|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
1.05e-124 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 352.04 E-value: 1.05e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVFRRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNT--IDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA 158
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSrkERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-220 |
2.99e-110 |
|
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: 315.20 E-value: 2.99e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFR 84
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKI 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-222 |
8.77e-88 |
|
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: 258.90 E-value: 8.77e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRtyvDKIIHLLH---LEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDAR---ARARALLErvgLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-222 |
3.22e-79 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 236.87 E-value: 3.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 8 KNLKKYYGQEPnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRRn 87
Cdd:COG2884 5 ENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 88 IGFVFQNYNLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIIL 165
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 166 ADEPTGNLDSKTSLEVMQLLKmtstEF---GQTLVMITHNPEL-AQIADRMIHIEDGKIVE 222
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLE----EInrrGTTVLIATHDLELvDRMPKRVLELEDGRLVR 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-222 |
1.12e-76 |
|
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: 230.55 E-value: 1.12e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRnIGFVFQNYNLVPILNVYQNIVLPIELDGntIDRTYVD-KIIHLLH---LEEKLDNLPNNLSGGQQQRVAIARALAS 159
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAG--VPKAEIEeRVLELLElvgLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVkRICDRVAVMEKGEVVE 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-222 |
1.48e-73 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 226.50 E-value: 1.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRnIGFVFQNYNLVPILNVYQNIVLPIELDG---NTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:COG1135 81 RRK-IGMIFQHFNLLSSRTVAENVALPLEIAGvpkAEIRKR-VAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHnpELA---QIADRMIHIEDGKIVE 222
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH--EMDvvrRICDRVAVLENGRIVE 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-221 |
1.89e-73 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 223.01 E-value: 1.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRnIGFVFQNYNLVPILNVYQNIvlpieLDG------------NTIDRTYVDKIIHLLH---LEEKLDNLPNNLSGGQQ 148
Cdd:COG3638 79 RRR-IGMIFQQFNLVPRLSVLTNV-----LAGrlgrtstwrsllGLFPPEDRERALEALErvgLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 149 QRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLArRYADRIIGLRDGRVV 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-213 |
1.83e-71 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 218.42 E-value: 1.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKmndeqltvf 83
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAerRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517425933 162 AIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMI 213
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAvFLADRVV 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-219 |
6.04e-70 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 212.88 E-value: 6.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:TIGR02673 1 MIEFHNVSKAY---PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRnIGFVFQNYNLVPILNVYQNIVLPIELDG---NTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGkkeREIQRR-VGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNPELA-QIADRMIHIEDGK 219
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLK-RLNKRGTTVIVATHDLSLVdRVAHRVIILDDGR 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-222 |
1.45e-68 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 210.02 E-value: 1.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTiDRTYVDKIIHLLH---LEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGES-SRQSRNGAKALLEqlgLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-222 |
3.82e-68 |
|
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: 208.14 E-value: 3.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMndeqltVFR 84
Cdd:cd03259 1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------PPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAeiRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRIVQ 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-222 |
3.97e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 209.08 E-value: 3.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVf 83
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQNYNLVPILNVYQNIVL-PIELDGntIDRTYVDKI-IHLL---HLEEKLDNLPNNLSGGQQQRVAIARALA 158
Cdd:COG1126 76 -RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKK--MSKAEAEERaMELLervGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHnpELA---QIADRMIHIEDGKIVE 222
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTH--EMGfarEVADRVVFMDGGRIVE 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-221 |
6.03e-68 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 212.27 E-value: 6.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvf 83
Cdd:COG3842 5 ALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQNYNLVPILNVYQNIVLPIELDG---NTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:COG3842 76 -KRNVGMVFQDYALFPHLTVAENVAFGLRMRGvpkAEIRAR-VAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPE--LAqIADRMIHIEDGKIV 221
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLA-LADRIAVMNDGRIE 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-223 |
6.78e-68 |
|
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: 208.13 E-value: 6.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVf 83
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFVFQNY--NLVPILNVYQNIVLPIELDGN-----TIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARA 156
