkDERgKLDELVDQLELRhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--IKQRLn 177
|
170 180 190
....*....|....*....|....*....|..
gi 1261293288 169 MDILLNFMKEPGKSVFFSTHITSDLDKIADMI 200
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-203 |
1.24e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 7 VNNLNKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERksKNKIGIV--L 82
Cdd:PRK15056 9 VNDVTVTWRNghTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ--KNLVAYVpqS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDELTLKEMKNIIAPSYTDW-------DEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLM 153
Cdd:PRK15056 87 EEVDWSFPVLVEDVVMMGRYGHMGWlrrakkrDRQIVTAALARVDMVefRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 154 DEPTSGLDplVRSELMDI-LLNFMKEPGKSVFFSTHITSDLDKIADMIILI 203
Cdd:PRK15056 167 DEPFTGVD--VKTEARIIsLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-231 |
1.33e-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: 63.20 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 12 KCYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIgivldEGYFYDEL 91
Cdd:cd03237 8 KTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADY-----EGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 92 TlkemkNIIAPSYTDwdePVFQ-DYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSEL 168
Cdd:cd03237 83 S-----SITKDFYTH---PYFKtEIAKPLQIEqiLDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 169 MDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIdDGKILVNDEKDmliDSHALIKGSNRFI 231
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVAN---PPQSLRSGMNRFL 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-201 |
1.61e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKInflgndmdkherksknKIGI 80
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI----------------KIGE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYfydeltLKEMKNIIAPSYTDWDEpVF--QDYIK-------------QFNLN---LKQKISTLSKGMRMKFAVAL 142
Cdd:PRK11819 386 TVKLAY------VDQSRDALDPNKTVWEE-ISggLDIIKvgnreipsrayvgRFNFKggdQQKKVGVLSGGERNRLHLAK 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 143 ALSHHADLLLMDEPTSGLDPLVRSELMDILLNFmkePGKSVFfsthITSD---LDKIADMII 201
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PGCAVV----ISHDrwfLDRIATHIL 513
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-208 |
2.00e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.80 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYEN-------FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM--DKHE 71
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 72 RKSKNKIGIVL--------------DEGYFYDELTL--KEMKNIIAPSYTDWDEPVFQDYIKQFnlnlkqkistLSKGMR 135
Cdd:PRK13633 81 WDIRNKAGMVFqnpdnqivativeeDVAFGPENLGIppEEIRERVDESLKKVGMYEYRRHAPHL----------LSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 136 MKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKiADMIILIDDGKI 208
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-208 |
2.17e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLnkCYENFS----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKH-------- 70
Cdd:COG3845 256 VVLEVENL--SVRDDRgvpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLsprerrrl 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 71 -------ERkskNKIGIVLDegyfydeLTLKEmkNIIAPSYtdwDEPVF---------------QDYIKQFNL---NLKQ 125
Cdd:COG3845 334 gvayipeDR---LGRGLVPD-------MSVAE--NLILGRY---RRPPFsrggfldrkairafaEELIEEFDVrtpGPDT 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 126 KISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP----LVRSELMDillnfMKEPGKSVFFsthITSDLD---KIAD 198
Cdd:COG3845 399 PARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaieFIHQRLLE-----LRDAGAAVLL---ISEDLDeilALSD 470
|
250
....*....|
gi 1261293288 199 MIILIDDGKI 208
Cdd:COG3845 471 RIAVMYEGRI 480
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-208 |
2.26e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 31 ITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERK-----SKNKIGIVLDEGYFYDELTLKemKNI---IAP 102
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppEKRRIGYVFQDARLFPHYKVR--GNLrygMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 103 SytdwDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPG 180
Cdd:PRK11144 104 S----MVAQFDKIVALLGIEplLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREIN 179
|
170 180 190
....*....|....*....|....*....|.
gi 1261293288 181 KSVFFSTHitsDLDKI---ADMIILIDDGKI 208
Cdd:PRK11144 180 IPILYVSH---SLDEIlrlADRVVVLEQGKV 207
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-199 |
2.30e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.49 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKA---ILGLI--LKDSGKINFLG---NDMDKHER 72
Cdd:PRK14243 8 ETVLRTENLNVYYGSFlAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIpgFRVEGKVTFHGknlYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 73 KSKNKIGIVLDEGY-----FYDELTLKEMKNiiapSYT-DWDEPVfQDYIKQFNL------NLKQKISTLSKGMRMKFAV 140
Cdd:PRK14243 88 EVRRRIGMVFQKPNpfpksIYDNIAYGARIN----GYKgDMDELV-ERSLRQAALwdevkdKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 141 ALALSHHADLLLMDEPTSGLDPL--VRSELMdillnfMKEPGK--SVFFSTHITSDLDKIADM 199
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPIstLRIEEL------MHELKEqyTIIIVTHNMQQAARVSDM 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
35-188 |
2.94e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 63.53 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 35 IGTNGSGKTTTIKAILGLILKDSGKINFLGNDM-DKHERKSKNKIGIVLDEGYFYDElTLKEMKNIIAPSYTD---WD-- 108
Cdd:TIGR02868 367 LGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSLDQDEVRRRVSVCAQDAHLFDT-TVRENLRLARPDATDeelWAal 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 109 EPV-FQDYIKQFNLNLKQKI----STLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMkePGKSV 183
Cdd:TIGR02868 446 ERVgLADWLRALPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL--SGRTV 523
|
....*
gi 1261293288 184 FFSTH 188
Cdd:TIGR02868 524 VLITH 528
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-209 |
3.19e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.07 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYE-NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINfLGN---DMDKHERKSKNKI- 78
Cdd:PRK11264 3 AIEVKNLVKKFHgQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIR-VGDitiDTARSLSQQKGLIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 ------GIVLDEGYFYDELTLKEmkNIIAPSYTDWDEPVFQDYIKQFNLNLKQKIS--------TLSKGMRMKFAVALAL 144
Cdd:PRK11264 82 qlrqhvGFVFQNFNLFPHRTVLE--NIIEGPVIVKGEPKEEATARARELLAKVGLAgketsyprRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 145 SHHADLLLMDEPTSGLDPlvrsELMDILLNFMK---EPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK11264 160 AMRPEVILFDEPTSALDP----ELVGEVLNTIRqlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-188 |
4.12e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMD--KHERksknkiGI 80
Cdd:PRK11248 1 MLQISHLYADYGGKpALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAER------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VldegyFYDELTL---KEMKNI-----IAPSYTDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:PRK11248 75 V-----FQNEGLLpwrNVQDNVafglqLAGVEKMQRLEIAHQMLKKVGLEgaEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1261293288 151 LLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTH 188
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-209 |
4.41e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.57 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFrisnDCITG----FIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMD-------KHER 72
Cdd:PRK11124 3 IQLNGINCFYgAHQALFDITL----DCPQGetlvLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpsdKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 73 KSKNKIGIVLDEGYFYDELTLkeMKNII-APSYT---DWDEPVFQ-----------DYIKQFNLNLkqkistlSKGMRMK 137
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTV--QQNLIeAPCRVlglSKDQALARaekllerlrlkPYADRFPLHL-------SGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 138 FAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-209 |
6.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.26 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENFS----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-K 75
Cdd:PRK13642 1 MNKILEVENLVFKYEKESdvnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 NKIGIVLDE------GYFYDELTLKEMKNIIAPS---YTDWDEPVFQDYIKQFNlnlKQKISTLSKGMRMKFAVALALSH 146
Cdd:PRK13642 81 RKIGMVFQNpdnqfvGATVEDDVAFGMENQGIPReemIKRVDEALLAVNMLDFK---TREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 147 HADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLDKIA--DMIILIDDGKIL 209
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITH---DLDEAAssDRILVMKAGEII 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-212 |
9.94e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTtikaILGLI-----LKdSGKINFLGNDM-DKHERKS-------------KNkig 79
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIagarkIQ-QGRVEVLGGDMaDARHRRAvcpriaympqglgKN--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 ivldegyFYDELTLKEmkNIiapsytdwdepvfqdyikQFNLNL--------KQKI-----ST------------LSKGM 134
Cdd:NF033858 89 -------LYPTLSVFE--NL------------------DFFGRLfgqdaaerRRRIdellrATglapfadrpagkLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 135 RMKFAVALALSHHADLLLMDEPTSGLDPLVRS---ELMDILLNfmKEPGKSVFFSThitsdldkiADM--------IILI 203
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIRA--ERPGMSVLVAT---------AYMeeaerfdwLVAM 210
|
....*....
