|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
5.00e-105 |
|
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: 302.43 E-value: 5.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYV 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFALAS--GKGEEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPS 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAyaRRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 162 KGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELRED 222
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-232 |
4.12e-103 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 298.05 E-value: 4.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEE---TFALASGKGEEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLI 157
Cdd:COG0410 81 GYVPEGRRIFPSLTVEEnllLGAYARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 158 DEPSKGLSPIMIEKLMVAILKMK-EKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKYLGI 232
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-232 |
9.10e-73 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 220.86 E-value: 9.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYV 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFAL-ASGKGEEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSK 162
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTgLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 163 GLSPIMIEKLMVAILKMKEKT--TVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKetCHKYLGI 232
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK--VRRYLAV 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
1.33e-49 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 161.97 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEETFALAS--GKGEEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGffAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 159 EPSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKYLG 231
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-221 |
7.09e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 7.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLisRKGIGYV 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV--RRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFALASG----KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARlyglPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 160 PSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELRE 221
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-224 |
2.59e-44 |
|
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: 148.35 E-value: 2.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYV 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEE--------------TFALASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFI 149
Cdd:cd03219 81 FQIPRLFPELTVLEnvmvaaqartgsglLLARARREEREARERAEELLERV-GLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 150 NSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKE 224
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-221 |
5.73e-43 |
|
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: 145.39 E-value: 5.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLisRKGIGY 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA--RRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEE----TFALASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:COG4555 79 LPDERGLYDRLTVREniryFAELYGLFDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 159 EPSKGLSpIMIEKLMVAILK--MKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELRE 221
Cdd:COG4555 158 EPTNGLD-VMARRLLREILRalKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-225 |
5.15e-42 |
|
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: 142.47 E-value: 5.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGY 82
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 V---PENQgIFHDlTVEE--TFALA-SG-KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLL 155
Cdd:COG1122 80 VfqnPDDQ-LFAP-TVEEdvAFGPEnLGlPREEIRERVEEALELV-GLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 156 LIDEPSKGLSPIMIEKLMVAILKM-KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKET 225
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-220 |
3.88e-41 |
|
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: 139.95 E-value: 3.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 14 DQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqVNGLS--THLIS-RKGIGYVPENQGIF 90
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY-----INGYSirTDRKAaRQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 91 HDLTVEET---FALASGK-GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP 166
Cdd:cd03263 88 DELTVREHlrfYARLKGLpKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447119455 167 IMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELR 220
Cdd:cd03263 167 ASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-211 |
2.94e-40 |
|
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: 137.27 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlisRKGIGYV 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEET--FALASGKG--EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:cd03259 78 FQDYALFPHLTVAENiaFGLKLRGVpkAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 160 PSKGLSPIMIEKLMVAILKM--KEKTTVLLV----EQNFMMASQIgdyfYIMDNGRIV 211
Cdd:cd03259 157 PLSALDAKLREELREELKELqrELGITTIYVthdqEEALALADRI----AVMNEGRIV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
18-209 |
2.54e-38 |
|
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: 132.21 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYV---PENQgIFHDlT 94
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVfqnPDDQ-FFGP-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 95 VEE--TFAL--ASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIE 170
Cdd:cd03225 93 VEEevAFGLenLGLPEEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447119455 171 KLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGR 209
Cdd:cd03225 172 ELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
7.95e-38 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 132.47 E-value: 7.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEETFALA----SGKG---------------EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQM 141
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLVAaharLGRGllaallrlprarreeREARERAEELLERV-GLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 142 LAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKE--KTTVLLVEQN--FMMAsqIGDYFYIMDNGRIVHKGFMN 217
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDmdLVMG--LADRIVVLDFGRVIAEGTPA 238
|
250
....*....|....
gi 447119455 218 ELREDKETCHKYLG 231
Cdd:COG0411 239 EVRADPRVIEAYLG 252
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-214 |
1.13e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.46 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlisRKGI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE---KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEE--TFALASGK--GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLL 156
Cdd:COG3842 80 GMVFQDYALFPHLTVAEnvAFGLRMRGvpKAEIRARVAELLELV-GLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 157 IDEPSKGLSPIMIEKL---MVAILKmKEKTTVLLV----EQNFMMASQIGdyfyIMDNGRIVHKG 214
Cdd:COG3842 159 LDEPLSALDAKLREEMreeLRRLQR-ELGITFIYVthdqEEALALADRIA----VMNDGRIEQVG 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-210 |
2.56e-37 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 128.28 E-value: 2.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNglSTHLISRKGIGYV 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFalasgkgeevhekidwmlelfpdlkqfwnkksgLLSGGQKQMLAISRAFINSDGLLLIDEPSKG 163
Cdd:cd03230 79 PEEPSLYENLTVRENL---------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447119455 164 LSPIMIEKLMVAILKM-KEKTTVLLVEQNFMMASQIGDYFYIMDNGRI 210
Cdd:cd03230 126 LDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-214 |
2.83e-37 |
|
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: 130.93 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGY 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEETFALA--------SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGL 154
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGryphlglfGRPSAEDREAVEEALERT-GLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 155 LLIDEPSKGLSPIMIEKLM--VAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLelLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-231 |
2.39e-36 |
|
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: 127.66 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYVPENQGIFHDLTVE 96
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFRKLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 97 ETFALA----SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKL 172
Cdd:cd03218 94 ENILAVleirGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 173 --MVAILKMKeKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKYLG 231
Cdd:cd03218 173 qkIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-214 |
2.79e-36 |
|
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: 127.62 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLD----QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHL--IS 76
Cdd:cd03257 1 LLEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 RKGIGYVPenQGIFHDL----TVEETFA------LASGKGEEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISR 146
Cdd:cd03257 81 RKEIQMVF--QDPMSSLnprmTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 147 AFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-222 |
4.12e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 129.07 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFhriangeIYYDSTQV--NGLSTHLISRKGIG 81
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI-------LAPDSGEVlwDGEPLDPEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFHDLTVEETFA-LASGKG---EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLI 157
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVyLARLKGlskAEAKRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 158 DEPSKGLSPIMIEKLMVAILKMKEK-TTVL-------LVEqnfmmasQIGDYFYIMDNGRIVHKGFMNELRED 222
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAKgTTVIfsshqmeLVE-------ELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-209 |
3.86e-35 |
|
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: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 5 QVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVP 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 85 EnqgifhdltveetfalasgkgeevhekidwmlelfpdlkqfwnkksglLSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:cd00267 80 Q------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447119455 165 SPIMIEKLMVAILKM-KEKTTVLLVEQNFMMASQIGDYFYIMDNGR 209
Cdd:cd00267 112 DPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-231 |
4.47e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.06 E-value: 4.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVE-------ETFALASgkgEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDG 153
Cdd:COG1137 81 GYLPQEASIFRKLTVEdnilavlELRKLSK---KEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 154 LLLIDEPSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKYLG 231
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERgIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-211 |
7.20e-34 |
|
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: 121.13 E-value: 7.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRI-----ANGEIYYDSTQVNGLSTHLIS-R 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 78 KGIGYVPENQGIFHdLTVEETFALA-----SGKGEEVHEKIDWMLE---LFPDLKQfwNKKSGLLSGGQKQMLAISRAFI 149
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGlrlhgIKLKEELDERVEEALRkaaLWDEVKD--RLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 150 NSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIV 211
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-221 |
3.37e-33 |
|
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: 119.70 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS--RKG 79
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 80 IGYVPENQGIFHDLTVEE--TFAL--ASGKGE-EVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGL 154
Cdd:COG1127 84 IGMLFQGGALFDSLTVFEnvAFPLreHTDLSEaEIRELVLEKLELV-GLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 155 LLIDEPSKGLSPIM---IEKLmvaILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELRE 221
Cdd:COG1127 163 LLYDEPTAGLDPITsavIDEL---IRELRDElgLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-231 |
6.91e-33 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 118.92 E-value: 6.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYV 83
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETF--ALASGKG---EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:TIGR04406 82 PQEASIFRKLTVEENImaVLEIRKDldrAEREERLEALLEEF-QISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 159 EPSKGLSPIMIEKLMVAILKMKEKTT-VLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKYLG 231
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIgVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-211 |
7.54e-33 |
|
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: 118.02 E-value: 7.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 5 QVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqVNGLSTHLiSRKGIGYVP 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR-----VFGKPLEK-ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 85 ENQGIFHD--LTVEETFALA--------SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGL 154
Cdd:cd03235 75 QRRSIDRDfpISVRDVVLMGlyghkglfRRLSKADKAKVDEALERV-GLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 155 LLIDEPSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYfYIMDNGRIV 211
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDR-VLLLNRTVV 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-214 |
1.15e-32 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 117.77 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSTHLISRKGIGYV 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV-----LFDGKPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFA-LASGKG---EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:cd03269 76 PEERGLYPKMKVIDQLVyLAQLKGlkkEEARRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 160 PSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-160 |
1.74e-32 |
|
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: 115.44 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlISRKGIGYVPENQGIFHDLTVEET 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 99 FALA--------SGKGEEVHEKIDWmLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:pfam00005 80 LRLGlllkglskREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-214 |
3.03e-32 |
|
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: 117.44 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHiLQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSThliSRKGIGYV 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFA----LASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:cd03299 77 PQNYALFPHMTVYKNIAyglkKRKVDKKEIERKVLEIAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 160 PSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEfgVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
18-209 |
3.53e-32 |
|
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: 115.17 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFHDlTVEE 97
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL-RKNIAYVPQDPFLFSG-TIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 tfalasgkgeevhekidwmlelfpdlkqfwNkksgLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAIL 177
Cdd:cd03228 95 ------------------------------N----ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|..
gi 447119455 178 KMKEKTTVLLVEQNFMMAsQIGDYFYIMDNGR 209
Cdd:cd03228 141 ALAKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-220 |
1.05e-31 |
|
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: 115.54 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTT-------LRSVMGFHRIANGEIYYDSTQVnglsthlis 76
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTikmlttlLKPTSGRATVAGHDVVREPREV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 RKGIGYVPENQGIFHDLTVEETFA----LASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSD 152
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYiharLYGVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 153 GLLLIDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELR 220
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfgMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
1.12e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSTHLiSRKGI 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV-----RLFGKPPRR-ARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHD--LTVEETFA--------LASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFIN 150
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDVVLmgrygrrgLFRRPSRADREAVDEALERV-GLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 151 SDGLLLIDEPSKGLSPIMIEKLMvAILKM--KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVH 212
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALY-ELLRElrREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-231 |
1.51e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 115.98 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIG 81
Cdd:COG4674 9 PILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFHDLTVEETFALASGK------------GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFI 149
Cdd:COG4674 89 RKFQKPTVFEELTVFENLELALKGdrgvfaslfarlTAEERDRIEEVLETI-GLTDKADRLAGLLSHGQKQWLEIGMLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 150 NSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNfmMA--SQIGDYFYIMDNGRIVHKGFMNELREDKETCH 227
Cdd:COG4674 168 QDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHD--MEfvRQIARKVTVLHQGSVLAEGSLDEVQADPRVIE 245
|
....
gi 447119455 228 KYLG 231
Cdd:COG4674 246 VYLG 249
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-214 |
2.95e-31 |
|
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: 114.64 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlisRKGIGYV 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFA----LASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:cd03300 78 FQNYALFPHLTVFENIAfglrLKKLPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 160 PSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-188 |
2.95e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 115.19 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNI----ETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlis 76
Cdd:COG1116 5 APALELRGVskrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 rkgIGYVPENQGIFHDLTVEE--TFAL-ASGKG-EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSD 152
Cdd:COG1116 82 ---RGVVFQEPALLPWLTVLDnvALGLeLRGVPkAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 447119455 153 GLLLIDEPSKGLSPIMIEKLMVAILK--MKEKTTVLLV 188
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFV 195
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-210 |
3.02e-31 |
|
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: 114.12 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLDQ---FHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTH---LIS 76
Cdd:cd03255 1 IELKNLSkTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 RKGIGYVPENQGIFHDLTVEETFALA---SG-KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSD 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPlllAGvPKKERRERAEELLERV-GLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 153 GLLLIDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASqIGDYFYIMDNGRI 210
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-223 |
4.31e-31 |
|
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: 114.59 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLI--SRKGI 80
Cdd:cd03256 1 IEVENLSkTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEE---TFALASgkgeevHEKIDWMLELFP--------------DLKQFWNKKSGLLSGGQKQMLA 143
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnvlSGRLGR------RSTWRSLFGLFPkeekqralaalervGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 144 ISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILK--MKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELRE 221
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD 234
|
..
gi 447119455 222 DK 223
Cdd:cd03256 235 EV 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-214 |
5.14e-31 |
|
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: 113.62 E-value: 5.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 16 FHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSTH---LISRKGIGYVPENQGIFHD 92
Cdd:cd03266 18 VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA-----TVDGFDVVkepAEARRRLGFVSDSTGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 LTVEET---FALASG-KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIM 168
Cdd:cd03266 93 LTARENleyFAGLYGlKGDELTARLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447119455 169 IEKLMVAILKMKEKTTVLLVEQNFMM-ASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03266 172 TRALREFIRQLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-220 |
6.52e-31 |
|
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: 113.75 E-value: 6.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTH--LISRKGIG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFHDLTVEETFAL-----ASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLL 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFplrehTRLSEEEIREIVLEKLEAV-GLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 157 IDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELR 220
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-209 |
1.29e-30 |
|
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: 111.51 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS-THLISRKGIGY 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEETFALAsgkgeevhekidwmlelfpdlkqfwnkksglLSGGQKQMLAISRAFINSDGLLLIDEPSK 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447119455 163 GLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGR 209
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-231 |
1.41e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 113.55 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 21 GVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYVPENQGIFHDLTVEETFA 100
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 101 LA----------SG----------KGEEVHEKIDWMLELfpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:PRK11300 103 VAqhqqlktglfSGllktpafrraESEALDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 161 SKGLSPIMIEKL--MVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKYLG 231
Cdd:PRK11300 181 AAGLNPKETKELdeLIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAYLG 253
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
2.66e-30 |
|
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: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNN--IETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFH----RIAnGEIYYDSTQVNGLSTHLI 75
Cdd:COG1123 3 PLLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggRIS-GEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 76 SRKgIGYV---PENQgiFHDLTVEE--TFALASGK--GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAF 148
Cdd:COG1123 82 GRR-IGMVfqdPMTQ--LNPVTVGDqiAEALENLGlsRAEARARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 149 INSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-211 |
2.73e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSThliSRKGI 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP---KDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEE--TFALASGK--GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLL 156
Cdd:COG3839 78 AMVFQSYALYPHMTVYEniAFPLKLRKvpKAEIDRRVREAAELL-GLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 157 IDEPskgLSPI-------MIEKLMvAILKmKEKTTVLLV--EQN--FMMASQIGdyfyIMDNGRIV 211
Cdd:COG3839 157 LDEP---LSNLdaklrveMRAEIK-RLHR-RLGTTTIYVthDQVeaMTLADRIA----VMNDGRIQ 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-212 |
3.57e-30 |
|
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: 111.41 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLD---QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlisrkg 79
Cdd:cd03293 1 LEVRNVSkTYGGgggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 80 IGYVPENQGIFHDLTVEETFAL----ASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLL 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALglelQGVPKAEARERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 156 LIDEPSKGLSPIMIEKLMVAILKM--KEKTTVLLV----EQNFMMASQIgdyfYIMDN--GRIVH 212
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwrETGKTVLLVthdiDEAVFLADRV----VVLSArpGRIVA 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
4.06e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.06 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYV 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW-RRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDlTVEETFALASGKGEEV--HEKIDWMLELFpDL-KQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRERKfdRERALELLERL-GLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 161 SKGLSP---IMIEKLMVAILKmKEKTTVLLV----EQnfmmASQIGDYFYIMDNGRI 210
Cdd:COG4619 158 TSALDPentRRVEELLREYLA-EEGRAVLWVshdpEQ----IERVADRVLTLEAGRL 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-210 |
5.87e-29 |
|
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: 108.00 E-value: 5.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS-RKGIGY 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEE--TFALASGKGEEVHEKIDWMLELFPD--LKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:cd03262 81 VFQQFNLFPHLTVLEniTLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 159 EPSKGLSPIMIE---KLMVAIlkMKEKTTVLLV--EQNFmmASQIGDYFYIMDNGRI 210
Cdd:cd03262 161 EPTSALDPELVGevlDVMKDL--AEEGMTMVVVthEMGF--AREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-214 |
7.25e-29 |
|
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: 107.73 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSThliSRKGIGYV 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFA----LASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:cd03301 78 FQNYALYPHMTVYDNIAfglkLRKVPKDEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 160 PSKGLSPimieKLMVAI------LKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03301 157 PLSNLDA----KLRVQMraelkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-214 |
7.32e-29 |
|
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: 106.75 E-value: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 5 QVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYVP 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 85 EnqgifhdltveetfalasgkgeevhekidwMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:cd03214 80 Q------------------------------ALELL-GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447119455 165 SP---IMIEKLMVAILKMKEKtTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03214 129 DIahqIELLELLRRLARERGK-TVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-172 |
1.16e-28 |
|
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: 107.18 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLisRKGIG 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY--RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFHDLTVEE--TFALASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:COG4133 79 YLGHADGLKPELTVREnlRFWAALYGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170
....*....|...