Cdd:cd03257 80 RRKEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKlskkeARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 157 LASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKIVER 223
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVvAKIADRVAVMYAGKIVEE 227
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-220 |
9.55e-68 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 207.65 E-value: 9.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFVFQNYNLVPILNVYQNIVLPIELDG----NTIDRtyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALAS 159
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGvakkERIER--VNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHNPELAQIADRMIHIEDGKI 220
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYIN-QKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-213 |
3.51e-67 |
|
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: 206.17 E-value: 3.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKmndeqltvfR 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMI 213
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAvFLADRVV 203
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-221 |
4.59e-67 |
|
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: 206.65 E-value: 4.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFR 84
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRnIGFVFQNYNLVPILNVYQNIvlpieLDGNTIDRTYVDKIIHLLHLEEKLDNLPN---------------NLSGGQQQ 149
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENV-----LSGRLGRRSTWRSLFGLFPKEEKQRALAAlervglldkayqradQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRIV 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-223 |
1.90e-64 |
|
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: 207.83 E-value: 1.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQ-EPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTV 82
Cdd:COG1123 260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 FRRRnIGFVFQNYN--LVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHL----EEKLDNLPNNLSGGQQQRVAIARA 156
Cdd:COG1123 340 LRRR-VQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERvglpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 157 LASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVER 223
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVrYIADRVAVMYDGRIVED 486
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-221 |
5.51e-64 |
|
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: 198.33 E-value: 5.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYN--LV-PIlnVYQNIVLPIE---LDGNTIDRtYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA 158
Cdd:COG1122 74 RRKVGLVFQNPDdqLFaPT--VEEDVAFGPEnlgLPREEIRE-RVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIV 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-223 |
1.19e-63 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 198.10 E-value: 1.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfR 84
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNY--NLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEK-LDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:COG1124 78 RRRVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 162 AIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVER 223
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAhLCDRVAVMQNGRIVEE 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-223 |
4.45e-63 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 199.64 E-value: 4.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 6 ETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRR 85
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 86 rNIGFVFQNYNLVPILNVYQNIVLPIELDG---NTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:PRK11153 83 -QIGMIFQHFNLLSSRTVFDNVALPLELAGtpkAEIKAR-VTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHnpELA---QIADRMIHIEDGKIVER 223
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH--EMDvvkRICDRVAVIDAGRLVEQ 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-222 |
4.97e-63 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 199.60 E-value: 4.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmnDEQLTVfR 84
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLPP-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIV--LPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENIAfgLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEAlELADRVVVMNQGRIEQ 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-221 |
5.06e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 199.91 E-value: 5.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEigkMNDeqLTVfR 84
Cdd:COG3839 4 LELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD---VTD--LPP-K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIEL---DGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLrkvPKAEIDRR-VREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 162 AIILADEPTGNLDSK----TSLEVMQLLKmtstEFGQTLVMITHNPELAQ-IADRMIHIEDGKIV 221
Cdd:COG3839 153 KVFLLDEPLSNLDAKlrveMRAEIKRLHR----RLGTTTIYVTHDQVEAMtLADRIAVMNDGRIQ 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
5.66e-63 |
|
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: 195.97 E-value: 5.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVFRRRnIGFVFQNYNLVPILNVYQNIVLPI----ELDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARA 156
Cdd:COG1127 78 YELRRR-IGMLFQGGALFDSLTVFENVAFPLrehtDLSEAEIREL-VLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 157 LASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIA 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-221 |
1.13e-62 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 206.11 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVFRRRNIGFVFQNYNLVPILNVYQNIVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA 158
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLR-DRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-219 |
5.63e-62 |
|
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: 191.25 E-value: 5.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfR 84
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPieldgntidrtyvdkiihllhleekldnlpnnLSGGQQQRVAIARALASKPAII 164
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGK 219
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAArLADRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-220 |