gi 1261293288 204 DDGKILVND 212
Cdd:NF033858 211 DAGRVLATG 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-208 |
1.24e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM-------------DKH 70
Cdd:PRK10619 6 LNVIDLHKRYgEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 71 E-RKSKNKIGIVLDEGYFYDELTLKEmkNII-AP------SYTDWDEPVFQdYIKQFNLNLKQKI---STLSKGMRMKFA 139
Cdd:PRK10619 86 QlRLLRTRLTMVFQHFNLWSHMTVLE--NVMeAPiqvlglSKQEARERAVK-YLAKVGIDERAQGkypVHLSGGQQQRVS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 140 VALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-188 |
1.45e-10 |
|
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: 61.95 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFSLKDVTfRI-----SNDCItGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKI 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVD-RLcvgvrPGECF-GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 GIVLDEGYFYDELTLKEMKNIIA-----PSytDWDEPVFQDYIKQFNLNL--KQKISTLSKGMRMKFAVALALSHHADLL 151
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYArlrgvPA--EEIEKVANWSIQSLGLSLyaDRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190
....*....|....*....|....*....|....*..
gi 1261293288 152 LMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTH 188
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSH 2128
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-208 |
1.49e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 30 CItgfIGTNGSGKTTTIKAILGLILKDSGKINF--------LGNDMDKHERksknkiGIVLD---EG----------YF- 87
Cdd:PRK11147 33 CL---VGRNGAGKSTLMKILNGEVLLDDGRIIYeqdlivarLQQDPPRNVE------GTVYDfvaEGieeqaeylkrYHd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 88 --------YDELTLKEMKNI--IAPSYTDWD-EPVFQDYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEP 156
Cdd:PRK11147 104 ishlvetdPSEKNLNELAKLqeQLDHHNLWQlENRINEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 157 TSGLDplvrSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK11147 184 TNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-208 |
1.58e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.86 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM---DKHE-RKS 74
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERElRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 75 KNKIGivldegyfydeltlkeMkniiapsytdwdepVFQdyikQFNL--------NL----------KQKI--------- 127
Cdd:COG1135 81 RRKIG----------------M--------------IFQ----HFNLlssrtvaeNValpleiagvpKAEIrkrvaelle 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 128 ------------STLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD- 194
Cdd:COG1135 127 lvglsdkadaypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH---EMDv 203
|
250
....*....|....*.
gi 1261293288 195 --KIADMIILIDDGKI 208
Cdd:COG1135 204 vrRICDRVAVLENGRI 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-195 |
2.04e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYEN-FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVL 82
Cdd:PRK13540 1 MLDVIELDFDYHDqPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDELTLKEmkNIIAPSYTDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGL 160
Cdd:PRK13540 81 HRSGINPYLTLRE--NCLYDIHFSPGAVGITELCRLFSLEhlIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1261293288 161 DPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDK 195
Cdd:PRK13540 159 DELSLLTIITKIQEHRAK-GGAVLLTSHQDLPLNK 192
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-198 |
2.05e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.67 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAI-----LGLILKDSGKINFLGNDMdkHERKS---- 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKiLEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNI--YERRVnlnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 75 -KNKIGIVLDEGYF-----YDELTLK----------EMKNIIAPSYTD---WDEpvfqdyIKQfnlNLKQKISTLSKGMR 135
Cdd:PRK14258 86 lRRQVSMVHPKPNLfpmsvYDNVAYGvkivgwrpklEIDDIVESALKDadlWDE------IKH---KIHKSALDLSGGQQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 136 MKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIAD 198
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-201 |
2.15e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.49 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLnKCYenFSLKD-----------------VTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLG 64
Cdd:PRK15079 6 KVLLEVADL-KVH--FDIKDgkqwfwqppktlkavdgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 65 NDM----DKHERKSKNKIGIVldegyFYDEL-------TLKEmknIIApsytdwdEPVFQDYIKQFNLNLKQKISTL--- 130
Cdd:PRK15079 83 KDLlgmkDDEWRAVRSDIQMI-----FQDPLaslnprmTIGE---IIA-------EPLRTYHPKLSRQEVKDRVKAMmlk 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 131 ---------------SKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDK 195
Cdd:PRK15079 148 vgllpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKH 227
|
....*.
gi 1261293288 196 IADMII 201
Cdd:PRK15079 228 ISDRVL 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-188 |
2.57e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.06 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSK--- 75
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 76 --NKIGIVLDEGYFYDELTLKE---MKNIIAPSYTDWDEPVFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHA 148
Cdd:PRK11629 85 rnQKLGFIYQFHHLLPDFTALEnvaMPLLIGKKKPAEINSRALEMLAAVGLEhrANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1261293288 149 DLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTH 188
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-208 |
2.70e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLNkcyeNFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIV- 81
Cdd:PRK10762 256 VRLKVDNLS----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVy 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYDELTL----KEMKNIIAPSY----------TDWDEPVfQDYIKQFNL---NLKQKISTLSKGMRMKFAVALAL 144
Cdd:PRK10762 332 ISEDRKRDGLVLgmsvKENMSLTALRYfsraggslkhADEQQAV-SDFIRLFNIktpSMEQAIGLLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 145 SHHADLLLMDEPTSGLDPLVRSELMDiLLNFMKEPGKSVFFsthITSDLDKI---ADMIILIDDGKI 208
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIIL---VSSEMPEVlgmSDRILVMHEGRI 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-208 |
2.79e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIG 79
Cdd:PRK15439 8 APPLLCARSISKQYSGVEvLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IVL--DEGYFYDELTLKEmkNII--APSYTDwDEPVFQDYIKQFN--LNLKQKISTLSKGMRMKFAVALALSHHADLLLM 153
Cdd:PRK15439 88 IYLvpQEPLLFPNLSVKE--NILfgLPKRQA-SMQKMKQLLAALGcqLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 154 DEPTSGLDPlVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK15439 165 DEPTASLTP-AETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-200 |
2.91e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 31 ITGFIGTNGSGKTTTIKailglILkdSGKI--NfLGNDMDKHERKSknkigiVLDE-------GYFYDeLTLKEMKNIIA 101
Cdd:PRK13409 101 VTGILGPNGIGKTTAVK-----IL--SGELipN-LGDYEEEPSWDE------VLKRfrgtelqNYFKK-LYNGEIKVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 102 PSYTDW----------------DEP-VFQDYIKQFNLN--LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:PRK13409 166 PQYVDLipkvfkgkvrellkkvDERgKLDEVVERLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190
....*....|....*....|....*....|....*...