gi 447119455 160 PSKGLSPIMIEKL 172
Cdd:COG4133 158 PFTALDAAGVALL 170
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-211 |
1.43e-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: 112.30 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIE-TYL----DQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS- 76
Cdd:COG1123 260 LLEVRNLSkRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRe 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 -RKGIGYV---PENQgIFHDLTVEETFA-----LASGKGEEVHEKIDWMLE---LFPDlkqFWNKKSGLLSGGQKQMLAI 144
Cdd:COG1123 340 lRRRVQMVfqdPYSS-LNPRMTVGDIIAeplrlHGLLSRAERRERVAELLErvgLPPD---LADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 145 SRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKT--TVLLVEQNFMMASQIGDYFYIMDNGRIV 211
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-223 |
1.76e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 112.16 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGY 82
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDlTVEETFALASGK--GEEVHEKIDW--MLELFPDLKQFWNKKSG----LLSGGQKQMLAISRAFINSDGL 154
Cdd:COG4988 416 VPQNPYLFAG-TIRENLRLGRPDasDEELEAALEAagLDEFVAALPDGLDTPLGeggrGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 155 LLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLV---EQNFMMASQIgdyfYIMDNGRIVHKGFMNELREDK 223
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKGRTVILIthrLALLAQADRI----LVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-219 |
3.06e-27 |
|
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: 104.30 E-value: 3.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 7 NNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYVPEN 86
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK-IGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 87 QGIFHDLTVEETFALASG----KGEEVHEKIDWMLELFP-DLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPS 161
Cdd:cd03295 84 IGLFPHMTVEENIALVPKllkwPKEKIRERADELLALVGlDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 162 KGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-221 |
1.44e-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: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFHDlTVEE 97
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-RRQIGVVLQDVFLFSG-TIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFALASGKGEEvhEKIDWMLELFpDLKQFWNK-KSGL----------LSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP 166
Cdd:COG2274 568 NITLGDPDATD--EEIIEAARLA-GLHDFIEAlPMGYdtvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 167 IMIEKLMVAILKMKEKTTVLLV---EQNFMMASQIgdyfYIMDNGRIVHKGFMNELRE 221
Cdd:COG2274 645 ETEAIILENLRRLLKGRTVIIIahrLSTIRLADRI----IVLDKGRIVEDGTHEELLA 698
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-211 |
1.90e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.67 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 11 TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS--RKGIGYVPENQG 88
Cdd:COG2884 10 RYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylRRRIGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 89 IFHDLTVEE--TFAL-ASGKGE-EVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:COG2884 90 LLPDRTVYEnvALPLrVTGKSRkEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447119455 165 SPIMIEKLMvAILKM--KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIV 211
Cdd:COG2884 169 DPETSWEIM-ELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-214 |
1.91e-26 |
|
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: 101.50 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGtITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLisRKGIGYVPENQGIFHDLTVE 96
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL--RRRIGYLPQEFGVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 97 E---TFALASG-KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP---IMI 169
Cdd:cd03264 91 EfldYIAWLKGiPSKEVKARVDEVLELV-NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPeerIRF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447119455 170 EKLMVAIlkMKEKTTVL---LVEQNFMMASQIGdyfyIMDNGRIVHKG 214
Cdd:cd03264 170 RNLLSEL--GEDRIVILsthIVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
9-214 |
2.98e-26 |
|
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: 101.22 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 9 IETYLDQFHIlqGVSLTVEKGTiTVLFGRNGAGKTTTLRSVMGFHRIANGEI------YYDSTQVNGLSTHlisRKGIGY 82
Cdd:cd03297 6 IEKRLPDFTL--KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvLFDSRKKINLPPQ---QRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEE--TFALASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:cd03297 80 VFQQYALFPHLNVREnlAFGLKRKRNREDRISVDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 161 SKGLSPIMIEKLMVAILKMKE--KTTVLLVEQN----FMMASQIgdyfYIMDNGRIVHKG 214
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKnlNIPVIFVTHDlseaEYLADRI----VVMEDGRLQYIG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-214 |
3.43e-26 |
|
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: 101.50 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLI--SRKGIGYVPENQGIFHD 92
Cdd:cd03258 17 KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkARRRIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 LTVEETFAL----ASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIM 168
Cdd:cd03258 97 RTVFENVALpleiAGVPKAEIEERVLELLELV-GLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447119455 169 IEKLMVAILKMKEKT--TVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03258 176 TQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEG 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-214 |
5.45e-26 |
|
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: 100.37 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNI-ETYLDQfHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLisrKGIGY 82
Cdd:cd03268 1 LKTNDLtKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL---RRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEE---TFALASGKGEEVHEKIDWMLElfpdLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:cd03268 77 LIEAPGFYPNLTAREnlrLLARLLGIRKKRIDEVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 160 PSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
6.14e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.14 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSvmgFHRI--------ANGEIYYDSTQVNGLST 72
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRV---FNRLielypearVSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 73 HLISRK--GIGYVPE---NQGIFHDLTVEETFALASGKGEEVHEKIDWMLE---LFPDLKQFWNKKSGLLSGGQKQMLAI 144
Cdd:PRK14247 78 IELRRRvqMVFQIPNpipNLSIFENVALGLKLNRLVKSKKELQERVRWALEkaqLWDEVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 145 SRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL--RED 222
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVftNPR 237
|
....*...
gi 447119455 223 KETCHKYL 230
Cdd:PRK14247 238 HELTEKYV 245
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-231 |
1.86e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.58 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEETFALA-----SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLL 155
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVlqirdDLSAEQREDRANELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 156 LIDEPSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKYLG 231
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-211 |
2.19e-25 |
|
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: 98.48 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 11 TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqVNGLSTHLISR-KGIGYVPENQG- 88
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL-----LNGKPIKAKERrKSIGYVMQDVDy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 89 -IFHDlTVEETFALASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI 167
Cdd:cd03226 83 qLFTD-SVREELLLGLKELDAGNEQAETVLKDL-DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447119455 168 MIEKLMVAILKM-KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIV 211
Cdd:cd03226 161 NMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-211 |
2.44e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 97.11 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYV 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PEnqgifhdltveetfalasgkgeevhekidwmlelfpdlkqfwnkksglLSGGQKQMLAISRAFINSDGLLLIDEPSKG 163
Cdd:cd03216 81 YQ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447119455 164 LSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIV 211
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-214 |
4.11e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 100.99 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqVNG--LSTHLISRK-GI 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV-----LNGrdLFTNLPPRErRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEE--TFALASGKG--EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLL 156
Cdd:COG1118 78 GFVFQHYALFPHMTVAEniAFGLRVRPPskAEIRARVEELLELV-QLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 157 IDEP--------SKGLspimiEKLMVAILKmKEKTTVLLV----EQNFMMASQIGdyfyIMDNGRIVHKG 214
Cdd:COG1118 157 LDEPfgaldakvRKEL-----RRWLRRLHD-ELGGTTVFVthdqEEALELADRVV----VMNQGRIEQVG 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-223 |
1.89e-24 |
|
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: 96.98 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNI-ETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLI--SRKG 79
Cdd:TIGR02315 1 MLEVENLsKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrkLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 80 IGYVPENQGIFHDLTVEETF---ALASgkgeevHEKIDWMLELFP--------------DLKQFWNKKSGLLSGGQKQML 142
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGY------KPTWRSLLGRFSeedkeralsalervGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 143 AISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELR 220
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdgITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
...
gi 447119455 221 EDK 223
Cdd:TIGR02315 235 DEV 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
4.25e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHliSRKGIG 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH--ARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFHDLTVEET-------FALASGkgeEVHEKIDWMLElFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGL 154
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENllvfgryFGLSAA---AARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 155 LLIDEPSKGLSP----IMIEKLMVAILKMKektTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETC 226
Cdd:PRK13537 160 LVLDEPTTGLDPqarhLMWERLRSLLARGK---TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGC 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-225 |
5.62e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.37 E-value: 5.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlisRKGIGY 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEE--TFALASGK--GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:PRK11607 96 MFQSYALFPHMTVEQniAFGLKQDKlpKAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 159 EPSKGLSPIMIEKLMVAILKMKEKTTVLLV------EQNFMMASQIGdyfyIMDNGRIVHKGFMNELREDKET 225
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVmvthdqEEAMTMAGRIA----IMNRGKFVQIGEPEEIYEHPTT 243
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-188 |
9.56e-24 |
|
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: 98.90 E-value: 9.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSTHLIS----RK 78
Cdd:TIGR02857 322 LEFSGVSvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-----AVNGVPLADADadswRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 79 GIGYVPENQGIFHDlTVEETFALAS--GKGEEVHEKID--WMLELFPDLKQFWNKKSG----LLSGGQKQMLAISRAFIN 150
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLARpdASDAEIREALEraGLDEFVAALPQGLDTPIGeggaGLSGGQAQRLALARAFLR 475
|
170 180 190
....*....|....*....|....*....|....*...
gi 447119455 151 SDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLV 188
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLV 513
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-224 |
1.99e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.52 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRS------------VMGFHRIANGEIYydSTQVNGLS 71
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearVEGEVRLFGRNIY--SPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 72 ThlisRKGIGYVPENQGIFHDLTVEETFA-------LASGKgEEVHEKIDWMLE---LFPDLKQFWNKKSGLLSGGQKQM 141
Cdd:PRK14267 83 V----RREVGMVFQYPNPFPHLTIYDNVAigvklngLVKSK-KELDERVEWALKkaaLWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 142 LAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELRE 221
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
...
gi 447119455 222 DKE 224
Cdd:PRK14267 238 NPE 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-214 |
2.18e-23 |
|
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: 93.81 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 14 DQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFHDl 93
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLFYG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEETFALA--SGKGEEVHEKIDwmlelFPDLKQFWNK-KSGL----------LSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:cd03245 93 TLRDNITLGapLADDERILRAAE-----LAGVTDFVNKhPNGLdlqigergrgLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 161 SKGLSpIMIEKLMVAILK--MKEKTTVLLVEQNFMMasQIGDYFYIMDNGRIVHKG 214
Cdd:cd03245 168 TSAMD-MNSEERLKERLRqlLGDKTLIIITHRPSLL--DLVDRIIVMDSGRIVADG 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-214 |
8.94e-23 |
|
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: 91.79 E-value: 8.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 23 SLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVnglsTHL-ISRKGIGYVPENQGIFHDLTVEETFAL 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV----TAApPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 102 ASGKG----EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKL--MVA 175
Cdd:cd03298 94 GLSPGlkltAEDRQAIEVALARV-GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMldLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 447119455 176 ILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-223 |
9.93e-23 |
|
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: 92.29 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFHDlTVE 96
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL-RSMIGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 97 ETFALAS--GKGEEVHE-----KIDWMLELFPD-LKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIM 168
Cdd:cd03254 95 ENIRLGRpnATDEEVIEaakeaGAHDFIMKLPNgYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 169 IEKLMVAILKMKEKTTVllveqnFMMA---SQI--GDYFYIMDNGRIVHKGFMNELREDK 223
Cdd:cd03254 175 EKLIQEALEKLMKGRTS------IIIAhrlSTIknADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-210 |
1.53e-22 |
|
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: 90.57 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNietyLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIG 81
Cdd:cd03215 3 PVLEVRG----LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPEN---QGIFHDLTVEETFALASgkgeevhekidwmlelfpdlkqfwnkksgLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:cd03215 79 YVPEDrkrEGLVLDLSVAENIALSS-----------------------------LLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 159 EPSKGLSPIMIEKLMVAILKMKEK-TTVLLV----EQNFMMASQIgdyfYIMDNGRI 210
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAgKAVLLIsselDELLGLCDRI----LVMYEGRI 182
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-211 |
2.59e-22 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 94.93 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDstqvnGLSTHLIS----RKGIGYVPENQGIFHDlT 94
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLD-----GVDIRQIDpadlRRNIGYVPQDPRLFYG-T 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 95 VEETFALASGKGEEvhEKIDWMLELFpDLKQFWNKK-SGL----------LSGGQKQMLAISRAFINSDGLLLIDEPSKG 163
Cdd:TIGR03375 555 LRDNIALGAPYADD--EEILRAAELA-GVTEFVRRHpDGLdmqigergrsLSGGQRQAVALARALLRDPPILLLDEPTSA 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447119455 164 LSpIMIEKLMVAILK--MKEKTTVLLVEQNFMMasQIGDYFYIMDNGRIV 211
Cdd:TIGR03375 632 MD-NRSEERFKDRLKrwLAGKTLVLVTHRTSLL--DLVDRIIVMDNGRIV 678
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-212 |
3.11e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 90.87 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIE-TYLD---QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS- 76
Cdd:COG1136 3 PLLELRNLTkSYGTgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 --RKGIGYVPenQGiFH---DLTVEETFALA---SGKG-EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRA 147
Cdd:COG1136 83 lrRRHIGFVF--QF-FNllpELTALENVALPlllAGVSrKERRERARELLERV-GLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 148 FINSDGLLLIDEPSKGLSPIMIEKLMVAILKM--KEKTTVLLVEQNFMMASqIGDYFYIMDNGRIVH 212
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-219 |
9.56e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 89.60 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 12 YLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFH 91
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL-RRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 D------------LTVEETFALAsgKGEEVHEKIdwmlELFPDLKQFWNKKSGL-LSGGQKQMLAISRAFINSDGLLLID 158
Cdd:cd03253 89 DtigynirygrpdATDEEVIEAA--KAAQIHDKI----MRFPDGYDTIVGERGLkLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 159 EPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNF---MMASQIgdyfYIMDNGRIVHKGFMNEL 219
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTIVIAHRLstiVNADKI----IVLKDGRIVERGTHEEL 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-212 |
1.25e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.76 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGT-ITVLfGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYVPEN--QGIFHDL 93
Cdd:COG1101 20 RALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDpmMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEETFALASGKG--------------EEVHEKIDwMLELfpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:COG1101 98 TIEENLALAYRRGkrrglrrgltkkrrELFRELLA-TLGL--GLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 160 PSKGLSPIMIEKLMVAILKM--KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVH 212
Cdd:COG1101 175 HTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-223 |
3.78e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYVPENQGIFHDLTVEET 98
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 99 FALasgkGEEVHEK--IDW---------MLELF-----PDlkqfwnKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSK 162
Cdd:COG1129 100 IFL----GREPRRGglIDWramrrrareLLARLgldidPD------TPVGDLSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 163 GLSPIMIEKLMVAILKMKEK-TTVLLV----EQNFmmasQIGDYFYIMDNGRIVHKGFMNELREDK 223
Cdd:COG1129 170 SLTEREVERLFRIIRRLKAQgVAIIYIshrlDEVF----EIADRVTVLRDGRLVGTGPVAELTEDE 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-224 |
5.59e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 12 YLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS-RKGIGYV---PENQ 87
Cdd:PRK13636 15 YSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlRESVGMVfqdPDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 88 GIFHDLTVEETFALASGK--GEEVHEKIDWMLELfPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLS 165
Cdd:PRK13636 95 LFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKR-TGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 166 PIMIEKLMVAILKMKEKT--TVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKE 224
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
4-210 |
8.66e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 86.84 E-value: 8.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIeTYLDQfHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSThliSRKGIGYV 83
Cdd:TIGR01277 1 LALDKV-RYEYE-HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP---YQRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFALASGKG--------EEVHE-----KIDWMLELFPdlkqfwnkksGLLSGGQKQMLAISRAFIN 150
Cdd:TIGR01277 76 FQENNLFAHLTVRQNIGLGLHPGlklnaeqqEKVVDaaqqvGIADYLDRLP----------EQLSGGQRQRVALARCLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 151 SDGLLLIDEPSKGLSPIMIEKL--MVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRI 210
Cdd:TIGR01277 146 PNPILLLDEPFSALDPLLREEMlaLVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-222 |
1.27e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 88.32 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 34 LFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlisRKGIGYVPENQGIFHDLTVEET--FALASGK--GEEV 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH---LRHINMVFQSYALFPHMTVEENvaFGLKMRKvpRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 110 HEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK--TTVLL 187
Cdd:TIGR01187 78 KPRVLEALRLV-QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlgITFVF 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 447119455 188 V----EQNFMMASQIGdyfyIMDNGRIVHKGFMNELRED 222
Cdd:TIGR01187 157 VthdqEEAMTMSDRIA----IMRKGKIAQIGTPEEIYEE 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-214 |
1.31e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 89.84 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 11 TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIF 90
Cdd:COG1132 348 SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL-RRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 91 HDlTVEETFALasGKG----EEV---------HEKIdwmlELFPDlkqfwnkksGL----------LSGGQKQMLAISRA 147
Cdd:COG1132 427 SG-TIRENIRY--GRPdatdEEVeeaakaaqaHEFI----EALPD---------GYdtvvgergvnLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 148 FI-NSDgLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNF---MMASQIgdyfYIMDNGRIVHKG 214
Cdd:COG1132 491 LLkDPP-ILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLstiRNADRI----LVLDDGRIVEQG 556
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-224 |
1.94e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.75 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVmgfHRIAN--------GEIYYDSTQVNGLSTH 73
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI---NRMNDlnpevtitGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 74 LIS-RKGIGYVPENQGIFHDLTVEETFALASGKGEEVHEKIDWMLElfPDLKQ--FWNK------KSGL-LSGGQKQMLA 143
Cdd:PRK14239 81 TVDlRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVE--KSLKGasIWDEvkdrlhDSALgLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 144 ISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG-----FMNE 218
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNdtkqmFMNP 238
|
....*.