1.21e-61 |
|
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: 191.85 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFR 84
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRnIGFVFQNYNLVPILNVYQNIVLPIELDGNT--IDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPprEIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKI 220
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLK-KINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-221 |
3.50e-60 |
|
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: 189.05 E-value: 3.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRnIGFVFQNYNLVPILNVYQNIvlpieLDGNTIDRTYVDKIIHLLHLEEK---LDNLP------------NNLSGGQQ 148
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENV-----LHGRLGYKPTWRSLLGRFSEEDKeraLSALErvgladkayqraDQLSGGQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 149 QRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEIV 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-222 |
3.02e-59 |
|
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: 186.55 E-value: 3.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFR 84
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRnIGFVFQNYNLVPILNVYQNIVLPI----ELDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPLrehtRLSEEEIREI-VLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIVA 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-220 |
3.29e-59 |
|
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: 185.43 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVfr 84
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVL-PIELDGntIDRTYVDKI-IHLLH---LEEKLDNLPNNLSGGQQQRVAIARALAS 159
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLaPIKVKG--MSKAEAEERaLELLEkvgLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHIEDGKI 220
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAReVADRVIFMDDGRI 213
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-215 |
8.35e-59 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 184.36 E-value: 8.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 8 KNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRRN 87
Cdd:TIGR03608 2 KNISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 88 IGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHL--LHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIIL 165
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALekVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517425933 166 ADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQIADRMIHI 215
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-219 |
1.99e-58 |
|
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: 183.44 E-value: 1.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 6 ETKNLKKYYGQEPniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrR 85
Cdd:cd03225 1 ELKNLSFSYPDGA--RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 86 RNIGFVFQNynlvP---ILN--VYQNIVLPIE---LDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARAL 157
Cdd:cd03225 75 RKVGLVFQN----PddqFFGptVEEEVAFGLEnlgLPEEEIEER-VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 158 ASKPAIILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGK 219
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEGKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-222 |
7.67e-57 |
|
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: 180.13 E-value: 7.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmndEQLTVFR 84
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-----TNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RrNIGFVFQNYNLVPILNVYQNIVLPIEL---DGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:cd03300 72 R-PVNTVFQNYALFPHLTVFENIAFGLRLkklPKAEIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 162 AIILADEPTGNLDSKTSlEVMQL-LKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:cd03300 150 KVLLLDEPLGALDLKLR-KDMQLeLKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQ 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-221 |
8.02e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.26 E-value: 8.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfr 84
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKeaRERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAIIDKGRIV 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-223 |
1.00e-55 |
|
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: 180.25 E-value: 1.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIP---SSGSVKIRGKEIGKMNDEQL 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVFRRRNIGFVFQN-YN-LVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHL------EEKLDNLPNNLSGGQQQRVA 152
Cdd:COG0444 81 RKIRGREIQMIFQDpMTsLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERvglpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 153 IARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADR---MIHiedGKIVER 223
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlGVVAEIADRvavMYA---GRIVEE 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-222 |
1.29e-54 |
|
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: 182.41 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEPniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPS----SGSVKIRGKEIGKMN 76
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHggriSGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 DEQltvfRRRNIGFVFQN--YNLVPiLNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVA 152
Cdd:COG1123 78 EAL----RGRRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAeaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 153 IARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKIVE 222
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVE 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-222 |
1.99e-54 |
|
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: 173.59 E-value: 1.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEigkMNDEQLtvfR 84
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD---VTDLPP---K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDG---NTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKvpkDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 162 AIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNP-ELAQIADRMIHIEDGKIVE 222