gi 1261293288 163 LVRSELMDILLNFMKepGKSVFFSTHITSDLDKIADMI 200
Cdd:PRK13409 246 RQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNV 281
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-209 |
3.20e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.16 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLI-----LKDSGKINFLGND---MDKHERKSKNK----IGIVLDEGY 86
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDifkMDVIELRRRVQmvfqIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 87 FYDELTLKEMKNIIAPSYTDWDEPVFQDYIK-QFNLNLKQKI----STLSKGMRMKFAVALALSHHADLLLMDEPTSGLD 161
Cdd:PRK14247 99 IFENVALGLKLNRLVKSKKELQERVRWALEKaQLWDEVKDRLdapaGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1261293288 162 PLVRSELMDILLNFMKEpgKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK14247 179 PENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-208 |
3.47e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 60.51 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVLDEGYFYDE------- 90
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlHRQVALVGQEPVLFSGsvrenia 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 91 --LTLKEMKNIIAPSYTDWDEPVFQDYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDplVRSEl 168
Cdd:TIGR00958 577 ygLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD--AECE- 653
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1261293288 169 mDILLNFMKEPGKSVFFSTHITSDLDKiADMIILIDDGKI 208
Cdd:TIGR00958 654 -QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-188 |
4.33e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGND--------MDKHE 71
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRkGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyaLSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 72 RK--SKNKIGIVldEGYFYDELtlkEMK-----NI--------------IAPSYTDWDEPVFQDYIKqfnlnLKQKISTL 130
Cdd:PRK11701 83 RRrlLRTEWGFV--HQHPRDGL---RMQvsaggNIgerlmavgarhygdIRATAGDWLERVEIDAAR-----IDDLPTTF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 131 SKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTH 188
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-208 |
4.52e-10 |
|
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: 59.82 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGL--ILKDSGKI----------------NFLG- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKeVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 65 -----------------NDMDKHERKSKNKIGIVLDEGY-FYDELT-----LKEMKNIIAPSYTDWDEPVfqDYIKQfnL 121
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLSDKLRRRIRKRIAIMLQRTFaLYGDDTvldnvLEALEEIGYEGKEAVGRAV--DLIEM--V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 122 NLKQKIS----TLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIA 197
Cdd:TIGR03269 157 QLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|.
gi 1261293288 198 DMIILIDDGKI 208
Cdd:TIGR03269 237 DKAIWLENGEI 247
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-209 |
5.32e-10 |
|
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: 58.32 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM-DKHERKSKNKIGIVLDEGYFYDeLTLKEmk 97
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIGLVSQEPVLFD-GTIAE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 98 NIiapSYTDWDEPVFQ-----------DYI----KQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:cd03249 96 NI---RYGKPDATDEEveeaakkanihDFImslpDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261293288 163 LVRSELMDILLNFMKepGKSVFFSTHITSDLDKiADMIILIDDGKIL 209
Cdd:cd03249 173 ESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-208 |
6.17e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.47 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 22 VTFRISNDCITGFIGTNGSGKTTTIKAILG-LILKDSGKINflG---NDMD-KHERKsknKIGIV-----LDEGyfydel 91
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPYQGSLKIN--GielRELDpESWRK---HLSWVgqnpqLPHG------ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 92 TLKEmkNII--APSYTD--WDEPVFQDYIKQFNLNLKQKIST--------LSKGMRMKFAVALALSHHADLLLMDEPTSG 159
Cdd:PRK11174 438 TLRD--NVLlgNPDASDeqLQQALENAWVSEFLPLLPQGLDTpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 160 LDplVRSE--LMDILLNFMKepGKSVFFSTHITSDLDKIaDMIILIDDGKI 208
Cdd:PRK11174 516 LD--AHSEqlVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-208 |
6.19e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 59.65 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY---ENFSLKDVTFRISNDCITGFIGTNGSGKTTtikaILGLILK----DSGKINFLGNDMDKHERKS-KN 76
Cdd:PRK11176 342 IEFRNVTFTYpgkEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRDYTLASlRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 77 KIGIVLDEGYFYDEltlkEMKNIIAPSYTDW------DEPVFQDYIKQFNLNLKQKIST--------LSKGMRMKFAVAL 142
Cdd:PRK11176 418 QVALVSQNVHLFND----TIANNIAYARTEQysreqiEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 143 ALSHHADLLLMDEPTSGLDplVRSEL-----MDILlnfmkEPGKSVFFSTHITSDLDKiADMIILIDDGKI 208
Cdd:PRK11176 494 ALLRDSPILILDEATSALD--TESERaiqaaLDEL-----QKNRTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-209 |
6.44e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 21 DVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHER----KSKNKIGIVLDEGYFYDELTLKEm 96
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrlyTVRKRMSMLFQSGALFTDMNVFD- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 97 kNIIAP--SYTDWDEPVFQDYI--KQFNLNL----KQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSEL 168
Cdd:PRK11831 104 -NVAYPlrEHTQLPAPLLHSTVmmKLEAVGLrgaaKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1261293288 169 MDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-202 |
7.10e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 31 ITGFIGTNGSGKTTTIKAILGLILKDSGKINFLgnDMDKHERksknkigivldegyfydeltlkemkniiapsytdwdep 110
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPGGGVIYI--DGEDILE-------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 111 vfQDYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDI-----LLNFMKEPGKSVFF 185
Cdd:smart00382 44 --EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLTVIL 121
|
170
....*....|....*..
gi 1261293288 186 STHITSDLDKIADMIIL 202
Cdd:smart00382 122 TTNDEKDLGPALLRRRF 138
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-162 |
1.38e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.35 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAI---LGLI--LKDSGKINFLGND-----MDK 69
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIpgARVEGEILLDGEDiydpdVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 70 HE-RKsknKIGIVldegyF----------YDeltlkemkNIIAP-------SYTDWDEPVfQDYIKQFNL------NLKQ 125
Cdd:COG1117 88 VElRR---RVGMV-----FqkpnpfpksiYD--------NVAYGlrlhgikSKSELDEIV-EESLRKAALwdevkdRLKK 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1261293288 126 KISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDP 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-239 |
1.60e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.92 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYE-NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMdKHERKSKNKIGIVL 82
Cdd:PRK11607 19 LLEIRNLTKSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDELT--------LKEMKNIIAPSYTDWDEPVFQDYIKQFnlnLKQKISTLSKGMRMKFAVALALSHHADLLLMD 154
Cdd:PRK11607 98 QSYALFPHMTveqniafgLKQDKLPKAEIASRVNEMLGLVHMQEF---AKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 155 EPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDMlIDSHALIKGSNRFINeq 234
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE-IYEHPTTRYSAEFIG-- 251
|
....*
gi 1261293288 235 TKNLF 239
Cdd:PRK11607 252 SVNVF 256
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
130-250 |
2.06e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.63 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 130 LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1261293288 210 VNDekdmliDSHALIKGSNRfinEQTKNLfLNLHQTHYGFE 250
Cdd:PRK10418 221 EQG------DVETLFNAPKH---AVTRSL-VSAHLALYGME 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-219 |
2.20e-09 |
|
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: 57.91 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDS--GKINFLGNDMDKHERKSKNKIGI 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVkALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLdegyFYDELTL-KEM---KNI-------IAPSYTDWDEPVF--QDYIKQFNL---NLKQKISTLSKGMRMKFAVALAL 144
Cdd:TIGR02633 81 VI----IHQELTLvPELsvaENIflgneitLPGGRMAYNAMYLraKNLLRELQLdadNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1261293288 145 SHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGK-ILVNDEKDMLID 219
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQhVATKDMSTMSED 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-208 |
3.20e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLNKcYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMdkhERKS-----KNK 77
Cdd:PRK09700 264 TVFEVRNVTS-RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSpldavKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 78 IGIVLD---EGYFYDELTLKEmkNI-IAPSYTD---------WDEPVFQDYIKQFN--LNLK-----QKISTLSKGMRMK 137
Cdd:PRK09700 340 MAYITEsrrDNGFFPNFSIAQ--NMaISRSLKDggykgamglFHEVDEQRTAENQRelLALKchsvnQNITELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 138 FAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-215 |
4.38e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 31 ITGFIGTNGSGKTTTIKAILGLiLKDSGKINFLGNDMDKHerkSKNKIGIVldEGYF------------YDELTLkemkN 98
Cdd:PRK03695 24 ILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAW---SAAELARH--RAYLsqqqtppfampvFQYLTL----H 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 99 IIAPSYTDWDEPVFQDYIKQFNLN--LKQKISTLSKG--MRMKFAVAL-----ALSHHADLLLMDEPTSGLDpLVRSELM 169
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDdkLGRSVNQLSGGewQRVRLAAVVlqvwpDINPAGQLLLLDEPMNSLD-VAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1261293288 170 DILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKILVNDEKD 215
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSH---DLNhtlRHADRVWLLKQGKLLASGRRD 218
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
15-216 |
4.74e-09 |
|
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: 56.55 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 15 ENF-SLKDVTFRISNDcITGFIGTNGSGKTTTIKAIlGLILKDSGKINFLGNDMDKHERKSKNKIGIVLDEGYFYDELT- 92
Cdd:COG3593 9 KNFrSIKDLSIELSDD-LTVLVGENNSGKSSILEAL-RLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSLLSRLLr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 93 -------------------------LKEMKNIIAPSYTDWDEPV----------FQDYIKQFNLNLKQK----ISTLSKG 133
Cdd:COG3593 87 lllkeedkeeleealeelneelkeaLKALNELLSEYLKELLDGLdlelelsldeLEDLLKSLSLRIEDGkelpLDRLGSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 134 MR--MKFAVALALSHHAD-----LLLMDEPTSGLDPLVRSELMDILLNFMKEPGKsVFFSTH--ITSDLDKIADMIILID 204
Cdd:COG3593 167 FQrlILLALLSALAELKRapanpILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQ-VIITTHspHLLSEVPLENIRRLRR 245
|
250
....*....|....*...