gi 447119455 219 LREDKE 224
Cdd:PRK14239 239 KHKETE 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-214 |
2.58e-20 |
|
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: 86.29 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLrsvmgfhRIANGEIYydstQVNGLSTHL------ 74
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLL-------SLITGDLP----PTYGNDVRLfgerrg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 75 ------IsRKGIGYV-PENQGIFH-DLTVEEtfALASGK----------GEEVHEKIDWMLELFpDLKQFWNKKSGLLSG 136
Cdd:COG1119 70 gedvweL-RKRIGLVsPALQLRFPrDETVLD--VVLSGFfdsiglyrepTDEQRERARELLELL-GLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 137 GQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKL--MVAILKMKEKTTVLLVEQNfmmASQIGDYFY---IMDNGRIV 211
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLlaLLDKLAAEGAPTLVLVTHH---VEEIPPGIThvlLLKDGRVV 222
|
...
gi 447119455 212 HKG 214
Cdd:COG1119 223 AAG 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-214 |
3.60e-20 |
|
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: 84.52 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHR--IANGEIYydstqVNGLSTHLIS-RKGIGYVPENQGIFHDLT 94
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVL-----INGRPLDKRSfRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 95 VEETFALASGkgeevhekidwmlelfpdLKQfwnkksglLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMV 174
Cdd:cd03213 99 VRETLMFAAK------------------LRG--------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447119455 175 AILKM-KEKTTVLLV-----EQNFMMASQIgdyfYIMDNGRIVHKG 214
Cdd:cd03213 153 LLRRLaDTGRTIICSihqpsSEIFELFDKL----LLLSQGRVIYFG 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-210 |
7.31e-20 |
|
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: 84.70 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSthlISRKGIGYV 83
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEE--TFALASGKGE------EVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLL 155
Cdd:cd03296 80 FQHYALFRHMTVFDnvAFGLRVKPRSerppeaEIRAKVHELLKLV-QLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 156 LIDEPSKGLSPIMIEKLMVAILKMKEKT--TVLLVEQNFMMASQIGDYFYIMDNGRI 210
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-214 |
8.04e-20 |
|
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: 85.39 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS-THL--ISRKGIGYVPENQGIFHDLTV 95
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrKELreLRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 EETFALA---SGKGEEV-HEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI---- 167
Cdd:cd03294 120 LENVAFGlevQGVPRAErEERAAEALELV-GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLirre 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447119455 168 MIEKLMVaiLKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03294 199 MQDELLR--LQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
1.37e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.42 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIetyLDQFH---ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFH-----RIANGEIYYDST----QVN 68
Cdd:PRK11264 1 MSAIEVKNL---VKKFHgqtVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEqpeagTIRVGDITIDTArslsQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 69 GLSTHLisRKGIGYVPENQGIFHDLTVEETfaLASG----KGEEVHEKIDWMLELFpdlkqfwnKKSGL----------L 134
Cdd:PRK11264 78 GLIRQL--RQHVGFVFQNFNLFPHRTVLEN--IIEGpvivKGEPKEEATARARELL--------AKVGLagketsyprrL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 135 SGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKM-KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHK 213
Cdd:PRK11264 146 SGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
....*.
gi 447119455 214 GFMNEL 219
Cdd:PRK11264 226 GPAKAL 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-214 |
2.05e-19 |
|
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: 83.09 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMG---FHRIANGEIYYDSTQvngLSTHLiSRKGIGYVPEnQGIFHD-L 93
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQP---RKPDQ-FQKCVAYVRQ-DDILLPgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEET------FALASGKGEEVHEKID-WMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP 166
Cdd:cd03234 97 TVRETltytaiLRLPRKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447119455 167 iMIEKLMVAILK--MKEKTTVLL-VEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03234 177 -FTALNLVSTLSqlARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-223 |
2.71e-19 |
|
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: 85.16 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 22 VSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIY------YDSTQVNGLSTHlisRKGIGYVPENQGIFHDLTV 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlFDSRKGIFLPPE---KRRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 EET--FALASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLM 173
Cdd:TIGR02142 93 RGNlrYGMKRARPSERRISFERVIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447119455 174 VAILKMKEKTT--VLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDK 223
Cdd:TIGR02142 172 PYLERLHAEFGipILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
3.24e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.59 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIE-TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS-RKGI 80
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYV---PENQgIFHDlTVEETFA---LASG-KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDG 153
Cdd:PRK13639 81 GIVfqnPDDQ-LFAP-TVEEDVAfgpLNLGlSKEEVEKRVKEALKAV-GMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 154 LLLIDEPSKGLSPIMIEKLMVAILKM-KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKET 225
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-160 |
3.49e-19 |
|
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: 84.77 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 22 VSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHR-----IA-NGEIYYDSTQVNGLSTHlisRKGIGYVPENQGIFHDLTV 95
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERpdsgrIRlGGEVLQDSARGIFLPPH---RRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 96 EET------FALASGKGEEVHEKIDwMLELFPDLkqfwNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:COG4148 95 RGNllygrkRAPRAERRISFDEVVE-LLGIGHLL----DRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-222 |
3.52e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGY 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEETFALASGKGEEVH--EKIDW--------MLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSD 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVCgvNIIDWremrvraaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 153 GLLLIDEPSKGLSPIMIEKLMVAILKM-KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELRED 222
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-166 |
4.01e-19 |
|
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: 82.07 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS--RKGIGYVPENQGIFHDLTVE 96
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 97 ETFALA----SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP 166
Cdd:cd03292 97 ENVAFAlevtGVPPREIRKRVPAALELV-GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-219 |
4.17e-19 |
|
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: 82.66 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFHDlTVEE 97
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL-RRQIGLVSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TfaLASGKGEEVHEKIDWMLEL---------FPD-LKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGL--- 164
Cdd:cd03251 95 N--IAYGRPGATREEVEEAARAanahefimeLPEgYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALdte 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 165 SpimiEKLMVAILK--MKEKTTvllveqnFMMA---SQI--GDYFYIMDNGRIVHKGFMNEL 219
Cdd:cd03251 173 S----ERLVQAALErlMKNRTT-------FVIAhrlSTIenADRIVVLEDGKIVERGTHEEL 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-221 |
5.08e-19 |
|
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: 81.42 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFH--RIANGEIYYDSTQVNGLSTHLISRKGIG 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 ----YVPENQGI-FHDL--TVEETFalaSGkGEEvhekidwmlelfpdlkqfwnKKSGLLsggqkQMLAisrafINSDgL 154
Cdd:cd03217 81 lafqYPPEIPGVkNADFlrYVNEGF---SG-GEK--------------------KRNEIL-----QLLL-----LEPD-L 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 155 LLIDEPSKGLSPIMIEKLMVAILKMK-EKTTVLLVEQNFMMASQI-GDYFYIMDNGRIVHKGFMNELRE 221
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALE 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-188 |
8.86e-19 |
|
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: 84.33 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 12 YLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYVPENQGIFh 91
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSVCAQDAHLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 DLTVEETFALASGK--GEEVHEKI------DWMLELfPDLKQFWNKKSG-LLSGGQKQMLAISRAFINSDGLLLIDEPSK 162
Cdd:TIGR02868 422 DTTVRENLRLARPDatDEELWAALervglaDWLRAL-PDGLDTVLGEGGaRLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180
....*....|....*....|....*.
gi 447119455 163 GLSPIMIEKLMVAILKMKEKTTVLLV 188
Cdd:TIGR02868 501 HLDAETADELLEDLLAALSGRTVVLI 526
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-219 |
9.58e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.68 E-value: 9.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLST--HLIsRKGI 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdeRLI-RQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEETFALA----SGKGEEVHEKIdwMLELFpdlkqfwnKKSGL----------LSGGQKQMLAISR 146
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGplrvRGASKEEAEKQ--ARELL--------AKVGLaerahhypseLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 147 AFINSDGLLLIDEPSKGLSPimieKLMVAILK-MK----EKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDP----ELRHEVLKvMQdlaeEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-163 |
2.06e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYldqfHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGY 82
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPEN---QGIFHDLTVEETFALAS----------GKGEEvHEKIDWMLELF----PDLKQfwnkKSGLLSGGQKQMLAIS 145
Cdd:COG1129 332 VPEDrkgEGLVLDLSIRENITLASldrlsrggllDRRRE-RALAEEYIKRLriktPSPEQ----PVGNLSGGNQQKVVLA 406
|
170
....*....|....*...
gi 447119455 146 RAFINSDGLLLIDEPSKG 163
Cdd:COG1129 407 KWLATDPKVLILDEPTRG 424
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
17-164 |
2.79e-18 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 80.06 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS--RKGIGYVPENQGIFHDLT 94
Cdd:TIGR02982 19 QVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVqlRRRIGYIFQAHNLLGFLT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 95 VEE----TFALASGKG-EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:TIGR02982 99 ARQnvqmALELQPNLSyQEARERARAMLEAV-GLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAAL 172
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-226 |
2.99e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSThlISRKGIGYVPENQGIFHDLTVEE 97
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR--LARARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 T-------FALASGKGEEVhekIDWMLElFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP---- 166
Cdd:PRK13536 134 NllvfgryFGMSTREIEAV---IPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPharh 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 167 IMIEKLMVAILKMKektTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETC 226
Cdd:PRK13536 210 LIWERLRSLLARGK---TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGC 266
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
3.59e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.68 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNI----ETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSthliS 76
Cdd:COG4525 1 MSMLTVRHVsvryPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 RKGIgyVPENQGIFHDLTVEETFALA-----SGKGEEvHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINS 151
Cdd:COG4525 77 DRGV--VFQKDALLPWLNVLDNVAFGlrlrgVPKAER-RARAEELLALV-GLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 152 DGLLLIDEPSKGLSPIMIEKLMVAILKMKEKT--TVLL----VEQNFMMASQIgdyfYIMDN--GRIVH 212
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLithsVEEALFLATRL----VVMSPgpGRIVE 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-214 |
3.60e-18 |
|
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: 83.14 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 22 VSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVnglSTHL-ISRKGIGYVPENQGIFHDLTVEET-- 98
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLdAVRQSLGMCPQHNILFHHLTVAEHil 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 99 -FALASGKG-EEVHEKIDWMLElFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAI 176
Cdd:TIGR01257 1026 fYAQLKGRSwEEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....*...
gi 447119455 177 LKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-219 |
5.02e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 82.48 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFhDLTVEE 97
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL-RQFINYLPQEPYIF-SGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFALASGKG---EEVHEKIDwMLELFPDLKQF-------WNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI 167
Cdd:TIGR01193 567 NLLLGAKENvsqDEIWAACE-IAEIKDDIENMplgyqteLSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447119455 168 MIEKLMVAILKMKEKtTVLLVEQNFMMASQIgDYFYIMDNGRIVHKGFMNEL 219
Cdd:TIGR01193 646 TEKKIVNNLLNLQDK-TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-210 |
7.24e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.90 E-value: 7.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLstHLISRKgIGYV 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRK-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFALA--------SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLL 155
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGltvlprreRPNAAAIKAKVTQLLEMV-QLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 156 LIDEPSKGLSPIMIEKLMVAILKMKE--KTTVLLVEQNFMMASQIGDYFYIMDNGRI 210
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-214 |
9.09e-18 |
|
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: 77.74 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLDQF-HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLisRKGIG 81
Cdd:cd03247 1 LSINNVSfSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL--SSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFhDLTVEETFAlasgkgeevhekidwmlelfpdlKQFwnkksgllSGGQKQMLAISRAFINSDGLLLIDEPS 161
Cdd:cd03247 79 VLNQRPYLF-DTTLRNNLG-----------------------RRF--------SGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447119455 162 KGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIgDYFYIMDNGRIVHKG 214
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-162 |
1.37e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.91 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHR---IANGEIYYDSTQVNGLSTHlisRKGI 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAE---QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEET--FALASG-KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLI 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENlaFALPPTiGRAQRRARVEQALEEA-GLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
....*.