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQvEAMTMADRIAVMNDGQIQQ 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-221 |
4.34e-54 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 173.02 E-value: 4.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkaLDgIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfr 84
Cdd:COG3840 2 LRLDDLTYRYGDFP-----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 rRNIGFVFQNYNLVPILNVYQNIVLPIE--LDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:COG3840 71 -RPVSMLFQENNLFPHLTVAQNIGLGLRpgLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAaRIADRVLLVADGRIA 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-222 |
5.44e-54 |
|
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: 172.75 E-value: 5.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL-----DIPSSGSVKIRGKEIGKMNDEQ 79
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 LTVfrRRNIGFVFQNYNLVPiLNVYQNIVLPIELDGnTIDRTYVDKIIH------LLHLEEKLDNLPNNLSGGQQQRVAI 153
Cdd:cd03260 77 LEL--RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHG-IKLKEELDERVEealrkaALWDEVKDRLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 154 ARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFgqTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAArVADRTAFLLNGRLVE 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-221 |
7.52e-54 |
|
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: 173.31 E-value: 7.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvf 83
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFVFQNYNLVPILNVYQnIVL--------PIELDGNTiDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIAR 155
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRE-LVAlgryphlgLFGRPSAE-DREAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 156 ALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAaRYADRLVLLKDGRIV 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-220 |
1.41e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.15 E-value: 1.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLkkyyGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:COG4619 1 LELEGL----SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNynlvPIL---NVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEK-LDNLPNNLSGGQQQRVAIARALASK 160
Cdd:COG4619 73 RRQVAYVPQE----PALwggTVRDNLPFPFQLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKI 220
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-222 |
2.14e-53 |
|
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: 171.71 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGqepNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:cd03295 1 IEFENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDG---NTIdRTYVDKIIHLLHLEEK--LDNLPNNLSGGQQQRVAIARALAS 159
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIALVPKLLKwpkEKI-RERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQ 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-222 |
2.45e-53 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 171.73 E-value: 2.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIG---KMNDEQLT 81
Cdd:COG4161 3 IQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 82 VFRRrNIGFVFQNYNLVPILNVYQN-IVLPIELDGNT--IDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA 158
Cdd:COG4161 79 LLRQ-KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSkeQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFArKVASQVVYMEKGRIIE 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-223 |
3.38e-53 |
|
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: 181.57 E-value: 3.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 12 KYYGQEPNItkaLDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFV 91
Cdd:COG2274 482 RYPGDSPPV---LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL----RRQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNynlVPILN--VYQNIVLpieldGN-TIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARAL 157
Cdd:COG2274 555 LQD---VFLFSgtIRENITL-----GDpDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 158 ASKPAIILADEPTGNLDSKTSLEVMQLLKmtSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLR--RLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-224 |
4.75e-53 |
|
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: 169.78 E-value: 4.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 20 ITKALDGIDVKVE---PGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigKMNDEQLTVF---RRRNIGFVFQ 93
Cdd:cd03297 6 IEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT---VLFDSRKKINlppQQRKIGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 94 NYNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNL 173
Cdd:cd03297 83 QYALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 174 DSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVERK 224
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEyLADRIVVMEDGRLQYIG 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-220 |
3.15e-52 |
|
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: 168.67 E-value: 3.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNdeqltvFR 84
Cdd:cd03296 3 IEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIEL-------DGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARAL 157
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVkprserpPEAEIRAK-VHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 158 ASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKI 220
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-222 |
7.85e-52 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 167.88 E-value: 7.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGqepnITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKE--IGKMNDEQLTV 82
Cdd:PRK11124 3 IQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 FRRRNIGFVFQNYNLVPILNVYQN-IVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALAS 159
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGlsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARkTASRVVYMENGHIVE 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-222 |
1.23e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 167.19 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI-GKMNDEQLTv 82
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKVDERLI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 frRRNIGFVFQNYNLVPILNVYQNIVL-PIELDG------NTIDRTYVDKIihllHLEEKLDNLPNNLSGGQQQRVAIAR 155