gi 1261293288 205 DG------KILVNDEKDM 216
Cdd:COG3593 246 DSggttstKLIDLDDEDL 263
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
33-208 |
4.83e-09 |
|
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: 56.62 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 33 GFIGTNGSGKTTTIKAILGLIlKDSGKINFLGNDMDKHERKS----KNKIGIV-----------------LDEGY--FYD 89
Cdd:COG4172 316 GLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrplRRRMQVVfqdpfgslsprmtvgqiIAEGLrvHGP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 90 ELTLKEMKNIIAPSYTD--WDEPVFQDYIKQFnlnlkqkistlSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSE 167
Cdd:COG4172 395 GLSAAERRARVAEALEEvgLDPAARHRYPHEF-----------SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQ 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1261293288 168 LMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKI 208
Cdd:COG4172 464 ILDLLRDLQREHGLAYLFISH---DLAvvrALAHRVMVMKDGKV 504
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-211 |
5.51e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.66 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKaILGLILK-DSGKINFLGNDM-----DK 69
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEeqvevLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKpTSGTYRVAGQDVatldaDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 70 HERKSKNKIGIVLDEGYFYDELTLK---EMKNIIAPSYTDWDEPVFQDYIKQfnLNLKQKI----STLSKGMRMKFAVAL 142
Cdd:PRK10535 80 LAQLRREHFGFIFQRYHLLSHLTAAqnvEVPAVYAGLERKQRLLRAQELLQR--LGLEDRVeyqpSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 143 ALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSVFFSTHiTSDLDKIADMIILIDDGKILVN 211
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRN 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-223 |
5.81e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.76 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS--LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM-DKHERKSKNKI-G 79
Cdd:PRK13644 1 MIRLENVSYSYPDGTpaLENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IVLD--EGYFYDELTLKEM----KNIIAPSY---TDWDEPVFQDYIKQFNlnlKQKISTLSKGMRMKFAVALALSHHADL 150
Cdd:PRK13644 81 IVFQnpETQFVGRTVEEDLafgpENLCLPPIeirKRVDRALAEIGLEKYR---HRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293288 151 LLMDEPTSGLDPlvrSELMDILLNFMK--EPGKSVFFSTHITSDLdKIADMIILIDDGKILVNDEKDMLIDSHAL 223
Cdd:PRK13644 158 LIFDEVTSMLDP---DSGIAVLERIKKlhEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-209 |
5.93e-09 |
|
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: 55.19 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY---ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDK-HERKSKNKIGI 80
Cdd:cd03244 3 IEFKNVSLRYrpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 V--------------LD-EGYFYDE---LTLKEMKNIiapsytdwdepvfqDYIKQFNLNLKQKIST----LSKGMRMKF 138
Cdd:cd03244 83 IpqdpvlfsgtirsnLDpFGEYSDEelwQALERVGLK--------------EFVESLPGGLDTVVEEggenLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 139 AVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKepGKSVFFSTH-ITSDLDkiADMIILIDDGKIL 209
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHrLDTIID--SDRILVLDKGRVV 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-208 |
9.08e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 9.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLnkCYE---NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLG---NDMDKHERKS-- 74
Cdd:PRK13548 1 AMLEARNL--SVRlggRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrplADWSPAELARrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 75 -----KNKIG-------IVldegyfydeltlkEMKNIIAPSYTDWDEPVFQDYIKQFNL-NLKQK-ISTLSKG--MRMKF 138
Cdd:PRK13548 79 avlpqHSSLSfpftveeVV-------------AMGRAPHGLSRAEDDALVAAALAQVDLaHLAGRdYPQLSGGeqQRVQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 139 AVALALSHHAD----LLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDGKI 208
Cdd:PRK13548 146 ARVLAQLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLH---DLNlaaRYADRIVLLHQGRL 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-188 |
1.16e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKInflgndmdkhERKSKNKIGIVLDEGYFYDELTLKEMKN 98
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLRIGYVPQKLYLDTTLPLTVNRF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 99 I-IAPSYTDWDEPVFQDYIKQFNLnLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMK 177
Cdd:PRK09544 90 LrLRPGTKKEDILPALKRVQAGHL-IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
170
....*....|.
gi 1261293288 178 EPGKSVFFSTH 188
Cdd:PRK09544 169 ELDCAVLMVSH 179
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-207 |
1.41e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 35 IGTNGSGKTTTIKAILGLILKDSGKINFLGNDMD-KHERKSKNK-IGIVLDEGYFYDELTLKEmkNI-IAPSYT------ 105
Cdd:PRK10762 36 VGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAgIGIIHQELNLIPQLTIAE--NIfLGREFVnrfgri 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 106 DWDEpVFQDYIKQF-NLNLK----QKISTLSKGMRMKFAVALALSHHADLLLMDEPTsglDPLVRSELMDI--LLNFMKE 178
Cdd:PRK10762 114 DWKK-MYAEADKLLaRLNLRfssdKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT---DALTDTETESLfrVIRELKS 189
|
170 180
....*....|....*....|....*....
gi 1261293288 179 PGKSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:PRK10762 190 QGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
131-217 |
1.45e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 131 SKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDDGKILV 210
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
....*..
gi 1261293288 211 NDEKDML 217
Cdd:NF000106 225 DGKVDEL 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-201 |
2.70e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 16 NFSLKDVTFRIsndcITGfigTNGSGKTTTIKAILGLILKDSGKINFLGNDMD--KHERKSKNKIGIVLDEGYF----YD 89
Cdd:PRK10247 27 SFSLRAGEFKL----ITG---PSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVSYCAQTPTLFgdtvYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 90 ELTLKEMKNIIAPsytdwDEPVFQDYIKQFNLN---LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRS 166
Cdd:PRK10247 100 NLIFPWQIRNQQP-----DPAIFLDDLERFALPdtiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1261293288 167 ELMDILLNFMKEPGKSVFFSTHitsDLDKI--ADMII 201
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTH---DKDEInhADKVI 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-219 |
2.76e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAI-----LGLILKDSGKINFLGNDM-----DKHE- 71
Cdd:PRK14239 5 ILQVSDLSVYYnKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIysprtDTVDl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 72 RKsknKIGIVLD----------EGYFY--------DELTLKEM--KNIIAPSYtdWDEpvfqdyIKQfnlNLKQKISTLS 131
Cdd:PRK14239 85 RK---EIGMVFQqpnpfpmsiyENVVYglrlkgikDKQVLDEAveKSLKGASI--WDE------VKD---RLHDSALGLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 132 KGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpgKSVFFSTHITSDLDKIADMIILIDDGKIL-V 210
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIeY 228
|
....*....