gi 447119455 158 DEP-SK 162
Cdd:COG4136 158 DEPfSK 163
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-232 |
1.38e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.26 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHiLQgVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSthlISRKGIGYV 83
Cdd:COG3840 2 LRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP---PAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFALA---SGK-GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGlrpGLKlTAEQRAQVEQALERV-GLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 160 PSKGLSPIM-IEKL-MVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL--REDKETCHKYLGI 232
Cdd:COG3840 156 PFSALDPALrQEMLdLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALldGEPPPALAAYLGI 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-210 |
1.41e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.93 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRS------------VMGFHRIANGEIYYDSTQVNGLs 71
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKClnrmnelesevrVEGRVEFFNQNIYERRVNLNRL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 72 thlisRKGIGYVPENQGIFhDLTVEETFALASG-KGEEVHEKIDWMLELFPDLKQFWNK------KSGL-LSGGQKQMLA 143
Cdd:PRK14258 87 -----RRQVSMVHPKPNLF-PMSVYDNVAYGVKiVGWRPKLEIDDIVESALKDADLWDEikhkihKSALdLSGGQQQRLC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 144 ISRAFINSDGLLLIDEPSKGLSPIMIEKL--MVAILKMKEKTTVLLVEQNFMMASQIGDY--FYIMDNGRI 210
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVesLIQSLRLRSELTMVIVSHNLHQVSRLSDFtaFFKGNENRI 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-211 |
1.45e-17 |
|
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: 79.71 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLD----QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHR---IANGEIYYDSTQVNGLSTHLI 75
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 76 SR---KGIGYvpenqgIFHD--------LTVEETFALA-----SGKGEEVHEKIDWMLEL--FPDLKQFWNKKSGLLSGG 137
Cdd:COG0444 81 RKirgREIQM------IFQDpmtslnpvMTVGDQIAEPlrihgGLSKAEARERAIELLERvgLPDPERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 138 QKQMLAISRAFINSDGLLLIDEPSKGLSPIM---IEKLMVAiLKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIV 211
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIqaqILNLLKD-LQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-214 |
3.37e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRsVMGFHRIA-NGEI-----YYDSTQVNGLSTHLISR 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETPdSGQLniaghQFDFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 78 KGIGYVPENQGIFHDLTVEETFALASGK-----GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSD 152
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPCKvlglsKEQAREKAMKLLARL-RLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 153 GLLLIDEPSKGLSPiMIEKLMVAILKMKEKT--TVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:COG4161 161 QVLLFDEPTAALDP-EITAQVVEIIRELSQTgiTQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
4.01e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.92 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNI-ETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKG 79
Cdd:PRK13652 1 MHLIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-RKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 80 IGYV---PENQgIFHDlTVEETFALAS---GKGEE-VHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSD 152
Cdd:PRK13652 80 VGLVfqnPDDQ-IFSP-TVEQDIAFGPinlGLDEEtVAHRVSSALHML-GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 153 GLLLIDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNE--LRED 222
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEifLQPD 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-214 |
5.48e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.47 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 11 TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYV---PENQ 87
Cdd:PRK13647 13 RYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-RSKVGLVfqdPDDQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 88 gIFhDLTVEETFALASG----KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKG 163
Cdd:PRK13647 92 -VF-SSTVWDDVAFGPVnmglDKDEVERRVEEALKAV-RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447119455 164 LSPIMIEKLMvAILKM--KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK13647 169 LDPRGQETLM-EILDRlhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-214 |
6.22e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEI-----YYDSTQVNGLSTHLISRK 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 79 GIGYVPENQGIFHDLTVEETFALASGK-----GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDG 153
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRvlglsKDQALARAEKLLERL-RLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 154 LLLIDEPSKGLSPiMIEKLMVAILKMKEKT--TVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK11124 162 VLLFDEPTAALDP-EITAQIVSIIRELAETgiTQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-214 |
6.76e-17 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 79.02 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDstqvnGLSTHLISR----KGIGYVPENQGIFhDL 93
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD-----GADLSQWDReelgRHIGYLPQDVELF-DG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEETFA-LASGKGEEV---------HEkidwMLELFPDlkqfwnkksG----------LLSGGQKQMLAISRAFINSDG 153
Cdd:COG4618 421 TIAENIArFGDADPEKVvaaaklagvHE----MILRLPD---------GydtrigeggaRLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 154 LLLIDEPSKGLSPIMIEKLMVAILKMKE-KTTVLLVEQNfMMASQIGDYFYIMDNGRIVHKG 214
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHR-PSLLAAVDKLLVLRDGRVQAFG 548
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-214 |
1.30e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.43 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTH-LIS-RKGIGYVPENQGIFHD 92
Cdd:COG1135 17 PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEReLRAaRRKIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 LTVEETFALA---SG-KGEEVHEKIDWMLEL---------FPDlkQfwnkksglLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:COG1135 97 RTVAENVALPleiAGvPKAEIRKRVAELLELvglsdkadaYPS--Q--------LSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 160 PSKGLSPIMIEklmvAILKM------KEKTTVLLV--EqnfmMA--SQIGDYFYIMDNGRIVHKG 214
Cdd:COG1135 167 ATSALDPETTR----SILDLlkdinrELGLTIVLIthE----MDvvRRICDRVAVLENGRIVEQG 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-210 |
1.32e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.68 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSThliSRKGI 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA---ENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEET--FALASGK--GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLL 156
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENvaFGLRMQKtpAAEITPRVMEALRMV-QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 157 IDEPskgLSPI--MIEKLMVAILKMKEKT---TVLLV----EQNFMMASQIgdyfYIMDNGRI 210
Cdd:PRK09452 168 LDES---LSALdyKLRKQMQNELKALQRKlgiTFVFVthdqEEALTMSDRI----VVMRDGRI 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-214 |
1.35e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.58 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 12 YLDQfHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS-RKGIGYV---PENQ 87
Cdd:PRK13638 11 YQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlRQQVATVfqdPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 88 GIFHDLTVEETFALAS-GKGE-EVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLS 165
Cdd:PRK13638 90 IFYTDIDSDIAFSLRNlGVPEaEITRRVDEALTLV-DAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447119455 166 PIMIEKlMVAILK--MKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK13638 169 PAGRTQ-MIAIIRriVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-201 |
1.75e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.97 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSvmgFHRI--------ANGEIYYDSTQVNGLSTHL 74
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRC---FNRLndlipgfrVEGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 75 IS-RKGIGYV-----PENQGIFHDLTVEETFALASGKGEEVHEKidwmlelfpDLKQ--FWN------KKSGL-LSGGQK 139
Cdd:PRK14243 87 VEvRRRIGMVfqkpnPFPKSIYDNIAYGARINGYKGDMDELVER---------SLRQaaLWDevkdklKQSGLsLSGGQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 140 QMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDY 201
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDM 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-214 |
1.98e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 75.93 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLDQF-HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqVNGLST------HLI 75
Cdd:TIGR04520 1 IEVENVSfSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVT-----VDGLDTldeenlWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 76 sRKGIGYV---PENQgiFHDLTVEE--TFALASgKG---EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRA 147
Cdd:TIGR04520 76 -RKKVGMVfqnPDNQ--FVGATVEDdvAFGLEN-LGvprEEMRKRVDEALKLV-GMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 148 F-INSDGLLLiDEPSKGLSPIMIEKLM--VAILKMKEKTTVLLVeQNFM----MAsqigDYFYIMDNGRIVHKG 214
Cdd:TIGR04520 151 LaMRPDIIIL-DEATSMLDPKGRKEVLetIRKLNKEEGITVISI-THDMeeavLA----DRVIVMNKGKIVAEG 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-229 |
2.84e-16 |
|
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: 74.88 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFhDLTVEE 97
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFALASGKGEEVHEK-------IDWMLELFPD-LKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGL---SP 166
Cdd:cd03249 96 NIRYGKPDATDEEVEeaakkanIHDFIMSLPDgYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALdaeSE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 167 IMIEKLMVAIlkMKEKTTV-----LLVEQNfmmasqiGDYFYIMDNGRIVHKGFMNELREDKETCHKY 229
Cdd:cd03249 176 KLVQEALDRA--MKGRTTIviahrLSTIRN-------ADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-224 |
2.85e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLI--SRKGIGYVPENQGIFHDLTV 95
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRMSMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 EETFALASGKGEEVHEKI---DWMLELFP-DLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEK 171
Cdd:PRK11831 102 FDNVAYPLREHTQLPAPLlhsTVMMKLEAvGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 172 LMVAI--LKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKE 224
Cdd:PRK11831 182 LVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-214 |
3.33e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 74.81 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQvnglsthlISRKGigyvPENQGIFHD------ 92
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ--------ITEPG----PDRMVVFQNysllpw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 LTVEETFALA------SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP 166
Cdd:TIGR01184 69 LTVRENIALAvdrvlpDLSKSERRAIVEEHIALV-GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447119455 167 IMIEKLMVAILKMKEKT--TVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-214 |
3.38e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSvmgFHRI---ANGEIYYDSTQVNGLSTHLISRKgIGYVPENQGIFHDLT 94
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKC---FARLltpQSGTVFLGDKPISMLSSRQLARR-LALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 95 VEETFALAS-------GK-GEEVHEKIDWMLELfPDLKQFWNKKSGLLSGGQKQmlaisRAFI------NSDgLLLIDEP 160
Cdd:PRK11231 93 VRELVAYGRspwlslwGRlSAEDNARVNQAMEQ-TRINHLADRRLTDLSGGQRQ-----RAFLamvlaqDTP-VVLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 161 SKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-219 |
3.52e-16 |
|
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: 74.83 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 14 DQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVnGLSTHLISRKGIGYVPENQGIFHDl 93
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPAWLRRQVGVVLQENVLFNR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEETFALASgKGEEVHEKI---------DWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:cd03252 91 SIRDNIALAD-PGMSMERVIeaaklagahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 165 ---SPIMIEKLMVAILKMKektTVLLVEQNfMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:cd03252 170 dyeSEHAIMRNMHDICAGR---TVIIIAHR-LSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-214 |
3.58e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.42 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgI 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEETFALA--------SGKGEEVHEKIDWMLELfPDLKQFWNKKSGLLSGGQKQMLAISRAFINSD 152
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGrtphrsrfDTWTETDRAAVERAMER-TGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 153 GLLLIDEPSKGLS-PIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK09536 159 PVLLLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-219 |
4.67e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.91 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSthlISRKGIGYVPENQGIFHDLTVEE 97
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQRDICMVFQSYALFPHMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFA-----LASGKgEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpimiekl 172
Cdd:PRK11432 98 NVGyglkmLGVPK-EERKQRVKEALELV-DLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD------- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 173 mvAILK--MKEK---------TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK11432 169 --ANLRrsMREKirelqqqfnITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-201 |
7.01e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.45 E-value: 7.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIE-TYLDQFhILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVN-GLSTHlisRKGI 80
Cdd:PRK13540 1 MLDVIELDfDYHDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkDLCTY---QKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEET--FALASGKGeevHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENclYDIHFSPG---AVGITELCRLF-SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447119455 159 EPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDY 201
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADY 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-214 |
7.42e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.67 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNG--LSTHLI--SRKGIGYV---PENQgiFH 91
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-----TVGGmvLSEETVwdVRRQVGMVfqnPDNQ--FV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 DLTVEETFALA-SGKG---EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI 167
Cdd:PRK13635 96 GATVQDDVAFGlENIGvprEEMVERVDQALRQV-GMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447119455 168 MIEKLMVAILKMKEKT--TVLLVEQNFMMASQiGDYFYIMDNGRIVHKG 214
Cdd:PRK13635 175 GRREVLETVRQLKEQKgiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-222 |
7.42e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQG-VSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRiangeiYYDSTQVNGLSTHLIS----RK 78
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP------YQGSLKINGIELRELDpeswRK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 79 GIGYVPENQGIFHDlTVEETFALASGKGEEvhEKID------WMLELFPDLKQFWN----KKSGLLSGGQKQMLAISRAF 148
Cdd:PRK11174 424 HLSWVGQNPQLPHG-TLRDNVLLGNPDASD--EQLQqalenaWVSEFLPLLPQGLDtpigDQAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 149 INSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFmmaSQIGDYFYI--MDNGRIVHKGFMNELRED 222
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQL---EDLAQWDQIwvMQDGQIVQQGDYAELSQA 573
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-228 |
7.56e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.66 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEI----YYDSTQVNGLSTHLISRKGIGYV---PENQ 87
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKEVKRLRKEIGLVfqfPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 88 gIFHDlTVEETFALA----SGKGEEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISrAFINSDG-LLLIDEPSK 162
Cdd:PRK13645 103 -LFQE-TIEKDIAFGpvnlGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALA-GIIAMDGnTLVLDEPTG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 163 GLSPIMIEKLMVAILKM--KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHK 228
Cdd:PRK13645 180 GLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTK 247
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-214 |
9.43e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.38 E-value: 9.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 22 VSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHL---ISRKGIGYV---PENQgIFHDLTV 95
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikPVRKKVGVVfqfPESQ-LFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 E------ETFALASGKGEEVHEKidwMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP--- 166
Cdd:PRK13643 104 KdvafgpQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPkar 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447119455 167 IMIEKLMVAILKMKEktTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK13643 181 IEMMQLFESIHQSGQ--TVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-232 |
2.22e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYVPENQGIFHDLTVEE 97
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFAL-------ASGK-GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLS-PIM 168
Cdd:PRK10575 105 LVAIgrypwhgALGRfGAADREKVEEAISLV-GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQ 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 169 IEKL-MVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREdKETCHKYLGI 232
Cdd:PRK10575 184 VDVLaLVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR-GETLEQIYGI 247
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-214 |
2.42e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 73.68 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS-THLIS-RKGIGYvpenqgIF-H 91
Cdd:PRK11153 17 TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSeKELRKaRRQIGM------IFqH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 -DL----TVEETFALA---SGKG-EEVHEKIDWMLEL--FPDLKQFWNKKsglLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:PRK11153 91 fNLlssrTVFDNVALPlelAGTPkAEIKARVTELLELvgLSDKADRYPAQ---LSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 161 SKGLSPimieKLMVAILKM-KE-----KTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK11153 168 TSALDP----ATTRSILELlKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-214 |
2.43e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.91 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSThliSRKGI 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEETFA----LASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLL 156
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSfglkLAGAKKEEINQRVNQVAEVL-QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 157 IDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRlgRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-214 |
2.47e-15 |
|
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: 72.37 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGL-----STHLISRKGIGYVPENQGIFhDL 93
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGLvpwkrRKKFLRRIGVVFGQKTQLWW-DL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEETFALASG----KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMI 169
Cdd:cd03267 111 PVIDSFYLLAAiydlPPARFKKRLDELSELL-DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447119455 170 EKL--MVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03267 190 ENIrnFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-218 |
2.67e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.21 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 10 ETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS--RKGIGYVPENQ 87
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQDH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 88 GIFHDLTVEETFAL----ASGKGEEVHEKIDWMLE---LFPDLKQFWNKksglLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:PRK10908 89 HLLMDRTVYDNVAIpliiAGASGDDIRRRVSAALDkvgLLDKAKNFPIQ----LSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 161 SKGLSpimiEKLMVAILKMKEK-----TTVLLVEQNFMMASQIGDYFYIMDNGRIvHKGFMNE 218
Cdd:PRK10908 165 TGNLD----DALSEGILRLFEEfnrvgVTVLMATHDIGLISRRSYRMLTLSDGHL-HGGVGGE 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-222 |
5.14e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGY 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEETFALASGKGEEVHEKIDWML-ELFPDLKqfWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPS 161
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLaALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 162 KGLSPIMIEKLMVAILKMKEKTT-VLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELRED 222
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-194 |
6.04e-15 |
|
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: 73.41 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMgfhRIAN--GEIyydstQVNGLSTHLIS----RKGIGYVPENQGIF- 90
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL---RLLSteGEI-----QIDGVSWNSVTlqtwRKAFGVIPQKVFIFs 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 91 ----------HDLTVEETFALAsgkgEEVHEKIdwMLELFPDLKQFWNKKSG-LLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:TIGR01271 1306 gtfrknldpyEQWSDEEIWKVA----EEVGLKS--VIEQFPDKLDFVLVDGGyVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447119455 160 PSKGLSPIMIEKLMVAILKMKEKTTVLLVE---------QNFMM 194
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSEhrveallecQQFLV 1423
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-219 |
6.44e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 71.62 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRI------ANGEIYY---DSTQVNGLSTh 73
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYfgkDIFQIDAIKL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 74 lisRKGIGYVPENQGIFHDLTVEETFALA-SGKGEEVHEKIDWMLE-------LFPDLKQFWNKKSGLLSGGQKQMLAIS 145
Cdd:PRK14246 89 ---RKEVGMVFQQPNPFPHLSIYDNIAYPlKSHGIKEKREIKKIVEeclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 146 RAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-219 |
7.20e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 72.76 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 10 ETYLDQFHILQGV---SLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLST---HLISRKGIGYV 83
Cdd:PRK10070 32 EQILEKTGLSLGVkdaSLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQGIFHDLTVEETFA----LASGKGEEVHEK-IDWMLELfpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAfgmeLAGINAEERREKaLDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 159 EPSKGLSPIMIEKLMVAILKM--KEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-198 |
7.23e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.27 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLisrkgiGY 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEETFA----LASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAfglqLAGVEKMQRLEIAHQMLKKV-GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447119455 159 EPSKGLSPIMIEKLMVAILKMKEKT--TVLL----VEQNFMMASQI 198
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETgkQVLLithdIEEAVFMATEL 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-214 |
7.49e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 11 TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSTHLISRKG-IGYVPENQGI 89
Cdd:PRK15056 15 TWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKNlVAYVPQSEEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 90 FHDLTVEETFALASGK----------GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:PRK15056 90 DWSFPVLVEDVVMMGRyghmgwlrraKKRDRQIVTAALARV-DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 160 PSKGLSpIMIEKLMVAILK--MKEKTTVLLVEQNFMMASQIGDYfYIMDNGRIVHKG 214
Cdd:PRK15056 169 PFTGVD-VKTEARIISLLRelRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASG 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-233 |
1.08e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIeTYLDQfHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqVNGlSTHL---ISRKG 79
Cdd:PRK10771 1 MLKLTDI-TWLYH-HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-----LNG-QDHTttpPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 80 IGYVPENQGIFHDLTVEETFALASGKG----EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLL 155
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLGLNPGlklnAAQREKLHAIARQM-GIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 156 LIDEPSKGLSPIMIEKlMVAILK---MKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKYLGI 232
Cdd:PRK10771 152 LLDEPFSALDPALRQE-MLTLVSqvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGI 230
|
.
gi 447119455 233 S 233
Cdd:PRK10771 231 K 231
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-210 |
2.02e-14 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 71.61 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYVPENQGIFhDLTVEE 97
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH-IGYLPQDVELF-PGTVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFA-----------LASGKGEEVHEkidwMLELFPD-LKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLS 165
Cdd:TIGR01842 411 NIArfgenadpekiIEAAKLAGVHE----LILRLPDgYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447119455 166 PIMIEKLMVAILKMK-EKTTVLLVEQNFMMASQIgDYFYIMDNGRI 210
Cdd:TIGR01842 487 EEGEQALANAIKALKaRGITVVVITHRPSLLGCV-DKILVLQDGRI 531
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-224 |
2.23e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.17 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 14 DQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYV---PENQGIF 90
Cdd:PRK13648 20 DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-RKHIGIVfqnPDNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 91 HDLTVEETFALA--SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIM 168
Cdd:PRK13648 99 SIVKYDVAFGLEnhAVPYDEMHRRVSEALKQV-DMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 169 IEKLMVAILKMKEK--TTVLLVEQNFMMASQiGDYFYIMDNGRIVHKGFMNELREDKE 224
Cdd:PRK13648 178 RQNLLDLVRKVKSEhnITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-186 |
2.41e-14 |
|
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: 68.40 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVN--GLSTHlisRKGIGYVPENQGIFhdltv 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNEL---GDHVGYLPQDDELF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 eetfalaSGKgeeVHEKIdwmlelfpdlkqfwnkksglLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVA 175
Cdd:cd03246 89 -------SGS---IAENI--------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170
....*....|...