Cdd:PRK09493 76 --RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGaskeeaEKQARELLAKV----GLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 156 ALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEkVASRLIFIDKGRIAE 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-222 |
1.25e-51 |
|
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: 168.21 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 16 QEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRRNIGFVFQNY 95
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 96 NLVPILNVYQNIVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNL 173
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 174 DSKTSLEvMQ--LLKMtSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:cd03294 192 DPLIRRE-MQdeLLRL-QAELQKTIVFITHDLDEAlRLGDRIAIMKDGRLVQ 241
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-221 |
4.31e-51 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 167.57 E-value: 4.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 8 KNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRN 87
Cdd:COG1125 5 ENVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL----RRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 88 IGFVFQNYNLVPILNVYQNIVLPIELDG---NTIDRTyVDKIIHLLHLEEK--LDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGwdkERIRAR-VDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 163 IILADEPTGNLD--SKTSL--EVMQLLKmtstEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:COG1125 157 ILLMDEPFGALDpiTREQLqdELLRLQR----ELGKTIVFVTHDIDEAlKLGDRIAVMREGRIV 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-220 |
6.99e-51 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 164.99 E-value: 6.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYgQEPNI-TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTV 82
Cdd:PRK11629 5 LLQCDNLCKRY-QEGSVqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 FRRRNIGFVFQNYNLVPILNVYQNIVLPIeLDGNTIDRTYVDKIIHLLH---LEEKLDNLPNNLSGGQQQRVAIARALAS 159
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAavgLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKI 220
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-219 |
1.33e-50 |
|
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: 162.17 E-value: 1.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNynlvPILnvyqnivlpieLDGnTIdrtyvdkiihllhleekLDNLpnnLSGGQQQRVAIARALASKPAII 164
Cdd:cd03228 75 RKNIAYVPQD----PFL-----------FSG-TI-----------------RENI---LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGK 219
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-223 |
2.27e-50 |
|
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: 171.86 E-value: 2.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynl 97
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQN--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 vPIL---NVYQNIVLpieldGN-TIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPA 162
Cdd:COG4988 420 -PYLfagTIRENLRL-----GRpDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-221 |
6.95e-50 |
|
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: 163.37 E-value: 6.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYgqEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGkeIGKMNDEQLTvFR 84
Cdd:TIGR04520 1 IEVENVSFSY--PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLW-EI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQN------------------YNL-VPilnvyqnivlPIELdgntidRTYVDKIIHLLHLEEKLDNLPNNLSG 145
Cdd:TIGR04520 76 RKKVGMVFQNpdnqfvgatveddvafglENLgVP----------REEM------RKRVDEALKLVGMEDFRDREPHLLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 146 GQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIV 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-226 |
5.19e-49 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 160.69 E-value: 5.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNL-KKYYGQEpnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI--GKMNDEQLT 81
Cdd:PRK11264 4 IEVKNLvKKFHGQT-----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 82 VFR--RRNIGFVFQNYNLVPILNVYQNIVL-PIELDGNTIDRTYV--DKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARA 156
Cdd:PRK11264 79 LIRqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATAraRELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 157 LASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHIEDGKIVERKES 226
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPA 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-221 |
7.12e-49 |
|
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: 157.98 E-value: 7.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 6 ETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfRR 85
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 86 RNIGFVFQnynlvpilnvyqnivlpieldgntidrtyvdkIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIIL 165
Cdd:cd03214 73 RKIAYVPQ--------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 166 ADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGRIV 177
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-218 |
2.07e-48 |
|
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: 158.78 E-value: 2.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrrrnigfVFQNYNLVPILNV 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 104 YQNIVLPIEL---DGNTID-RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSL 179
Cdd:TIGR01184 72 RENIALAVDRvlpDLSKSErRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517425933 180 EVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDG 218
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-222 |
4.43e-48 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 158.43 E-value: 4.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI-------GKM-- 75
Cdd:COG4598 9 LEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdGELvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 -NDEQLTVFRRRnIGFVFQNYNLVPILNVYQNIVL-PIELDGntIDRT-YVDKIIHLLH---LEEKLDNLPNNLSGGQQQ 149
Cdd:COG4598 85 aDRRQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVHVLG--RPKAeAIERAEALLAkvgLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSK---TSLEVMQLLkmtsTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPElvgEVLKVMRDL----AEEGRTMLVVTHEMGFArDVSSHVVFLHQGRIEE 234