gi 1261293288 211 NDEKDMLID 219
Cdd:PRK14239 229 NDTKQMFMN 237
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
34-208 |
3.08e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.42 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 34 FI-GTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVLDEGYFYDELtlkemkniiapsYTDWDEPV 111
Cdd:COG4615 362 FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQLFSAVFSDFHLFDRL------------LGLDGEAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 112 ---FQDYIKQFNLNLK-----QKIST--LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRselmDI----LLNFMK 177
Cdd:COG4615 430 parARELLERLELDHKvsvedGRFSTtdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFR----RVfyteLLPELK 505
|
170 180 190
....*....|....*....|....*....|....
gi 1261293288 178 EPGKSVFFSTHitsDlDK---IADMIILIDDGKI 208
Cdd:COG4615 506 ARGKTVIAISH---D-DRyfdLADRVLKMDYGKL 535
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-238 |
3.65e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 16 NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNdmdkherKSKNKIGIVLDEGYFYDE----- 90
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-------AALIAISSGLNGQLTGIEnielk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 91 -----LTLKEMKNIIaPSYTDWDEpvfqdyIKQFnlnLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVR 165
Cdd:PRK13545 110 glmmgLTKEKIKEII-PEIIEFAD------IGKF---IYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1261293288 166 SELMDiLLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL-VNDEKDMLIDSHALIKGSNRFINEQTKNL 238
Cdd:PRK13545 180 KKCLD-KMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKeYGDIKEVVDHYDEFLKKYNQMSVEERKDF 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
130-207 |
6.08e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 6.08e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 130 LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
35-188 |
6.97e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 35 IGTNGSGKTTTIKAILGLILKDSGKINFLGND---MDKHER---KSKNkIGIVLDEgyFYDELTLKEMKNIIAPSY---- 104
Cdd:PRK10584 42 IGESGSGKSTLLAILAGLDDGSSGEVSLVGQPlhqMDEEARaklRAKH-VGFVFQS--FMLIPTLNALENVELPALlrge 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 105 TDWDEPV-FQDYIKQFNL--NLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGK 181
Cdd:PRK10584 119 SSRQSRNgAKALLEQLGLgkRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGT 198
|
....*..
gi 1261293288 182 SVFFSTH 188
Cdd:PRK10584 199 TLILVTH 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-208 |
7.17e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 52.09 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS-KNKIGIVLDEGYFYDE------- 90
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSKVSLVGQEPVLFARslqdnia 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 91 --LTLKEMKNIIAPSYTDWDEPVFQDYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDplVRSEL 168
Cdd:cd03248 110 ygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD--AESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1261293288 169 MDILLNFMKEPGKSVFFSTHITSDLDKiADMIILIDDGKI 208
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-208 |
7.73e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.49 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLI---LKDSGKINFLGNDMDKHERKSKNKIGIVLDEGYFYDELTLKE 95
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 96 -MKniiapsytdwdepvfqdyikqFNLNLK--QKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDIL 172
Cdd:cd03233 103 tLD---------------------FALRCKgnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCI 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1261293288 173 LNFMKEPGKSVFFSTHITSD-LDKIADMIILIDDGKI 208
Cdd:cd03233 162 RTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQ 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
107-208 |
7.90e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 107 WDEPVFQDYIKQFNL---NLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKEPGKSV 183
Cdd:PRK11288 371 WEAENADRFIRSLNIktpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYE-LAAQGVAV 449
|
90 100
....*....|....*....|....*...
gi 1261293288 184 FFsthITSDLDK---IADMIILIDDGKI 208
Cdd:PRK11288 450 LF---VSSDLPEvlgVADRIVVMREGRI 474
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-208 |
8.42e-08 |
|
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: 51.64 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS---LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHE-RKSKNKIGI 80
Cdd:cd03369 7 IEVENLSVRYAPDLppvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 81 VLDEGYFYDeltlKEMKNIIAPSYTDWDEPVFQdyikqfNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGL 160
Cdd:cd03369 87 IPQDPTLFS----GTIRSNLDPFDEYSDEEIYG------ALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1261293288 161 DPLVRSELMDILLNFMKepGKSVFFSTHitsDLDKIADM--IILIDDGKI 208
Cdd:cd03369 157 DYATDALIQKTIREEFT--NSTILTIAH---RLRTIIDYdkILVMDAGEV 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-206 |
9.57e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 14 YENFS------LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNdMDKHERKSKNKIGIVLDE--- 84
Cdd:TIGR01271 431 FSNFSlyvtpvLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPQTSWIMPGTIKDNiif 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 85 GYFYDELtlkEMKNIIAPSYTDWDEPVFQDyikQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLV 164
Cdd:TIGR01271 510 GLSYDEY---RYTSVIKACQLEEDIALFPE---KDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1261293288 165 RSELMD-ILLNFMKEPGKSVffsthITSDLD--KIADMIILIDDG 206
Cdd:TIGR01271 584 EKEIFEsCLCKLMSNKTRIL-----VTSKLEhlKKADKILLLHEG 623
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-208 |
1.01e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.86 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 33 GFIGTNGSGKTTTIKAILGLILKDSGKINFlgndmdkherkSKnkiGIVLdeGYFY---------DELTLKEMKNIiAPS 103
Cdd:PRK10636 342 GLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AK---GIKL--GYFAqhqleflraDESPLQHLARL-APQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 104 YTdwdEPVFQDYIKQFNLN---LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFmkePG 180
Cdd:PRK10636 405 EL---EQKLRDYLGGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EG 478
|
170 180
....*....|....*....|....*...
gi 1261293288 181 KSVFFStHITSDLDKIADMIILIDDGKI 208
Cdd:PRK10636 479 ALVVVS-HDRHLLRSTTDDLYLVHDGKV 505
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
15-213 |
1.27e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 51.51 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 15 ENF-SLKDVTFRISNdcITGFIGTNGSGKTTTIKAILGL------------------------ILKDSGK-----INFLG 64
Cdd:COG4938 7 KNFgPFKEAELELKP--LTLLIGPNGSGKSTLIQALLLLlqsnfiylpaersgparlypslvrELSDLGSrgeytADFLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 65 N--DMDKHERKSKNKIgivldegyfydELTLKEMKNIIAPSYT-DWDEPVFQDYIKQFNLNLKQKISTLSKGMRMKFAVA 141
Cdd:COG4938 85 EleNLEILDDKSKELL-----------EQVEEWLEKIFPGKVEvDASSDLVRLVFRPSGNGKRIPLSNVGSGVSELLPIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 142 LALSHHA---DLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHitSD--LDKIAdmiILIDDGKILVNDE 213
Cdd:COG4938 154 LALLSAAkpgSLLIIEEPEAHLHPKAQSALAELLAELANS-GVQVIIETH--SDyiLNGLR---NLIKEGKLLDPDD 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-209 |
1.61e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDmDKHERKSKNKIGIVLDEGYFYDELTLKEMKN 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 99 IIA----PSYTDWDEP--VFQDYIKQFNLNLKQK-------ISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVR 165
Cdd:PLN03211 163 FCSllrlPKSLTKQEKilVAESVISELGLTKCENtiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1261293288 166 SELMDILLNfMKEPGKSVFFSTH-ITSDLDKIADMIILIDDGKIL 209
Cdd:PLN03211 243 YRLVLTLGS-LAQKGKTIVTSMHqPSSRVYQMFDSVLVLSEGRCL 286
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-209 |
1.97e-07 |
|
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: 50.22 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGL--ILKDSGKINFLGND---MDKHERkSKNKI 78
Cdd:cd03217 1 LEIKDLHVSVGGKEiLKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDitdLPPEER-ARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 GIVLDEGYFYDELTLKemkniiapsytdwdepvfqDYIKQFNLNLkqkistlSKGMRMKFAVALALSHHADLLLMDEPTS 158
Cdd:cd03217 80 FLAFQYPPEIPGVKNA-------------------DFLRYVNEGF-------SGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1261293288 159 GLDpLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKI-ADMIILIDDGKIL 209
Cdd:cd03217 134 GLD-IDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIV 184
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-204 |
1.97e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.67 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 21 DVTFriSNDCITGFIGTNGSGKTTTIKAIlGLILkdsgkinflGNDMDKHERKSKNKIGIvldegyfydeltlkemkNII 100
Cdd:cd03227 15 DVTF--GEGSLTIITGPNGSGKSTILDAI-GLAL---------GGAQSATRRRSGVKAGC-----------------IVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 101 APSYTdwdepvfqdyikqFNLNLKQkistLSKGMRMKFAVALALSHHA----DLLLMDEPTSGLDPLVRSELMDILLNFM 176
Cdd:cd03227 66 AVSAE-------------LIFTRLQ----LSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHL 128
|
170 180 190
....*....|....*....|....*....|.