gi 447119455 176 I--LKMKEKTTVL 186
Cdd:cd03246 139 IaaLKAAGATRIV 151
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
2.42e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIE-TYLDQ-FHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS-THLisRK 78
Cdd:PRK11160 337 VSLTLNNVSfTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeAAL--RQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 79 GIGYVPENQGIFHDlTVEETFALASGKG-----EEVHEKI--DWMLELFPDLKQfWNKKSG-LLSGGQKQMLAISRAFIN 150
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLLAAPNAsdealIEVLQQVglEKLLEDDKGLNA-WLGEGGrQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 151 SDGLLLIDEPSKGLSPiMIEKLMVAILK--MKEKtTVLLVEQNFMMASQIgDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK11160 493 DAPLLLLDEPTEGLDA-ETERQILELLAehAQNK-TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-188 |
2.57e-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: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGY 82
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDLTVEETFALASGKG-----------EEVHEKIDWM-LELFPDlkqfwnKKSGLLSGGQKQMLAISRAFIN 150
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTkggrldrkaarARIRELSERYgLDVDPD------AKVEDLSVGEQQRVEILKALYR 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 447119455 151 SDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK-TTVLLV 188
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFI 197
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-160 |
2.67e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.03 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNI-ETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSThliSRKG 79
Cdd:PRK11650 1 MAGLKLQAVrKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 80 IGYVPENQGIFHDLTVEETFALA-----SGKgEEVHEKID---WMLELFPDLKqfwnKKSGLLSGGQKQMLAISRAFINS 151
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGlkirgMPK-AEIEERVAeaaRILELEPLLD----RKPRELSGGQRQRVAMGRAIVRE 152
|
....*....
gi 447119455 152 DGLLLIDEP 160
Cdd:PRK11650 153 PAVFLFDEP 161
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-219 |
3.21e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.12 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYV---PENQgiFHDLTV 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK-IGMVfqnPDNQ--FVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 EETFALA-SGKG---EEVHEKIDWMLeLFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEK 171
Cdd:PRK13642 100 EDDVAFGmENQGiprEEMIKRVDEAL-LAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447119455 172 LMVAILKMKEK--TTVLLVEQNFMMASQiGDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK13642 179 IMRVIHEIKEKyqLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-218 |
3.80e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLD-----QFHILQGVSLTVEKGTITVLFGRNGAGKTT-------TLRSVMGFHRIA---NGEIYYDSTQV 67
Cdd:PRK13631 21 ILRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTlvthfngLIKSKYGTIQVGdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 68 NGLSTHLIS-----RKGIGYV---PENQgIFHDlTVEETF-----ALASGKgEEVHEKIDWMLELFPDLKQFWNKKSGLL 134
Cdd:PRK13631 101 TNPYSKKIKnfkelRRRVSMVfqfPEYQ-LFKD-TIEKDImfgpvALGVKK-SEAKKLAKFYLNKMGLDDSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 135 SGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMK-EKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHK 213
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250
....*....|
gi 447119455 214 G-----FMNE 218
Cdd:PRK13631 258 GtpyeiFTDQ 267
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-210 |
4.76e-14 |
|
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: 68.65 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNgLSTHLISRKGIGYVPENQGIF-HDLTVE 96
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFaRSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 97 ETFALASGKGEEVHEKI------DWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIE 170
Cdd:cd03248 108 IAYGLQSCSFECVKEAAqkahahSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447119455 171 KLMVAILKMKEKTTVLLVEQNFMMASQiGDYFYIMDNGRI 210
Cdd:cd03248 188 QVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-173 |
5.05e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 68.29 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISrkGIGYVPENQGIFHDLTVEE 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR--GLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 98 --TFALASGKGEEVHEKIDWMlelfpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLM 173
Cdd:cd03231 93 nlRFWHADHSDEQVEEALARV-----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-173 |
5.38e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 68.15 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLisRKGIGYVPENQGIFHDLTVEE 97
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 --TF--ALASGKGEEVHEKIDWMlelfpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLM 173
Cdd:TIGR01189 93 nlHFwaAIHGGAQRTIEDALAAV-----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-160 |
5.41e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGfhRIA--NGEIYYdSTQVNglsthlisrkgIGYVPENQGIFH-DLT 94
Cdd:COG0488 330 LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG--ELEpdSGTVKL-GETVK-----------IGYFDQHQEELDpDKT 395
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 95 VEETFALASGKGEEVHekIDWMLE--LFPDLKQFwnKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:COG0488 396 VLDELRDGAPGGTEQE--VRGYLGrfLFSGDDAF--KPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-219 |
6.28e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTH-----LISRKGIGYVPENQGIF-- 90
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFnyrdvLEFRRRVGMLFQRPNPFpm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 91 ------------HDLTVEETF-ALASGKGEEVHekidwmleLFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLI 157
Cdd:PRK14271 116 simdnvlagvraHKLVPRKEFrGVAQARLTEVG--------LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 158 DEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-199 |
1.14e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.92 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNI-ETYLD---QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLST----HL 74
Cdd:PRK11629 5 LLQCDNLcKRYQEgsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 75 ISRKgIGYVPENQGIFHDLTVEETFAL----ASGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFIN 150
Cdd:PRK11629 85 RNQK-LGFIYQFHHLLPDFTALENVAMplliGKKKPAEINSRALEMLAAV-GLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447119455 151 SDGLLLIDEPSKGLSPIMIEKL--MVAILKMKEKTTVLLVEQNFMMASQIG 199
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIfqLLGELNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-233 |
2.07e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIE-TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIG 81
Cdd:PRK13644 1 MIRLENVSySYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YV---PENQgiFHDLTVEETFALASGK----GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGL 154
Cdd:PRK13644 81 IVfqnPETQ--FVGRTVEEDLAFGPENlclpPIEIRKRVDRALAEI-GLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 155 LLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETchKYLGIS 233
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL--QTLGLT 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-224 |
2.86e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYV---PENQgiFHDLT 94
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-RKKIGIIfqnPDNQ--FIGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 95 VEE--TFALASGK--GEEVHEKIDwMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI--- 167
Cdd:PRK13632 101 VEDdiAFGLENKKvpPKKMKDIID-DLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKgkr 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 168 MIEKLMVAILKMKEKTTVLLVEQnfMMASQIGDYFYIMDNGRIVHKGFMNELREDKE 224
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHD--MDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-214 |
3.68e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 67.03 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqVNGLSTHLIS-----RKGIGYV---PENQGIf 90
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVY-----VDGLDTSDEEnlwdiRNKAGMVfqnPDNQIV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 91 hDLTVEETFALASG----KGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSP 166
Cdd:PRK13633 100 -ATIVEEDVAFGPEnlgiPPEEIRERVDESLKKV-GMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447119455 167 IMIEKLMVAILKMKEK--TTVLLVeQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK13633 178 SGRREVVNTIKELNKKygITIILI-THYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-214 |
6.13e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.61 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS-RKGIGYV---PENQgIFHDlT 94
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDiRKKVGLVfqyPEYQ-LFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 95 VEETFALA-SGKG---EEVHEKIDWMLELFP-DLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMI 169
Cdd:PRK13637 101 IEKDIAFGpINLGlseEEIENRVKRAMNIVGlDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447119455 170 EKLMVAILKMKE--KTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK13637 181 DEILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-182 |
6.40e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.16 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGF--HRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPENQGIFHDLTVEETFALA---SGKG------EEVHEKIDWMLELFPDLKQFwNKKSGLLSGGQKQMLAISRAFINS 151
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGneiTLPGgrmaynAMYLRAKNLLRELQLDADNV-TRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190
....*....|....*....|....*....|.
gi 447119455 152 DGLLLIDEPSKGLSPIMIEKLMVAILKMKEK 182
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAH 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-214 |
6.45e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.31 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTH---LISRKGIGYV---PENQgIFhD 92
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdiKQIRKKVGLVfqfPESQ-LF-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 LTVEETFALAS---GKGEEVHEKI-DWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIM 168
Cdd:PRK13649 101 ETVLKDVAFGPqnfGVSQEEAEALaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447119455 169 IEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK13649 181 RKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-211 |
1.33e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.18 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIG 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFHDLTVEETFALA----SGKGEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFI------NS 151
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAMGraphGLSRAEDDALVAAALAQV-DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 152 DGLLLIDEPSKGLSPIMIEKLMvAILK---MKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIV 211
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVL-RLARqlaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-223 |
1.40e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.20 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSthLIS-RKGIGYVPENQGIFHDlTVEE 97
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASlRNQVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFALASGKG---EEVHE--KIDWMLELFPDLKQFWNKKSG----LLSGGQKQMLAISRAFINSDGLLLIDEPSKGL---S 165
Cdd:PRK11176 436 NIAYARTEQysrEQIEEaaRMAYAMDFINKMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSALdteS 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 166 PIMIEKlmvAILKMKEKTTVLLVEQNFmmaSQI--GDYFYIMDNGRIVHKGFMNELREDK 223
Cdd:PRK11176 516 ERAIQA---ALDELQKNRTSLVIAHRL---STIekADEILVVEDGEIVERGTHAELLAQN 569
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-188 |
1.56e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.79 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstqvnglstHLISRKGIGYVPEnQGIFHD---LTV 95
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQ-RSEVPDslpLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 EETFALasGK----------GEEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLS 165
Cdd:NF040873 75 RDLVAM--GRwarrglwrrlTRDDRAAVDDALERV-GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180
....*....|....*....|....
gi 447119455 166 PIMIEKLMVAILKM-KEKTTVLLV 188
Cdd:NF040873 152 AESRERIIALLAEEhARGATVVVV 175
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-230 |
1.59e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.28 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGI----------GYVPENq 87
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVAlvgqepvlfsGSVREN- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 88 gIFHDLT-VEETFALASGKGEEVHekiDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSp 166
Cdd:TIGR00958 575 -IAYGLTdTPDEEIMAAAKAANAH---DFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 167 IMIEKLMVAILKMKEKtTVLLVEQNFMMASQiGDYFYIMDNGRIVHKGFMNELREDkETCHKYL 230
Cdd:TIGR00958 650 AECEQLLQESRSRASR-TVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED-QGCYKHL 710
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-210 |
1.97e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.14 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQ---FHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISR 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 78 KgIGYV---PENQgiFHDLTVEETFALA-SGKG---EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFIN 150
Cdd:PRK13650 82 K-IGMVfqnPDNQ--FVGATVEDDVAFGlENKGiphEEMKERVNEALELV-GMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 151 SDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASqIGDYFYIMDNGRI 210
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-209 |
2.10e-12 |
|
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: 62.47 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstqvnglstHLISRKGIGYV 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------TWGSTVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PEnqgifhdltveetfalasgkgeevhekidwmlelfpdlkqfwnkksglLSGGQKQMLAISRAFINSDGLLLIDEPSKG 163
Cdd:cd03221 69 EQ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447119455 164 LSPIMIEKLMVAILkmKEKTTVLLVEQNFMMASQIGDYFYIMDNGR 209
Cdd:cd03221 101 LDLESIEALEEALK--EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-209 |
2.62e-12 |
|
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: 63.64 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGlsthlisrkGIGYVPENQGIFHDlTVEE 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-----SVPG---------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 --TFalasgkGEEVHEkiDWMLE------LFPDLKQFwnkKSGL----------LSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:cd03250 85 niLF------GKPFDE--ERYEKvikacaLEPDLEIL---PDGDlteigekginLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 160 PskgLSPI-------MIEKLmvaILK-MKEKTTVLLVEQNFMMASQIgDYFYIMDNGR 209
Cdd:cd03250 154 P---LSAVdahvgrhIFENC---ILGlLLNNKTRILVTHQLQLLPHA-DQIVVLDNGR 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-187 |
2.63e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 G-------YVPEnqgifhdLTVEETFAL------------------ASGKGEEVHEKIDwmlelfPDLkqfwnkKSGLLS 135
Cdd:PRK11288 82 AiiyqelhLVPE-------MTVAENLYLgqlphkggivnrrllnyeAREQLEHLGVDID------PDT------PLKYLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447119455 136 GGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLL 187
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVIL 194
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-214 |
5.15e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIE-TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLStHLISRKGIGY 82
Cdd:PRK10790 341 IDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQGIFHDltveeTFALASGKGEEVHEKIDW-MLEL---------FPD-LKQFWNKKSGLLSGGQKQMLAISRAFINS 151
Cdd:PRK10790 420 VQQDPVVLAD-----TFLANVTLGRDISEEQVWqALETvqlaelarsLPDgLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 152 DGLLLIDEPSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNFmmaSQI--GDYFYIMDNGRIVHKG 214
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRL---STIveADTILVLHRGQAVEQG 556
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-214 |
5.98e-12 |
|
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: 62.94 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 16 FHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSTHLIsrkGIGYvpenqGIFHDLTV 95
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----TVRGRVSSLL---GLGG-----GFNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 EETF---ALASG-KGEEVHEKIDWMLElFPDLKQFWNKKSGLLSGGQKQML--AISRAFiNSDgLLLIDEpskglspiMI 169
Cdd:cd03220 102 RENIylnGRLLGlSRKEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLafAIATAL-EPD-ILLIDE--------VL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447119455 170 --------EKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:cd03220 171 avgdaafqEKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-214 |
6.44e-12 |
|
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: 64.32 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQ----FHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGF----HRIANGEIYYDSTQVNGLST 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 73 HLISR---KGIGYvpenqgIFHD--------LTVE----ETFALASG-KGEEVHEKIDWMLEL--FPD----LKQFWNKk 130
Cdd:COG4172 84 RELRRirgNRIAM------IFQEpmtslnplHTIGkqiaEVLRLHRGlSGAAARARALELLERvgIPDperrLDAYPHQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 131 sglLSGGQKQ--MLAIsrAFINSDGLLLIDEPSKGL-----SPIMieKLMvAILKMKEKTTVLLVEQNFMMASQIGDYFY 203
Cdd:COG4172 157 ---LSGGQRQrvMIAM--ALANEPDLLIADEPTTALdvtvqAQIL--DLL-KDLQRELGMALLLITHDLGVVRRFADRVA 228
|
250
....*....|.
gi 447119455 204 IMDNGRIVHKG 214
Cdd:COG4172 229 VMRQGEIVEQG 239
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-206 |
6.59e-12 |
|
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: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTIT-----VLFGRNGAGKTTTLRSVMGFHRIANGEIyydstqvnglsthLISRKGIGYVPENQGIFHDL 93
Cdd:cd03237 10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI-------------EIELDTVSYKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEetfALASGKGEEVHEKIDWMLELFPDLK--QFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpiMIEK 171
Cdd:cd03237 77 TVR---DLLSSITKDFYTHPYFKTEIAKPLQieQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQR 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 447119455 172 LMVA-ILK---MKEKTTVLLVEQNFMMASQIGDYFYIMD 206
Cdd:cd03237 152 LMASkVIRrfaENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-160 |
9.18e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.45 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDS--TQVN--GLSTHLI---SRKGIGYVpeNQgiFh 91
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdgGWVDlaQASPREIlalRRRTIGYV--SQ--F- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 dLTV------EETFA---LASGKGEEV-HEKIDWMLELFpDLKQ-FWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:COG4778 102 -LRViprvsaLDVVAeplLERGVDREEaRARARELLARL-NLPErLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-214 |
1.04e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.89 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 13 LDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMG----FHRIaNGEIYYDStqVNGLSTHLISRKGIGYVPENQG 88
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSV-EGDIHYNG--IPYKEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 89 IFHDLTVEET--FALaSGKGEEVHEKIdwmlelfpdlkqfwnkksgllSGGQKQMLAISRAFINSDGLLLIDEPSKGL-S 165
Cdd:cd03233 94 HFPTLTVRETldFAL-RCKGNEFVRGI---------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLdS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 166 PIMIE-----KLMVAILKMkekTTVLLVEQnfmmASQ----IGDYFYIMDNGRIVHKG 214
Cdd:cd03233 152 STALEilkciRTMADVLKT---TTFVSLYQ----ASDeiydLFDKVLVLYEGRQIYYG 202
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-164 |
1.41e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDStqvnGLSthlisrkgIGY 82
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLR--------IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPenQGIFHD----LTVEETFALASGkgeeVHEKidwmlELFPDLK-----QFWNKKSGLLSGGQKQMLAISRAFINSDG 153
Cdd:PRK09544 72 VP--QKLYLDttlpLTVNRFLRLRPG----TKKE-----DILPALKrvqagHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170
....*....|.