gi 1261293288 177 KEpGKSVFFSTH---ITSDLDKIADMIILID 204
Cdd:cd03227 129 VK-GAQVIVITHlpeLAELADKLIHIKKVIT 158
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-207 |
2.65e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-----LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINflgndMDKHERKSKNKI 78
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-----CDKMLLRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 GIVLDEgyfydeLTLKEMKN--------IIAPSYTDWDePVF------------------------------QDYIKQFN 120
Cdd:PRK10261 87 VIELSE------QSAAQMRHvrgadmamIFQEPMTSLN-PVFtvgeqiaesirlhqgasreeamveakrmldQVRIPEAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 121 LNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMI 200
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
|
....*..
gi 1261293288 201 ILIDDGK 207
Cdd:PRK10261 240 LVMYQGE 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-197 |
2.92e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.88 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYEN-----FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKD---SGKINFLGNDMDKHER 72
Cdd:PRK09473 9 ADALLDVKDLRVTFSTpdgdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 73 KSKNKIGIVLDEGYFYDELTL------------------KEMKNIIApsytdWDEPV-FQDYIKQFNLNLKQKI--STLS 131
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSlnpymrvgeqlmevlmlhKGMSKAEA-----FEESVrMLDAVKMPEARKRMKMypHEFS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 132 KGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDiLLNFMKEPgksvfFSTH---ITSDLDKIA 197
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT-LLNELKRE-----FNTAiimITHDLGVVA 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-208 |
3.66e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.87 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 18 SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKS----KNKIGIVLDEGYFYDELTL 93
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 KE---MKNIIAPSYTD---------WDEPVFQDYIKQFNLNlkqkistLSKGMRMKFAVALALSHHADLLLMDEPTSGLD 161
Cdd:PRK10908 97 YDnvaIPLIIAGASGDdirrrvsaaLDKVGLLDKAKNFPIQ-------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261293288 162 PLVRSELMDILLNFMKePGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK10908 170 DALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-172 |
3.85e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.86 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCY------------ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLIlKDSGKINFLGNDMDKHE 71
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 72 RKS----KNKIGIV-----------------LDEGYFYDELTL----KEMKNIIAPSYTDWDEPVFQDYIKQFnlnlkqk 126
Cdd:PRK15134 354 RRQllpvRHRIQVVfqdpnsslnprlnvlqiIEEGLRVHQPTLsaaqREQQVIAVMEEVGLDPETRHRYPAEF------- 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1261293288 127 istlSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDIL 172
Cdd:PRK15134 427 ----SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALL 468
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-209 |
5.70e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.13 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 22 VTFRISNDCITGFIGTNGSGKTTTIKAILGLIlkD------SGKINFLGNDMDKHERKSKNKIGIVLDEGYFYDELTlke 95
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI--DypgrvmAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMT--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 96 mknIIAPSYTdwdepV-FQ---------------------DYIKQFNL-----NLKQKISTLSKGMRMKFAVALALSHHA 148
Cdd:PRK11022 101 ---SLNPCYT-----VgFQimeaikvhqggnkktrrqraiDLLNQVGIpdpasRLDVYPHQLSGGMSQRVMIAMAIACRP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 149 DLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK11022 173 KLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-208 |
7.23e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 36 GTNGSGKTTTIKAILGLILKD---SGKINFLGNDMDKheRKSKNKIGIVLDEGYFYDELTLKEMKNIIA----PSYTDWD 108
Cdd:TIGR00955 58 GSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA--KEMRAISAYVQQDDLFIPTLTVREHLMFQAhlrmPRRVTKK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 109 EPV--FQDYIKQFNLNLKQK--------ISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNfMKE 178
Cdd:TIGR00955 136 EKRerVDEVLQALGLRKCANtrigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQ 214
|
170 180 190
....*....|....*....|....*....|.
gi 1261293288 179 PGKSVFFSTH-ITSDLDKIADMIILIDDGKI 208
Cdd:TIGR00955 215 KGKTIICTIHqPSSELFELFDKIILMAEGRV 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
130-208 |
7.41e-07 |
|
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: 50.07 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 130 LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHitsDLD---KIADMIILIDDG 206
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH---DLGvvrRFADRVAVMRQG 233
|
..
gi 1261293288 207 KI 208
Cdd:COG4172 234 EI 235
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
38-194 |
7.43e-07 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 49.70 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 38 NGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLDEGYFYDELTLKEMKNIIAPSYTDWDEPVFqdYIK 117
Cdd:pfam13304 147 IISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGL--ILL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 118 QFNLNLKQKISTLSKGMRMKFAVALALS---HHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKsVFFSTHITSDLD 194
Cdd:pfam13304 225 ENGGGGELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQ-LILTTHSPLLLD 303
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-208 |
1.23e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 49.26 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 9 NLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKInFLGNDMDKHERKSKNKIGIVLDEGYF 87
Cdd:PRK11000 8 NVTKAYGDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAERGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 88 YDELTLKE-----MKnIIAPSYTDWDEPVFQ-DYIKQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLD 161
Cdd:PRK11000 87 YPHLSVAEnmsfgLK-LAGAKKEEINQRVNQvAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1261293288 162 PLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKI 208
Cdd:PRK11000 166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-206 |
1.48e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.70 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNdMDKHERKSKNKIGIVLDE---GYFYDELtlkE 95
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSWIMPGTIKENiifGVSYDEY---R 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 96 MKNIIAPSYTDWDEPVFQDyikQFNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMD-ILLN 174
Cdd:cd03291 129 YKSVVKACQLEEDITKFPE---KDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEsCVCK 205
|
170 180 190
....*....|....*....|....*....|....
gi 1261293288 175 FMKEPGKSVffsthITSDLD--KIADMIILIDDG 206
Cdd:cd03291 206 LMANKTRIL-----VTSKMEhlKKADKILILHEG 234
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
8-215 |
2.05e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.89 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 8 NNLNKCYenFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKInflgndmDKHERKSKNKIGIVLD---- 83
Cdd:PRK13546 31 KHKNKTF--FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------DRNGEVSVIAISAGLSgqlt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 --EGYFYDELTL----KEMKNIIaPSYTDWDEpvFQDYIKQfnlnlkqKISTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:PRK13546 102 giENIEFKMLCMgfkrKEIKAMT-PKIIEFSE--LGEFIYQ-------PVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 158 SGLDPLVRSELMDILLNFmKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKD 215
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELD 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-209 |
2.57e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 47.86 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 1 MNVMLEVNNLNKCYEN----F------SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDM--- 67
Cdd:PRK15112 1 VETLLEVRNLSKTFRYrtgwFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 68 DKHERKSK---------------NKIGIVLDEgyfydELTLKemkniiapsyTDWDEPVFQdyiKQFNLNLKQ------- 125
Cdd:PRK15112 81 DYSYRSQRirmifqdpstslnprQRISQILDF-----PLRLN----------TDLEPEQRE---KQIIETLRQvgllpdh 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 126 ---KISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIIL 202
Cdd:PRK15112 143 asyYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLV 222
|
....*..