gi 447119455 154 LLLIDEPSKGL 164
Cdd:PRK09544 141 LLVLDEPTQGV 151
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-214 |
1.55e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.14 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMgfHRIANGEIYYDSTQVNGlstHLISRKGI----GYVPENQGIFHD 92
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA--FRSPKGVKGSGSVLLNG---MPIDAKEMraisAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 LTVEETFAL-----------ASGKGEEVHEKIDwMLELFP--DLK-QFWNKKSGLlSGGQKQMLAISRAFINSDGLLLID 158
Cdd:TIGR00955 114 LTVREHLMFqahlrmprrvtKKEKRERVDEVLQ-ALGLRKcaNTRiGVPGRVKGL-SGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 159 EPSKGLSPIMIEKLmVAILK---MKEKTTVLLVEQNfmmASQIGDYF---YIMDNGRIVHKG 214
Cdd:TIGR00955 192 EPTSGLDSFMAYSV-VQVLKglaQKGKTIICTIHQP---SSELFELFdkiILMAEGRVAYLG 249
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-229 |
1.63e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.54 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEI----YYDSTQVNGLSTHLIsRKGIGYV---PENQgIFH 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagYHITPETGNKNLKKL-RKKVSLVfqfPEAQ-LFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 DLTVEE------TFALASGKGEEvhEKIDWMLELFPDlKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLS 165
Cdd:PRK13641 101 NTVLKDvefgpkNFGFSEDEAKE--KALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 166 PiMIEKLMVAILK--MKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKY 229
Cdd:PRK13641 178 P-EGRKEMMQLFKdyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKH 242
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-221 |
1.73e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.41 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLR-------------SVMGF----HRIANgeiyydstqvnglsthlisRKGIG 81
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgilvptsgevRVLGYvpfkRRKEF-------------------ARRIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YV--PENQGIFhDLTVEETFALAS---GKGEEVHEK-IDWMLELFpDLKQFWNKKSGLLSGGQKqMLA-ISRAFINSDGL 154
Cdd:COG4586 99 VVfgQRSQLWW-DLPAIDSFRLLKaiyRIPDAEYKKrLDELVELL-DLGELLDTPVRQLSLGQR-MRCeLAAALLHRPKI 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 155 LLIDEPSKGLSPIMIEKLMVAILKM--KEKTTVLL-------VEQnfmMASQIgdyfYIMDNGRIVHKGFMNELRE 221
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLtshdmddIEA---LCDRV----IVIDHGRIIYDGSLEELKE 244
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-164 |
1.80e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDStqVNGLSTHLISRkgIGYVPENQGIFHDLTVEE 97
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG--GDIDDPDVAEA--CHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 98 --TF--ALASGKGEEVHEKIDWMlelfpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:PRK13539 93 nlEFwaAFLGGEELDIAAALEAV-----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-212 |
2.99e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.43 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIE-TYL---DQFHILQGVSLTVEKGTITVLFGRNGAGKTTtLRSVMGFHRIANGEIYY----DSTQVNGLSTH 73
Cdd:PRK10535 3 ALLELKDIRrSYPsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKST-LMNILGCLDKPTSGTYRvagqDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 74 LISRKGIGYVPENQGIFHDLTVE---ETFALASGKGEEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFIN 150
Cdd:PRK10535 82 QLRREHFGFIFQRYHLLSHLTAAqnvEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 151 SDGLLLIDEPSKGLSPIMIEKLMvAILK-MKEKT-TVLLVEQNFMMASQIGDYFYIMDnGRIVH 212
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVM-AILHqLRDRGhTVIIVTHDPQVAAQAERVIEIRD-GEIVR 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-210 |
3.30e-11 |
|
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: 61.41 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSvmgFHRIAN--GEIyydstQVNGLSTHLIS----RKGIGYVPENQGIFH 91
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSA---FLRLLNteGDI-----QIDGVSWNSVPlqkwRKAFGVIPQKVFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 -----------DLTVEETFALAsgkgEEVHEKIdwMLELFPDLKQFWNKKSG-LLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:cd03289 91 gtfrknldpygKWSDEEIWKVA----EEVGLKS--VIEQFPGQLDFVLVDGGcVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447119455 160 PSKGLSPIMIEKLMVAILKMKEKTTVLLVEQNF--MMASQigdYFYIMDNGRI 210
Cdd:cd03289 165 PSAHLDPITYQVIRKTLKQAFADCTVILSEHRIeaMLECQ---RFLVIEENKV 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-160 |
3.56e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRsvmgfhrIANGEIYYDSTQVnglsthlISRKG--IGYVPENQGIFHDLTV 95
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLK-------ILAGELEPDSGEV-------SIPKGlrIGYLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 EET--------------FALASGKGE----------EVHEKID----WMLE---------L-FPDlkQFWNKKSGLLSGG 137
Cdd:COG0488 79 LDTvldgdaelraleaeLEELEAKLAepdedlerlaELQEEFEalggWEAEaraeeilsgLgFPE--EDLDRPVSELSGG 156
|
170 180
....*....|....*....|....
gi 447119455 138 QKQMLAISRA-FINSDgLLLIDEP 160
Cdd:COG0488 157 WRRRVALARAlLSEPD-LLLLDEP 179
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-160 |
5.45e-11 |
|
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: 61.62 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 14 DQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRiANGEIYYDSTQVNGLSTH--LISRKGIgyvpenQGIFH 91
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRalRPLRRRM------QVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 D--------LTVEETFA--LA----SGKGEEVHEKIDWMLE---LFPDLKQ-----FwnkksgllSGGQKQMLAISRAFI 149
Cdd:COG4172 370 DpfgslsprMTVGQIIAegLRvhgpGLSAAERRARVAEALEevgLDPAARHrypheF--------SGGQRQRIAIARALI 441
|
170
....*....|.
gi 447119455 150 NSDGLLLIDEP 160
Cdd:COG4172 442 LEPKLLVLDEP 452
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-165 |
6.41e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.50 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGV----SLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGlsthlISRKGIGYVPENQGIF 90
Cdd:PRK13541 8 QFNIEQKNlfdlSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-----IAKPYCTYIGHNLGLK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 91 HDLTVEETFALASGKGEEVhEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLS 165
Cdd:PRK13541 83 LEMTVFENLKFWSEIYNSA-ETLYAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-211 |
7.12e-11 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 59.81 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVP-----------EN 86
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-RSRISIIPqdpvlfsgtirSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 87 QGIFHDLTVEETF-ALasgkgEEVHekidwmlelfpdLKQFWNKKSGLL-----------SGGQKQMLAISRAFINSDGL 154
Cdd:cd03244 98 LDPFGEYSDEELWqAL-----ERVG------------LKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 155 LLIDEPSKGLSPIMiEKLMVAILKMKEK-TTVLLVEQ--NFMMASqigDYFYIMDNGRIV 211
Cdd:cd03244 161 LVLDEATASVDPET-DALIQKTIREAFKdCTVLTIAHrlDTIIDS---DRILVLDKGRVV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-219 |
7.95e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.13 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSthLIS-RKGIGYVPENQGIFhDLTVEE 97
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT--RASlRRNIAVVFQDAGLF-NRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TfaLASGK----GEEVHEKI------DWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI 167
Cdd:PRK13657 428 N--IRVGRpdatDEEMRAAAeraqahDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 168 MIEKLMVAILK-MKEKTTvllveqnFMMA---SQI--GDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK13657 506 TEAKVKAALDElMKGRTT-------FIIAhrlSTVrnADRILVFDNGRVVESGSFDEL 556
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-182 |
1.05e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGF--HRIANGEIYYDSTQVNGLSTHLISRK 78
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 79 GIGYVPENQGIFHDLTVEETFALasgkGEEVHEK--IDWML------ELFPDLKQFWN--KKSGLLSGGQKQMLAISRAf 148
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFL----GNEITPGgiMDYDAmylraqKLLAQLKLDINpaTPVGNLGLGQQQLVEIAKA- 157
|
170 180 190
....*....|....*....|....*....|....*
gi 447119455 149 INSDGLLLI-DEPSKGLSPIMIEKLMVAILKMKEK 182
Cdd:PRK13549 158 LNKQARLLIlDEPTASLTESETAVLLDIIRDLKAH 192
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-208 |
1.67e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 58.88 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS---THLISRKGIGYVPENQGIFhDLTV 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfeaTRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 96 EETFALASGKGEEVHEKIDWMLELFPDLK------QFWNKKSGL-LSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIM 168
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDllpfgdQTEIGERGInLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447119455 169 IEKLMVA-ILKM--KEKTTVLLVEQNFMMASQiGDYFYIMDNG 208
Cdd:cd03290 176 SDHLMQEgILKFlqDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-226 |
1.81e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 14 DQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVM----GFHRIANGEIYYDstqvnGLSTHLISRKGIG---YVPEN 86
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYD-----GITPEEIKKHYRGdvvYNAET 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 87 QGIFHDLTVEETFALAS--------GKG---EEVHEKI-DWMLELFpDLKQFWNKKSGL-----LSGGQKQMLAISRAFI 149
Cdd:TIGR00956 147 DVHFPHLTVGETLDFAArcktpqnrPDGvsrEEYAKHIaDVYMATY-GLSHTRNTKVGNdfvrgVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 150 NSDGLLLIDEPSKGL-SPIMIE-----KLMVAILKMKEKTTVLLVEQNfmmASQIGDYFYIMDNGRIVHKGFMNELREDK 223
Cdd:TIGR00956 226 GGAKIQCWDNATRGLdSATALEfiralKTSANILDTTPLVAIYQCSQD---AYELFDKVIVLYEGYQIYFGPADKAKQYF 302
|
...
gi 447119455 224 ETC 226
Cdd:TIGR00956 303 EKM 305
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-220 |
1.86e-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: 60.41 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 26 VEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGE--IYYDSTQVNGLSTHlisrKGIGYVPENQGIFHDLTVEETFAL-A 102
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDatVAGKSILTNISDVH----QNMGYCPQFDAIDDLLTGREHLYLyA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 103 SGKG---EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI---MIEKLMVAI 176
Cdd:TIGR01257 2038 RLRGvpaEEIEKVANWSIQSL-GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQarrMLWNTIVSI 2116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447119455 177 LkmKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELR 220
Cdd:TIGR01257 2117 I--REGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK 2158
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-219 |
1.92e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKgIGYVPENQGIFHDLTVEE 97
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFAlasgKGEEVHEKI--DWMLE---------LFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLS- 165
Cdd:PRK10253 101 LVA----RGRYPHQPLftRWRKEdeeavtkamQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDi 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 166 PIMIEKL-MVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK10253 177 SHQIDLLeLLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-178 |
1.96e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 14 DQFHILQGVSLTVEKGTITVLFGRNGAGKTTT----LRSVMgfhriANGEIYYDstqvnGLSTHLISRKG-IGYVPENQG 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFD-----GQPLHNLNRRQlLPVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 89 IFHD--------LTVEETFAlasgKGEEVHEK-----------IDWMLE--LFPDLKQfwnKKSGLLSGGQKQMLAISRA 147
Cdd:PRK15134 367 VFQDpnsslnprLNVLQIIE----EGLRVHQPtlsaaqreqqvIAVMEEvgLDPETRH---RYPAEFSGGQRQRIAIARA 439
|
170 180 190
....*....|....*....|....*....|.
gi 447119455 148 FINSDGLLLIDEPSKGLSPiMIEKLMVAILK 178
Cdd:PRK15134 440 LILKPSLIILDEPTSSLDK-TVQAQILALLK 469
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-219 |
4.07e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.06 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqVNGLSTHLIS------- 76
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIV-----VNGQTINLVRdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 ----------RKGIGYVPENQGIFHDLTVEETF------ALASGKGEEVHEKIDWMLELFPDLKQfWNKKSGLLSGGQKQ 140
Cdd:PRK10619 81 vadknqlrllRTRLTMVFQHFNLWSHMTVLENVmeapiqVLGLSKQEARERAVKYLAKVGIDERA-QGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 141 MLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNEL 219
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-211 |
4.34e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.16 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIE-TY----LDQFH----ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS 71
Cdd:PRK10419 1 MTLLNVSGLShHYahggLSGKHqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 72 THLIS--RKGIgyvpenQGIFHD--------LTVEETFA-----LASGKGEEVHEKIDWML---ELFPDLKQfwnKKSGL 133
Cdd:PRK10419 81 RAQRKafRRDI------QMVFQDsisavnprKTVREIIReplrhLLSLDKAERLARASEMLravDLDDSVLD---KRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 134 LSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpIMIEKLMVAILK-MKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRI 210
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLD-LVLQAGVIRLLKkLQQQfgTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
.
gi 447119455 211 V 211
Cdd:PRK10419 231 V 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-160 |
5.52e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.35 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 31 ITVLFGRNGAGKTTTLRSVMGFH-----RIA-NGEIYYDSTQVNGLSTHlisRKGIGYVPENQGIFHDLTVEETfaLASG 104
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTrpqkgRIVlNGRVLFDAEKGICLPPE---KRRIGYVFQDARLFPHYKVRGN--LRYG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 105 KGEEVHEKIDWMLELF---PDLKQFwnkkSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:PRK11144 101 MAKSMVAQFDKIVALLgiePLLDRY----PGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-166 |
7.52e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGF-----HRIANGEIYYDSTQVNGLSTHLI-- 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGSHIELLGRTVQREGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 76 SRKGIGYVPENQGIFHDLTVEETFAL-ASGKGEEVHEKIDWMLelfPDLKQ-------------FWNKKSGLLSGGQKQM 141
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIgALGSTPFWRTCFSWFT---REQKQralqaltrvgmvhFAHQRVSTLSGGQQQR 160
|
170 180
....*....|....*....|....*
gi 447119455 142 LAISRAFINSDGLLLIDEPSKGLSP 166
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDP 185
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-229 |
1.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSTHLIS--------RKGIGYV--- 83
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV-----TVDDITITHKTkdkyirpvRKRIGMVfqf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQgIFHDLTVEETFALASGKGEEVHEKIDWMLELFPDL---KQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:PRK13646 94 PESQ-LFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLgfsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119455 161 SKGLSPIMIEKLMVAI--LKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKETCHKY 229
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADW 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-224 |
1.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.95 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNG--LSTHLIS-RKGIGYV---PENQgIFHD 92
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkKNKKLKPlRKKVGIVfqfPEHQ-LFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 lTVEETFALA----SGKGEEVHEKIDWMLELF---PDLKQfwnkKSGL-LSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:PRK13634 102 -TVEKDICFGpmnfGVSEEDAKQKAREMIELVglpEELLA----RSPFeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119455 165 SPI----MIEklMVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELREDKE 224
Cdd:PRK13634 177 DPKgrkeMME--MFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
11-224 |
1.28e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.73 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 11 TYLD-QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGF---HRIANGEIYYDSTQVNGLSTHLIsRKGIGYV--- 83
Cdd:PRK13640 14 TYPDsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDI-REKVGIVfqn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 84 PENQgiFHDLTVEETFALA-SGKGEEVHEKIDWMLELFPD--LKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEP 160
Cdd:PRK13640 93 PDNQ--FVGATVGDDVAFGlENRAVPRPEMIKIVRDVLADvgMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 161 SKGLSPIMIEKLMVAILKMKEKT--TVLLVEQNFMMASQiGDYFYIMDNGRIVHKGFMNELREDKE 224
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-182 |
1.49e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYVPENQGIFHDLTVEET 98
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 99 FALAS--GKGEEVHEKidwmlELFPDLKQFW---------NKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI 167
Cdd:PRK10982 94 MWLGRypTKGMFVDQD-----KMYRDTKAIFdeldididpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170
....*....|....*
gi 447119455 168 MIEKLMVAILKMKEK 182
Cdd:PRK10982 169 EVNHLFTIIRKLKER 183
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-224 |
1.77e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYydstqvnglsthliSRKGIGYVPENQGIFhDLTVEE 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFALASGKGEEVHEKIDWMLELFPDLKQFwnkKSGL----------LSGGQKQMLAISRA-FINSDGLLLiDEPSKGLSP 166
Cdd:PTZ00243 740 NILFFDEEDAARLADAVRVSQLEADLAQL---GGGLeteigekgvnLSGGQKARVSLARAvYANRDVYLL-DDPLSALDA 815
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 167 IMIEKLMVAIL--KMKEKTTVLLVEQNFMMAsqIGDYFYIMDNGRIVHKG----FMN---------ELREDKE 224
Cdd:PTZ00243 816 HVGERVVEECFlgALAGKTRVLATHQVHVVP--RADYVVALGDGRVEFSGssadFMRtslyatlaaELKENKD 886
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-211 |
2.06e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.86 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 11 TYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSTHLIsrkGIGyvpenqGIF 90
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-----EVNGRVSALL---ELG------AGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 91 H-DLTVEE---TFALASG-KGEEVHEKIDWMLElFPDLKQFWNKKSGLLSGGQKQMLAISRA-FINSDgLLLIDEpskGL 164
Cdd:COG1134 100 HpELTGREniyLNGRLLGlSRKEIDEKFDEIVE-FAELGDFIDQPVKTYSSGMRARLAFAVAtAVDPD-ILLVDE---VL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447119455 165 S---PIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQIGDYFYIMDNGRIV 211
Cdd:COG1134 175 AvgdAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-197 |
2.20e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIY---YDSTQVNGLSTHLISRKGIGYVPENQGIFH 91
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgQPLHQMDEEARAKLRAKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 DLTVEETFAL-ASGKGEEVHEKIDWMLELFPD--LKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIM 168
Cdd:PRK10584 102 TLNALENVELpALLRGESSRQSRNGAKALLEQlgLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190
....*....|....*....|....*....|.
gi 447119455 169 IEKLMVAILKMKEK--TTVLLVEQNFMMASQ 197
Cdd:PRK10584 182 GDKIADLLFSLNREhgTTLILVTHDLQLAAR 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-164 |
3.12e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 55.13 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTH---LISRKGIGYVPENqgiFH-- 91
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDaraRLRARHVGFVFQS---FQll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 92 -DLTVEETFALAsgkgeevhekidwmLELF--PDLKQF---WNKKSGL----------LSGGQKQMLAISRAFINSDGLL 155
Cdd:COG4181 103 pTLTALENVMLP--------------LELAgrRDARARaraLLERVGLghrldhypaqLSGGEQQRVALARAFATEPAIL 168
|
....*....
gi 447119455 156 LIDEPSKGL 164
Cdd:COG4181 169 FADEPTGNL 177
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-211 |
3.13e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIeTYLDQFHI--LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:COG3845 257 VLEVENL-SVRDDRGVpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYVPEN---QGIFHDLTVEETFALASGKGEEVHEK--IDW---------MLELF----PDLKQfwnkKSGLLSGG--QKQ 140
Cdd:COG3845 336 AYIPEDrlgRGLVPDMSVAENLILGRYRRPPFSRGgfLDRkairafaeeLIEEFdvrtPGPDT----PARSLSGGnqQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 141 MLAisRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKMKEK-TTVLLVeqnfmmaS-------QIGDYFYIMDNGRIV 211
Cdd:COG3845 412 ILA--RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgAAVLLI-------SedldeilALSDRIAVMYEGRIV 481
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-210 |
3.25e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.45 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS--THL------- 74
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARedTRLmfqdarl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 75 ------ISRKGIGYvpenQGIFHDLTVE--ETFALASGKGEevhekidwmlelfpdlkqfWnkkSGLLSGGQKQMLAISR 146
Cdd:PRK11247 93 lpwkkvIDNVGLGL----KGQWRDAALQalAAVGLADRANE-------------------W---PAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 147 AFINSDGLLLIDEP---SKGLSPIMIEKLMVAiLKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRI 210
Cdd:PRK11247 147 ALIHRPGLLLLDEPlgaLDALTRIEMQDLIES-LWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-214 |
3.62e-09 |
|
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: 56.35 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 21 GVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYY-------DSTQVnGLSTHLISRKGIGYVPENQGIFHDL 93
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvDMTKP-GPDGRGRAKRYIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEETFALASG--------KGEEVH---------EKIDWMLELFPDLkqfwnkksglLSGGQKQMLAISRAFINSDGLLL 156
Cdd:TIGR03269 381 TVLDNLTEAIGlelpdelaRMKAVItlkmvgfdeEKAEEILDKYPDE----------LSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 157 IDEPSKGLSPIMIEKLMVAILKMKEK--TTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-214 |
5.05e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.03 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGF--HRIANGEIYYDSTQVNGLSTHLISRKGI 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 ----GYVPENQGIfhdlTVEETFALA-------SGKGE----EVHEKIDWMLELFpDLKQFW---NKKSGlLSGGQKQML 142
Cdd:CHL00131 87 flafQYPIEIPGV----SNADFLRLAynskrkfQGLPEldplEFLEIINEKLKLV-GMDPSFlsrNVNEG-FSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 143 AISRAFINSDGLLLIDEPSKGLSpimIEKLM-----VAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLD---IDALKiiaegINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-230 |
1.23e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGfhRIANGEiyydstqvnglSTHLISRKGIGYVPENQGIFhDLTVEET 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--ELSHAE-----------TSSVVIRGSVAYVPQVSWIF-NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 99 FALASG-KGEEVHEKIDWM-----LELFP--DLKQFWNKKSGLlSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIE 170
Cdd:PLN03232 699 ILFGSDfESERYWRAIDVTalqhdLDLLPgrDLTEIGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 171 KLMVAILK--MKEKTTVLLVEQNFMMAsqIGDYFYIMDNGRIVHKGFMNELREDKETCHKYL 230
Cdd:PLN03232 778 QVFDSCMKdeLKGKTRVLVTNQLHFLP--LMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-211 |
1.88e-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: 52.80 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFhDLTVEE 97
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL-RSSLTIIPQDPTLF-SGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFALASGKGEEvhekidwmlELFPDLKQfwnKKSGL-LSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAI 176
Cdd:cd03369 101 NLDPFDEYSDE---------EIYGALRV---SEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 447119455 177 LKMKEKTTVLLVEQNFmmaSQIGDYFYI--MDNGRIV 211
Cdd:cd03369 169 REEFTNSTILTIAHRL---RTIIDYDKIlvMDAGEVK 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-212 |
1.91e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 22 VSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYVPENQ---GIFHD------ 92
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRqssGLYLDaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 ---LTVEE-TFALASGKGEEVHEKIDWMLEL-FPDLKQfwnkKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGL--- 164
Cdd:PRK15439 362 vcaLTHNRrGFWIKPARENAVLERYRRALNIkFNHAEQ----AARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVdvs 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447119455 165 SPIMIEKLMVAIlkMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVH 212
Cdd:PRK15439 438 ARNDIYQLIRSI--AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-210 |
2.10e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYldQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGY 82
Cdd:PRK09700 265 VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQ---GIFHDLTVEETFALA--------SGKGEEVHEKIDWML-----ELFPDLKQFWNKKSGLLSGGQKQMLAISR 146
Cdd:PRK09700 343 ITESRrdnGFFPNFSIAQNMAISrslkdggyKGAMGLFHEVDEQRTaenqrELLALKCHSVNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 147 AFINSDGLLLIDEPSKGL---SPIMIEKLMVAIlkMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRI 210
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIdvgAKAEIYKVMRQL--ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
107-220 |
5.39e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 107 EEVHEKIDWMLELFpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILKM-KEKTTV 185
Cdd:NF000106 119 KDARARADELLERF-SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATV 197
|
90 100 110
....*....|....*....|....*....|....*
gi 447119455 186 LLVEQNFMMASQIGDYFYIMDNGRIVHKGFMNELR 220
Cdd:NF000106 198 LLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-181 |
6.26e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIG 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFHDLTVEETFALasgkGEEVHEK---IDW--MLELFPDLKQFWN------KKSGLLSGGQKQMLAISRAFIN 150
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFL----GREFVNRfgrIDWkkMYAEADKLLARLNlrfssdKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190
....*....|....*....|....*....|.
gi 447119455 151 SDGLLLIDEPSKGLSPIMIEKLMVAILKMKE 181
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKS 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-210 |
6.34e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.52 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETY-LDQFHI--LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIA-NGEIYYDSTQVNGLSTHLISRK 78
Cdd:TIGR02633 257 ILEARNLTCWdVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 79 GIGYVPEN---QGIFHDLTVEETFALASGKGEEVHEKIDWMLEL---FPDLKQFWNKKS------GLLSGGQKQMLAISR 146
Cdd:TIGR02633 337 GIAMVPEDrkrHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELqiiGSAIQRLKVKTAspflpiGRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 147 AFINSDGLLLIDEPSKGL---SPIMIEKLMVAIlkMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRI 210
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVdvgAKYEIYKLINQL--AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-219 |
8.18e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGfhriangeiyydstQVNGLSTHLISRKGIGYVPENQGIFHDlTVEET 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEGHVHMKGSVAYVPQQAWIQND-SLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 99 FALASGKGEEVHEKIDWMLELFPDLKQF-------WNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPskgLSPI---- 167
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALLPDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDP---LSAVdahv 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 168 ---MIEKLMVAILKMKEKTTVlLVEQNFMMASQIgDYFYIMDNGRIVHKGFMNEL 219
Cdd:TIGR00957 796 gkhIFEHVIGPEGVLKNKTRI-LVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-166 |
2.28e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstQVNGLSthlISRKG--------IGYVPenQGI- 89
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-----EVLGGD---MADARhrravcprIAYMP--QGLg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 90 ---FHDLTVEET---FALASGKG-EEVHEKIDWMLE---LFPdlkqFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:NF033858 87 knlYPTLSVFENldfFGRLFGQDaAERRRRIDELLRatgLAP----FADRPAGKLSGGMKQKLGLCCALIHDPDLLILDE 162
|
....*..
gi 447119455 160 PSKGLSP 166
Cdd:NF033858 163 PTTGVDP 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-219 |
3.20e-07 |
|
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: 50.71 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTlrsVMGFHRI---ANGEIYYDSTQVNGLSTHLIsRKGIGYVPENQGIFHDLT 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGLNIAKIGLHDL-RFKITIIPQDPVLFSGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 95 VEETFALASGKGEEVHekidWMLEL---------FPDLKQFWNKKSGL-LSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:TIGR00957 1377 RMNLDPFSQYSDEEVW----WALELahlktfvsaLPDKLDHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119455 165 SpIMIEKLMVAILKMK-EKTTVLLVEQNFmmaSQIGDY--FYIMDNGRIVHKGFMNEL 219
Cdd:TIGR00957 1453 D-LETDNLIQSTIRTQfEDCTVLTIAHRL---NTIMDYtrVIVLDKGEVAEFGAPSNL 1506
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-231 |
3.81e-07 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 50.19 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTT---TLRSVMGFHRIAnGEIYYdstqvnglstHLISRKGI 80
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVlmhVLRGMDQYEPTS-GRIIY----------HVALCEKC 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 81 GYV--PENQG-----------------------IFHDLT------VEETFALASGK-------------GEEVHEKIDWM 116
Cdd:TIGR03269 70 GYVerPSKVGepcpvcggtlepeevdfwnlsdkLRRRIRkriaimLQRTFALYGDDtvldnvlealeeiGYEGKEAVGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 117 LELFpDLKQFWNKKSGL---LSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKLMVAILK-MKEKTTVLLVEQNF 192
Cdd:TIGR03269 150 VDLI-EMVQLSHRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHW 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447119455 193 -MMASQIGDYFYIMDNGRIVHKG--------FMNELREDKETCHKYLG 231
Cdd:TIGR03269 229 pEVIEDLSDKAIWLENGEIKEEGtpdevvavFMEGVSEVEKECEVEVG 276
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-160 |
7.95e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.88 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLDQfHIL-QGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQvnglsthlISRKG-- 79
Cdd:PRK13538 1 MLEARNLACERDE-RILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP--------IRRQRde 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 80 -------IGYVPenqGIFHDLTVEETFALASGKGEEVHEKIDWM------LELFPDL--KQfwnkksglLSGGQKQMLAI 144
Cdd:PRK13538 72 yhqdllyLGHQP---GIKTELTALENLRFYQRLHGPGDDEALWEalaqvgLAGFEDVpvRQ--------LSAGQQRRVAL 140
|
170
....*....|....*.
gi 447119455 145 SRAFINSDGLLLIDEP 160
Cdd:PRK13538 141 ARLWLTRAPLWILDEP 156
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-163 |
9.18e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 22 VSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYVPEN---QGIFHDLTVEET 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDrkaEGIIPVHSVADN 351
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 99 FALAS------------GKGEE--VHEKIDWMLELFPDLKQfwnkKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKG 163
Cdd:PRK11288 352 INISArrhhlragclinNRWEAenADRFIRSLNIKTPSREQ----LIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-163 |
1.07e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 21 GVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGYVPENQ---GIFHDLTVEE 97
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRkrdGLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFALASG----------KGEEVHEKIDWMLELF----PDLKQfwnkKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKG 163
Cdd:PRK10762 350 NMSLTALryfsraggslKHADEQQAVSDFIRLFniktPSMEQ----AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-51 |
1.17e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 1.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMG 51
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG 78
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-214 |
1.63e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLIS--RKGIgyvpenQGIFHD 92
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalRRDI------QFIFQD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 --------LTV-----EETFALASGKGEEVHEKIDWMLE---LFPDlkQFWnKKSGLLSGGQKQMLAISRAFINSDGLLL 156
Cdd:PRK10261 410 pyasldprQTVgdsimEPLRVHGLLPGKAAAARVAWLLErvgLLPE--HAW-RYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 157 IDEPSKGLSPIMIEKLMVAILKMKEKTTV--LLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-229 |
1.70e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.78 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIETYLD-------------QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNG 69
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 70 LSTH--LISRKGIgyvpenQGIFHD--------LTVEETFA------LASGKGEEVHEKIDWMLE---LFPDLkqfWNKK 130
Cdd:PRK15079 88 MKDDewRAVRSDI------QMIFQDplaslnprMTIGEIIAeplrtyHPKLSRQEVKDRVKAMMLkvgLLPNL---INRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 131 SGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpIMIEKLMVAILKMKEKT---TVLLVEQNFMMASQIGDYFYIMDN 207
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALD-VSIQAQVVNLLQQLQREmglSLIFIAHDLAVVKHISDRVLVMYL 237
|
250 260
....*....|....*....|..
gi 447119455 208 GRIVHKGFMNELREDkeTCHKY 229
Cdd:PRK15079 238 GHAVELGTYDEVYHN--PLHPY 257
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-214 |
1.79e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGfhRIaNGEIYYDSTQVNGLSTHLISRKGIGYVPENQGIFHDLTVEE 97
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RI-QGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 98 TFALAS--------GKGEEVHEKIDWMLELfpDLKQFWNKKSGL-----LSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:PLN03211 160 TLVFCSllrlpkslTKQEKILVAESVISEL--GLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447119455 165 SPIMIEKLMVAI--LKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PLN03211 238 DATAAYRLVLTLgsLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-172 |
5.07e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 1 MALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLrsvmgfhRIANGEIYYDSTQVNGLSTHLISR--- 77
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLM-------KILNGEVLLDDGRIIYEQDLIVARlqq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 78 ---------------KGIGYVPENQGIFHDLT--VEETFALAS-GKGEEVHEKID----WMLE-----------LFPDlk 124
Cdd:PRK11147 74 dpprnvegtvydfvaEGIEEQAEYLKRYHDIShlVETDPSEKNlNELAKLQEQLDhhnlWQLEnrinevlaqlgLDPD-- 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447119455 125 qfwnKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPIMIEKL 172
Cdd:PRK11147 152 ----AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWL 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-194 |
5.68e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTI---TVL--FGRNGAGKTTtlrsvmgFHRIANGEIYYDSTQVNGLSThlisrkgIGYVPENQGIFHDL 93
Cdd:PRK13409 350 LGDFSLEVEGGEIyegEVIgiVGPNGIGKTT-------FAKLLAGVLKPDEGEVDPELK-------ISYKPQYIKPDYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEETFALASGKGEEVHEKIDWMLELfpDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpiMIEKLM 173
Cdd:PRK13409 416 TVEDLLRSITDDLGSSYYKSEIIKPL--QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLA 491
|
170 180
....*....|....*....|....*
gi 447119455 174 VA--ILKMKE--KTTVLLVEQNFMM 194
Cdd:PRK13409 492 VAkaIRRIAEerEATALVVDHDIYM 516
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-51 |
7.04e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.97 E-value: 7.04e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 447119455 3 LLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMG 51
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-164 |
7.34e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.48 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 2 ALLQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHlISRKGIG 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE-IYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 82 YVPENQGIFHDlTVEETFALASgkgeEVHEKIDWMLELFPDLKQF------WNKKSGLLSGGQKQMLAISRAFINSDGLL 155
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFPW----QIRNQQPDPAIFLDDLERFalpdtiLTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
....*....