gi 1261293288 203 IDDGKIL 209
Cdd:PRK15112 223 MHQGEVV 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-208 |
4.45e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNKcYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKH----------- 70
Cdd:PRK10982 248 EVILEVRNLTS-LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaneainhgfa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 71 ----ERKS---------------------KNKIGIVLDEGYFYDELTLKEMKNIIAPSYtdwdepvfqdyikqfnlnlKQ 125
Cdd:PRK10982 327 lvteERRStgiyayldigfnslisnirnyKNKVGLLDNSRMKSDTQWVIDSMRVKTPGH-------------------RT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 126 KISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFSTHITSDLDKIADMIILIDD 205
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSN 466
|
...
gi 1261293288 206 GKI 208
Cdd:PRK10982 467 GLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-163 |
4.65e-06 |
|
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: 47.98 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYE---NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLiLKDSGKINFLGNDMDKHERKSKNKIGIV 81
Cdd:TIGR01271 1218 MDVQGLTAKYTeagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYDELTLKemKNIiaPSYTDW---------DEPVFQDYIKQF----NLNLKQKISTLSKGMRMKFAVALALSHHA 148
Cdd:TIGR01271 1297 IPQKVFIFSGTFR--KNL--DPYEQWsdeeiwkvaEEVGLKSVIEQFpdklDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170
....*....|....*
gi 1261293288 149 DLLLMDEPTSGLDPL 163
Cdd:TIGR01271 1373 KILLLDEPSAHLDPV 1387
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-208 |
5.29e-06 |
|
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: 47.63 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 18 SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFlgndmdkherksKNKIGIVLDEGYFYDElTLKEmk 97
Cdd:TIGR00957 653 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------------KGSVAYVPQQAWIQND-SLRE-- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 98 NIIAPSytDWDEPVFQDYIKQFNL-------------NLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLV 164
Cdd:TIGR00957 718 NILFGK--ALNEKYYQQVLEACALlpdleilpsgdrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1261293288 165 RSELMDILLNFMKE-PGKSVFFSTHITSDLDKIaDMIILIDDGKI 208
Cdd:TIGR00957 796 GKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-207 |
6.80e-06 |
|
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: 47.24 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLilkDSgkiNFLGndmdkHERKSKN-KIGIVLDEGYFYDELT----- 92
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DK---DFNG-----EARPQPGiKVGYLPQEPQLDPTKTvrenv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 93 ---LKEMKNI------IAPSYTDWDEPV---------FQDYIKQ---FNLNLK--------------QKISTLSKGMRMK 137
Cdd:TIGR03719 90 eegVAEIKDAldrfneISAKYAEPDADFdklaaeqaeLQEIIDAadaWDLDSQleiamdalrcppwdADVTKLSGGERRR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1261293288 138 FAVALALSHHADLLLMDEPTSGLDplvrSELMDILLNFMKE-PGkSVFFSTHITSDLDKIADMIILIDDGK 207
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEyPG-TVVAVTHDRYFLDNVAGWILELDRGR 235
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-191 |
1.06e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKHERKSKNKIGIVLD 83
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 84 egyFYDELTLKEMKNIIAPSYTDWDE-PVFQDYIKQFNLnLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDP 162
Cdd:PRK13541 81 ---LKLEMTVFENLKFWSEIYNSAETlYAAIHYFKLHDL-LDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180
....*....|....*....|....*....
gi 1261293288 163 LVRsELMDILLNFMKEPGKSVFFSTHITS 191
Cdd:PRK13541 157 ENR-DLLNNLIVMKANSGGIVLLSSHLES 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-194 |
1.14e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.25 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLnKCYEN--FSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDkherksknkigiv 81
Cdd:PRK13539 2 MLEGEDL-ACVRGgrVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 lDEGYF----Y--------DELTLKEmkNIIApsytdW------DEPVFQDYIKQFNL----NLKQKisTLSKGMRMKFA 139
Cdd:PRK13539 68 -DPDVAeachYlghrnamkPALTVAE--NLEF-----WaaflggEELDIAAALEAVGLaplaHLPFG--YLSAGQKRRVA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 140 VALALSHHADLLLMDEPTSGLDplVRSELMdiLLNFMK---EPGKSVFFSTHITSDLD 194
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALD--AAAVAL--FAELIRahlAQGGIVIAATHIPLGLP 191
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-209 |
1.45e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.87 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCY-ENFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMDKheRKSKNK-IGIVL 82
Cdd:PRK11432 7 VVLKNITKRFgSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQRdICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGYFYDELTL---------------KEMKNIIAPSYTDWDEPVFQD-YIKQfnlnlkqkistLSKGMRMKFAVALALSH 146
Cdd:PRK11432 85 QSYALFPHMSLgenvgyglkmlgvpkEERKQRVKEALELVDLAGFEDrYVDQ-----------ISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1261293288 147 HADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
123-204 |
1.98e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 123 LKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFmkePGKSVFFStHITSDLDKIADMIIL 202
Cdd:PRK10636 143 LERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSY---QGTLILIS-HDRDFLDPIVDKIIH 218
|
..
gi 1261293288 203 ID 204
Cdd:PRK10636 219 IE 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-213 |
2.81e-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: 45.20 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 2 NVMLEVNNLNkCYE--NFSLK---DVTFRISNDCITGFIGTNGSGKTTTIKAILGL--------ILKDSGKINF------ 62
Cdd:TIGR02633 255 DVILEARNLT-CWDviNPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAypgkfegnVFINGKPVDIrnpaqa 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 63 --LGNDMDKHERKsknKIGIVLDEGYFYDeLTLKEMKNIIAPSYTDwdEPVFQDYIKQFNLNLKQK-------ISTLSKG 133
Cdd:TIGR02633 334 irAGIAMVPEDRK---RHGIVPILGVGKN-ITLSVLKSFCFKMRID--AAAELQIIGSAIQRLKVKtaspflpIGRLSGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 134 MRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDiLLNFMKEPGKSVFFsthITSDLDK---IADMIILIDDGKI-- 208
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYK-LINQLAQEGVAIIV---VSSELAEvlgLSDRVLVIGEGKLkg 483
|
....*.
gi 1261293288 209 -LVNDE 213
Cdd:TIGR02633 484 dFVNHA 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-213 |
2.92e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.92 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 3 VMLEVNNLNkCY--ENFSLK---DVTFRISNDCITGFIGTNGSGKTTTIKAILGL--------ILKDSGKINF------- 62
Cdd:PRK13549 258 VILEVRNLT-AWdpVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAypgrwegeIFIDGKPVKIrnpqqai 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 63 -LGNDMDKHERKsknKIGIVLDEGYfydeltlkeMKNIIAPSYTDW------DEPVFQDYIKQFNLNLKQK-------IS 128
Cdd:PRK13549 337 aQGIAMVPEDRK---RDGIVPVMGV---------GKNITLAALDRFtggsriDDAAELKTILESIQRLKVKtaspelaIA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 129 TLSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpGKSVFFsthITSDLDK---IADMIILIDD 205
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIV---ISSELPEvlgLSDRVLVMHE 480
|
250
....*....|.