gi 447119455 156 LIDEPSKGL 164
Cdd:PRK10247 160 LLDEITSAL 168
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-164 |
9.71e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.93 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTL-----RSVMGfhrIANGEIYydstqVNGLSTHLISRKGIGYVPENQGIFHD 92
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLdvlagRKTAG---VITGEIL-----INGRPLDKNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 93 LTVEETfalasgkgeevhekidwmLELFPDLKQfwnkksglLSGGQKQMLAISRAFINSDGLLLIDEPSKGL 164
Cdd:cd03232 94 LTVREA------------------LRFSALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-219 |
1.17e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGfhriangEIYYDStqvnglSTHLISRKGIGYVPENQGIFhDLTVE 96
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-------ELPPRS------DASVVIRGTVAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 97 ETFALASGKGEEVHEK-IDWM-----LELFP--DLKQFWNKksGL-LSGGQKQMLAISRA-FINSDgLLLIDEPSKGLSP 166
Cdd:PLN03130 697 DNILFGSPFDPERYERaIDVTalqhdLDLLPggDLTEIGER--GVnISGGQKQRVSMARAvYSNSD-VYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 167 IMIEKLMVAILK--MKEKTTVLLVEQ-NFMmaSQIgDYFYIMDNGRIVHKGFMNEL 219
Cdd:PLN03130 774 HVGRQVFDKCIKdeLRGKTRVLVTNQlHFL--SQV-DRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-195 |
1.20e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.27 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVmGFhriangeiyydstqVNGLSTHLISRKGIGYVPENQGifhdlTVE 96
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-GL--------------ALGGAQSATRRRSGVKAGCIVA-----AVS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 97 ETFALAsgkgeevhekidwmlelfpdLKQfwnkksglLSGGQKQMLAISRAF----INSDGLLLIDEPSKGLSPIMIEKL 172
Cdd:cd03227 69 AELIFT--------------------RLQ--------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180
....*....|....*....|....
gi 447119455 173 MVAILKM-KEKTTVLLVEQNFMMA 195
Cdd:cd03227 121 AEAILEHlVKGAQVIVITHLPELA 144
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-179 |
1.44e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETY-LDQFHI--LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIAN-GEIYYDSTQVNGLSTHLISRKG 79
Cdd:PRK13549 260 LEVRNLTAWdPVNPHIkrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 80 IGYVPEN---QGIFHDLTVEETFALASGKGEEVHEKIDWMLEL---FPDLKQFWNKKS------GLLSGGQKQMLAISRA 147
Cdd:PRK13549 340 IAMVPEDrkrDGIVPVMGVGKNITLAALDRFTGGSRIDDAAELktiLESIQRLKVKTAspelaiARLSGGNQQKAVLAKC 419
|
170 180 190
....*....|....*....|....*....|....*
gi 447119455 148 FINSDGLLLIDEPSKGL---SPIMIEKLMVAILKM 179
Cdd:PRK13549 420 LLLNPKILILDEPTRGIdvgAKYEIYKLINQLVQQ 454
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-164 |
1.65e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGfhRIANGEIYYDSTQVNGLSTHLISRKGIGYVPENQGIFHDLTVEE 97
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119455 98 TFAL-------ASGKGEEVHEKIDWMLELFpDLKQFWNKKSGL----LSGGQKQMLAISRAFI-NSDGLLLIDEPSKGL 164
Cdd:TIGR00956 856 SLRFsaylrqpKSVSKSEKMEYVEEVIKLL-EMESYADAVVGVpgegLNVEQRKRLTIGVELVaKPKLLLFLDEPTSGL 933
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-205 |
1.69e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.16 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 25 TVEKGTITVLFGRNGAGKTTTLRsvmgfhrIANGEI------------------YYDSTQvngLSTHL--ISRKGIGYVP 84
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALK-------ILSGELkpnlgdydeepswdevlkRFRGTE---LQDYFkkLANGEIKVAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 85 ENQGIfhDLtVEETFalaSGKGEEVHEKIDW---MLELFP--DLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:COG1245 165 KPQYV--DL-IPKVF---KGTVRELLEKVDErgkLDELAEklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447119455 160 PSKGLSpiMIEKLMVAILKM---KEKTTVLLVEQNFMMASQIGDYFYIM 205
Cdd:COG1245 239 PSSYLD--IYQRLNVARLIRelaEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-188 |
1.79e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDStqvnGLSTHLISRK---GIG-------YvPENQ 87
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA----GARVLFLPQRpylPLGtlreallY-PATA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 88 GIFHDLTVEEtfALasgkgEEVHekIDWMLELFpDLKQFWNKksgLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSPI 167
Cdd:COG4178 453 EAFSDAELRE--AL-----EAVG--LGHLAERL-DEEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|.
gi 447119455 168 MIEKLMVAILKMKEKTTVLLV 188
Cdd:COG4178 520 NEAALYQLLREELPGTTVISV 540
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-194 |
2.01e-05 |
|
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: 44.78 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 19 LQGVSLTVEKGTI---TVL--FGRNGAGKTTtlrsvmgFHRIANGEIYYDSTQVNGLSThlisrkgIGYVPENQGIFHDL 93
Cdd:COG1245 351 YGGFSLEVEGGEIregEVLgiVGPNGIGKTT-------FAKILAGVLKPDEGEVDEDLK-------ISYKPQYISPDYDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 94 TVEEtfALASGKGEEVHEKIdWMLELF-P-DLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpiMIEK 171
Cdd:COG1245 417 TVEE--FLRSANTDDFGSSY-YKTEIIkPlGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQR 491
|
170 180
....*....|....*....|....*..
gi 447119455 172 LMVA--ILKMKE--KTTVLLVEQNFMM 194
Cdd:COG1245 492 LAVAkaIRRFAEnrGKTAMVVDHDIYL 518
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-188 |
2.25e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.75 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 31 ITVLFGRNGAGKTTTLRSVmgfhRIAngeIYYDSTQVNGLSTHL--ISRKGigyvpENQGIfhdltVEETFALASGKGEE 108
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAL----KYA---LTGELPPNSKGGAHDpkLIREG-----EVRAQ-----VKLAFENANGKKYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 109 VH--------------EKIDWMLELFPdlkqfwnkksGLLSGGQKQM------LAISRAFINSDGLLLIDEPSKGLSPIM 168
Cdd:cd03240 87 ITrslailenvifchqGESNWPLLDMR----------GRCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLDEEN 156
|
170 180
....*....|....*....|
gi 447119455 169 IEKLMVAILKMKEKTTVLLV 188
Cdd:cd03240 157 IEESLAEIIEERKSQKNFQL 176
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-197 |
2.26e-05 |
|
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: 43.47 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 17 HILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVM---GFHRIANG-EIYYDSTQVNGLSTHLISRKGIGYVPENQgifhd 92
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLyasGKARLISFlPKFSRNKLIFIDQLQFLIDVGLGYLTLGQ----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 ltveetfalasgkgeevhekidwmlelfpdlkqfwnkKSGLLSGGQKQMLAI-SRAFINSDG-LLLIDEPSKGLSPIMIE 170
Cdd:cd03238 84 -------------------------------------KLSTLSGGELQRVKLaSELFSEPPGtLFILDEPSTGLHQQDIN 126
|
170 180
....*....|....*....|....*...
gi 447119455 171 KLMVAILKM-KEKTTVLLVEQNFMMASQ 197
Cdd:cd03238 127 QLLEVIKGLiDLGNTVILIEHNLDVLSS 154
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-190 |
2.29e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 2.29e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 134 LSGGQKQMLAISRAFINSDGLLLIDEPSKGL---SPIMIEKLMVAILKMKEKTTVLLVEQ 190
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIEKTIVDIKDKADKTIITIAHR 1418
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-164 |
3.87e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.38 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 22 VSLTVEKGTITVLFGRNGAGKTTTLrsvmgfHRIA-----NGEIYYDSTQVNGLSTHLISRKGiGYVPENQG------IF 90
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLL------ARMAgllpgSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTppfampVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 91 HDLTVEETFALASGKGEEVHEKIDWMLELFPDLkqfwNKKSGLLSGGQKQ-------MLAISRAfINSDG-LLLIDEPSK 162
Cdd:PRK03695 88 QYLTLHQPDKTRTEAVASALNEVAEALGLDDKL----GRSVNQLSGGEWQrvrlaavVLQVWPD-INPAGqLLLLDEPMN 162
|
..
gi 447119455 163 GL 164
Cdd:PRK03695 163 SL 164
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-159 |
4.28e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.93 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNnietyLDQFH-------ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS-THL 74
Cdd:PRK10789 313 ELDVN-----IRQFTypqtdhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSW 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 75 ISRKGIgyVPENQGIFHDlTVEETFALasGKGEEVHEKIDWMLEL------FPDLKQFWNKKSG----LLSGGQKQMLAI 144
Cdd:PRK10789 388 RSRLAV--VSQTPFLFSD-TVANNIAL--GRPDATQQEIEHVARLasvhddILRLPQGYDTEVGergvMLSGGQKQRISI 462
|
170
....*....|....*
gi 447119455 145 SRAFINSDGLLLIDE 159
Cdd:PRK10789 463 ARALLLNAEILILDD 477
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-210 |
4.31e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 3 LLQVNNIeTYLDQFHIlQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLSTHLISRKGIGY 82
Cdd:PRK10982 250 ILEVRNL-TSLRQPSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPENQ---GIFHDLTVE------------ETFALASGKGEEVHEK--IDWMLELFPDLKqfwnKKSGLLSGGQKQMLAIS 145
Cdd:PRK10982 328 VTEERrstGIYAYLDIGfnslisnirnykNKVGLLDNSRMKSDTQwvIDSMRVKTPGHR----TQIGSLSGGNQQKVIIG 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 146 RAFINSDGLLLIDEPSKGL---SPIMIEKLMVAILKmKEKTTVLLVEQnfmMASQIG--DYFYIMDNGRI 210
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIdvgAKFEIYQLIAELAK-KDKGIIIISSE---MPELLGitDRILVMSNGLV 469
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-223 |
9.48e-05 |
|
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: 42.54 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYD-----STQVNGLSThlisrkgiGYVPENqgIFHD 92
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSgrisfSSQFSWIMP--------GTIKEN--IIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 LTVEETFALASGKGEEVHEKIdwmlELFPDLKQFWNKKSGL-LSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpIMIEK 171
Cdd:cd03291 122 VSYDEYRYKSVVKACQLEEDI----TKFPEKDNTVLGEGGItLSGGQRARISLARAVYKDADLYLLDSPFGYLD-VFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 172 LMV--AILK-MKEKTTVLLVEQnfMMASQIGDYFYIMDNGRIVHKGFMNELREDK 223
Cdd:cd03291 197 EIFesCVCKlMANKTRILVTSK--MEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-214 |
1.58e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.00 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 15 QFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYY------DSTQVNGLSTHLIS------------ 76
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdekNKKKTKEKEKVLEKlviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 77 -----RKGIGYV---PENQgIFHDlTVEETF---ALASG-KGEEVHEKIDWMLELFpDLKQFWNKKSGL-LSGGQKQMLA 143
Cdd:PRK13651 99 kikeiRRRVGVVfqfAEYQ-LFEQ-TIEKDIifgPVSMGvSKEEAKKRAAKYIELV-GLDESYLQRSPFeLSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119455 144 ISRAFINSDGLLLIDEPSKGLSPIMIEKlMVAILK--MKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKG 214
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKE-ILEIFDnlNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-223 |
1.84e-04 |
|
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: 42.20 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYD-----STQVNGLSThlisrkgiGYVPENqgIFHD 92
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSgrisfSPQTSWIMP--------GTIKDN--IIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 93 LTVEETFALASGKGEEVHEKIdwmlELFPDLKQFWNKKSGL-LSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpIMIEK 171
Cdd:TIGR01271 511 LSYDEYRYTSVIKACQLEEDI----ALFPEKDKTVLGEGGItLSGGQRARISLARAVYKDADLYLLDSPFTHLD-VVTEK 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119455 172 LMV--AILK-MKEKTTVLLVEQnfMMASQIGDYFYIMDNGRIVHKGFMNELREDK 223
Cdd:TIGR01271 586 EIFesCLCKlMSNKTRILVTSK--LEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
134-200 |
2.36e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.63 E-value: 2.36e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119455 134 LSGGQKQMLAISRAFINSDGLLLIDEPSKGLSpimIEKLMVAI-----LKMKEKTTVLLVEQNFMMASQIGD 200
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLD---IEQRLNAArairrLSEEGKKTALVVEHDLAVLDYLSD 140
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-158 |
2.45e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.05 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 28 KGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQvNGLSTHLISRKGIGYVPENQGIFHDLTVEETFALASGKG- 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE-DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKp 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 107 -----EEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINSDGLLLID 158
Cdd:smart00382 80 dvlilDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
138-219 |
2.61e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 138 QKQMLAIsrAFINSDGLLLIDEPSKGLSPIMIEKL--MVAILKMKEKTTVLLVEQNFMMASQIGDYFYIMDNGRIVHKGF 215
Cdd:PRK15093 165 QKVMIAI--ALANQPRLLIADEPTNAMEPTTQAQIfrLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
....
gi 447119455 216 MNEL 219
Cdd:PRK15093 243 SKEL 246
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-167 |
4.58e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 18 ILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFH-------------RIANGEIYYDstqvnglsthlISRKgIGYVP 84
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysndltlfgrRRGSGETIWD-----------IKKH-IGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 85 ENqgiFH-DLTVEETF--ALASG----------KGEEVHEKIDWMLELFPDLKQFWNKKSGLLSGGQKQMLAISRAFINS 151
Cdd:PRK10938 343 SS---LHlDYRVSTSVrnVILSGffdsigiyqaVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKH 419
|
170
....*....|....*.
gi 447119455 152 DGLLLIDEPSKGLSPI 167
Cdd:PRK10938 420 PTLLILDEPLQGLDPL 435
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-63 |
5.69e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 5.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 447119455 19 LQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIA--NGEIYYD 63
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFD 63
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-196 |
5.88e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 5.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119455 134 LSGGQKQMLAISRAF-INSDGLLLI-DEPSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMAS 196
Cdd:PRK00635 477 LSGGEQERTALAKHLgAELIGITYIlDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMIS 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-188 |
9.46e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 38.67 E-value: 9.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 4 LQVNNIETYLDQFHIL-QGVSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIyydstqvnglstHLISRKGIGY 82
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------------GMPEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 83 VPEnQGIFHDLTVEEtfALAsgkgeevhekidwmlelFPdlkqfWNKKsglLSGGQKQMLAISRAFINSDGLLLIDEPSK 162
Cdd:cd03223 69 LPQ-RPYLPLGTLRE--QLI-----------------YP-----WDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180
....*....|....*....|....*.
gi 447119455 163 GLSPIMiEKLMVAILKmKEKTTVLLV 188
Cdd:cd03223 121 ALDEES-EDRLYQLLK-ELGITVISV 144
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-159 |
9.70e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.96 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 22 VSLTVEKGTITVLFGRNGAGKTTTLRSVMGFHRIANGEIYYDSTQVNGLS----THLISrkgigyvpenqGIFHDLTVEE 97
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQpedyRKLFS-----------AVFTDFHLFD 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119455 98 TfaLASGKGEEVHEKI--DWM--LELFPDLKQFWNKKSGL-LSGGQKQMLAISRAFINSDGLLLIDE 159
Cdd:PRK10522 411 Q--LLGPEGKPANPALveKWLerLKMAHKLELEDGRISNLkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-51 |
2.75e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 2.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 447119455 4 LQVNNIETYLDQFHILQGVSLTVEKGTITVLFGRNGAGKTTTLRSVMG 51
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG 367
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
64-225 |
5.43e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 64 STQVNGLSTHLISRKGIGyvpENQGIFHDLTVEETFALASgkgEEVHEKIDWMLELFPDLKQFW---NKKSGLLSGGQKQ 140
Cdd:TIGR00630 422 AVTVGGKSIADVSELSIR---EAHEFFNQLTLTPEEKKIA---EEVLKEIRERLGFLIDVGLDYlslSRAAGTLSGGEAQ 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119455 141 MLAISRAfINSD--GLLLI-DEPSKGLSPIMIEKLMVAILKMKEK-TTVLLVEQNFMMASQiGDyfYIMD--------NG 208
Cdd:TIGR00630 496 RIRLATQ-IGSGltGVLYVlDEPSIGLHQRDNRRLINTLKRLRDLgNTLIVVEHDEDTIRA-AD--YVIDigpgagehGG 571
|
170
....*....|....*..
gi 447119455 209 RIVHKGFMNELREDKET 225
Cdd:TIGR00630 572 EVVASGTPEEILANPDS 588
|
|
| |