gi 1261293288 206 GKI---LVNDE 213
Cdd:PRK13549 481 GKLkgdLINHN 491
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-163 |
5.08e-05 |
|
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: 43.69 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYE---NFSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLiLKDSGKINFLGNDMDKHERKSKNKIGIV 81
Cdd:cd03289 3 MTVKDLTAKYTeggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 82 LDEGYFYDELTLKemKNIiaPSYTDW---------DEPVFQDYIKQF----NLNLKQKISTLSKGMRMKFAVALALSHHA 148
Cdd:cd03289 82 IPQKVFIFSGTFR--KNL--DPYGKWsdeeiwkvaEEVGLKSVIEQFpgqlDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170
....*....|....*
gi 1261293288 149 DLLLMDEPTSGLDPL 163
Cdd:cd03289 158 KILLLDEPSAHLDPI 172
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-221 |
9.00e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.89 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLI--------LKDSGKINFLGNDMDKHERKSKNKIGIVLDEG----- 85
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAaqpaf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 86 -YFYDELTL----KEMKNIIAPSYTDWDepvfqdyIKQFNLNL-------KQKISTLSKG--MRMKFAVALALSHHAD-- 149
Cdd:PRK13547 97 aFSAREIVLlgryPHARRAGALTHRDGE-------IAWQALALagatalvGRDVTTLSGGelARVQFARVLAQLWPPHda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 150 -----LLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDE-KDMLIDSH 221
Cdd:PRK13547 170 aqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGApADVLTPAH 247
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
15-49 |
1.89e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.23 E-value: 1.89e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1261293288 15 ENF-SLKDVTFRISNdcITGFIGTNGSGKTTTIKAI 49
Cdd:COG4637 8 KNFkSLRDLELPLGP--LTVLIGANGSGKSNLLDAL 41
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-225 |
2.09e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.90 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENF-SLKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNDMdkhERKSKNKI---G 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLlAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI---EGLPGHQIarmG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 80 IV--LDEGYFYDELTLKE----------MKNIIA-----PSYTDwDEPVFQDYIKQF--NLNLKQ----KISTLSKGMRM 136
Cdd:PRK11300 82 VVrtFQHVRLFREMTVIEnllvaqhqqlKTGLFSgllktPAFRR-AESEALDRAATWleRVGLLEhanrQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 137 KFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKILVNDEKDM 216
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
....*....
gi 1261293288 217 LIDSHALIK 225
Cdd:PRK11300 241 IRNNPDVIK 249
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
9-172 |
2.58e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 9 NLNKCYENfSLKDVTFRISNDCITGFIGTNGSGKTTTIKAILglilkdsgkinflgndmdkheRKSKNKIGIVLDEGYFY 88
Cdd:cd03238 2 TVSGANVH-NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---------------------YASGKARLISFLPKFSR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 89 DELT-LKEMKNIIApsytdwdepVFQDYikqfnLNLKQKISTLSKG--MRMKFAVALALSHHADLLLMDEPTSGLDPLVR 165
Cdd:cd03238 60 NKLIfIDQLQFLID---------VGLGY-----LTLGQKLSTLSGGelQRVKLASELFSEPPGTLFILDEPSTGLHQQDI 125
|
....*..
gi 1261293288 166 SELMDIL 172
Cdd:cd03238 126 NQLLEVI 132
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
131-209 |
2.96e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 2.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293288 131 SKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPGKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
124-161 |
3.26e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 3.26e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1261293288 124 KQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLD 161
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
130-220 |
4.14e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 130 LSKGMRMKFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEpgKSVFFSTHITSDLDKIADMIILIDDGKIL 209
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
90
....*....|.
gi 1261293288 210 VNDEKDMLIDS 220
Cdd:PRK14271 242 EEGPTEQLFSS 252
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-206 |
6.69e-04 |
|
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: 39.92 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTI-----KAILGLIlkdSGKINFLGNDMDKHERKSknkIGIVLDEGYFYDELTL 93
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAGVI---TGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 KEmkniiapsytdwdepvfqdyikqfNLNLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPTSGLDplvrSELMDILL 173
Cdd:cd03232 97 RE------------------------ALRFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD----SQAAYNIV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1261293288 174 NFMK---EPGKSVFFSTHITS-DLDKIADMIILIDDG 206
Cdd:cd03232 149 RFLKklaDSGQAILCTIHQPSaSIFEKFDRLLLLKRG 185
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-161 |
1.07e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 5 LEVNNLNKCYENFSL-KDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDSGKINFLGNdmdkherkskNKIG-IVL 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN----------ANIGyYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 83 DEGY-FYDELTLkemkniiapsyTDW---------DEPVFQDYIKQ--FNLN-LKQKISTLSKGM--RMKFAvALALSHH 147
Cdd:PRK15064 390 DHAYdFENDLTL-----------FDWmsqwrqegdDEQAVRGTLGRllFSQDdIKKSVKVLSGGEkgRMLFG-KLMMQKP 457
|
170
....*....|....
gi 1261293288 148 aDLLLMDEPTSGLD 161
Cdd:PRK15064 458 -NVLVMDEPTNHMD 470
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
130-164 |
1.31e-03 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 39.40 E-value: 1.31e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1261293288 130 LSKGMRMKFAVALALSHHADLLLMDEPTSGLDP-LV 164
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPeLV 190
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-209 |
2.07e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 4 MLEVNNLNKCYENFS-LKDVTFRISNDCITGFIGTNGSGKTTTIKAILG----LILkdSGKINFLGNDMDKHERKSKNKI 78
Cdd:CHL00131 7 ILEIKNLHASVNENEiLKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpayKIL--EGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 79 GIVLdeGYFY----------DELTLKEMKNIIAPSYTDWDEPVFQDYIKQfNLNL-KQKISTLSKGMRMKFA-------- 139
Cdd:CHL00131 85 GIFL--AFQYpieipgvsnaDFLRLAYNSKRKFQGLPELDPLEFLEIINE-KLKLvGMDPSFLSRNVNEGFSggekkrne 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293288 140 -VALALShHADLLLMDEPTSGLDplvrselMDIL------LNFMKEPGKSVFFSTHITSDLDKIA-DMIILIDDGKIL 209
Cdd:CHL00131 162 iLQMALL-DSELAILDETDSGLD-------IDALkiiaegINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKII 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-60 |
2.83e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.16 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293288 6 EVNNLNKCYENFSL-KDVTFRI-SNDCItGFIGTNGSGKTTTIKAILGLILKDSGKI 60
Cdd:PRK11147 321 EMENVNYQIDGKQLvKDFSAQVqRGDKI-ALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
108-204 |
3.35e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.73 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 108 DEPVFQDY-IKQFNLNLKQKISTLSKGMRM------KFAVALALSHHADLLLMDEPTSGLDPLVRSELMDILLNFMKEPG 180
Cdd:PRK01156 779 DIDVDQDFnITVSRGGMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSS 858
|
90 100
....*....|....*....|....*.
gi 1261293288 181 --KSVFFSTHiTSDLDKIADMIILID 204
Cdd:PRK01156 859 diPQVIMISH-HRELLSVADVAYEVK 883
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-230 |
5.79e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.85 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 19 LKDVTFRISNDCITGFIGTNGSGKTTTIKAILGLILKDS--GKINFLGNDMDKHERKSKNKIGIVLdegyFYDELTL--- 93
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGIVI----IHQELALipy 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 94 ------------KEMKNIIapsytDWDEPVFQ--DYIKQFNL--NLKQKISTLSKGMRMKFAVALALSHHADLLLMDEPT 157
Cdd:NF040905 93 lsiaeniflgneRAKRGVI-----DWNETNRRarELLAKVGLdeSPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 158 SGLDPLVRSELMDILLNFMKEPGKSVFFStHITSDLDKIADMIILIDDGK-ILVNDEKDMLIDSHALIKG------SNRF 230
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQGITSIIIS-HKLNEIRRVADSITVLRDGRtIETLDCRADEVTEDRIIRGmvgrdlEDRY 246
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
114-201 |
7.82e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.21 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293288 114 DYIKqfnlnLKQKISTLSKG--MRMKFAVALAL-SHHADLLLMDEPTSGLDPLVRSELMDIlLNFMKEPGKSVFFSTHiT 190
Cdd:cd03271 159 GYIK-----LGQPATTLSGGeaQRIKLAKELSKrSTGKTLYILDEPTTGLHFHDVKKLLEV-LQRLVDKGNTVVVIEH-N 231
|
90
....*....|.
gi 1261293288 191 SDLDKIADMII 201
Cdd:cd03271 232 LDVIKCADWII 242
|
|
| |