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
24-222 |
4.97e-48 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 161.01 E-value: 4.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfrrRNIGFVFQNYNLVPILNV 103
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEK------RGIAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 104 YQNIVLPIEL---DGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLE 180
Cdd:NF040840 90 FENIAFGLKLrkvPKEEIERK-VKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517425933 181 VMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:NF040840 169 LIREMKRWHREFGFTAIHVTHNFEEAlSLADRVGIMLNGRLSQ 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-222 |
6.48e-48 |
|
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: 157.50 E-value: 6.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfr 84
Cdd:cd03299 1 LKVENLSKDWKE-----FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIEL---DGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKrkvDKKEIERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 162 AIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQ 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-222 |
1.04e-47 |
|
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: 157.33 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfR 84
Cdd:COG4555 2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRTY--VDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKkrIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNP-ELAQIADRMIHIEDGKIVE 222
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMqEVEALCDRVVILHKGKVVA 212
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-221 |
2.03e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 157.61 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQE-PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:TIGR04521 1 IKLKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRnIGFVFQN--YNLVPiLNVYQNIVL-PIE--LDGNTIDRtYVDKIIHLLHLEEK-LDNLPNNLSGGQQQRVAIARAL 157
Cdd:TIGR04521 81 RKK-VGLVFQFpeHQLFE-ETVYKDIAFgPKNlgLSEEEAEE-RVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 158 ASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGKIV 221
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEdVAEYADRVIVMHKGKIV 222
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-222 |
2.41e-47 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 159.43 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQl 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tvfrrRNIGFVFQNYNLVPILNVYQNI---VLPIELDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARAL 157
Cdd:TIGR03265 76 -----RDYGIVFQSYALFPNLTVADNIaygLKNRGMGRAEVAER-VAELLDLVGLPGSERKYPGQLSGGQQQRVALARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 158 ASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:TIGR03265 150 ATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVIEQ 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-223 |
3.38e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 163.40 E-value: 3.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLkkYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:COG4987 334 LELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNynlVPILN--VYQNIVLPielDGNTIDrtyvDKIIHLLH---LEEKLDNLPN-----------NLSGGQQ 148
Cdd:COG4987 408 RRRIAVVPQR---PHLFDttLRENLRLA---RPDATD----EELWAALErvgLGDWLAALPDgldtwlgeggrRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 149 QRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLkMTSTEfGQTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADL-LEALA-GRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-219 |
5.01e-47 |
|
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: 152.78 E-value: 5.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 6 ETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrR 85
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 86 RNIGFVFQnynlvpilnvyqnivlpieldgntidrtyvdkiihllhleekldnlpnnLSGGQQQRVAIARALASKPAIIL 165
Cdd:cd00267 73 RRIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 166 ADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHIEDGK 219
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-221 |
5.17e-47 |
|
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: 154.57 E-value: 5.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 28 DVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfrRRNIGFVFQNYNLVPILNVYQNI 107
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 108 VLPIE--LDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLL 185
Cdd:cd03298 92 GLGLSpgLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 517425933 186 KMTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGKIV 221
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIA 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-221 |
6.21e-47 |
|
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: 158.34 E-value: 6.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 19 NITKALDG----IDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigKMNDEQLTVFR---RRNIGFV 91
Cdd:COG4148 6 DFRLRRGGftldVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE---VLQDSARGIFLpphRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNYNLVPILNVYQNIvlpieLDG-----NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILA 166
Cdd:COG4148 83 FQEARLFPHLSVRGNL-----LYGrkrapRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 167 DEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNP-ELAQIADRMIHIEDGKIV 221
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLdEVARLADHVVLLEQGRVV 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-221 |
6.76e-47 |
|
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: 154.51 E-value: 6.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfr 84
Cdd:cd03224 1 LEVENLNAGYGKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLL-HLEEKLDNLPNNLSGGQQQRVAIARALASKPAI 163
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 164 ILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFAlEIADRAYVLERGRVV 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-222 |
8.83e-47 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 157.20 E-value: 8.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYY-------GQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIG 73
Cdd:COG4608 4 AEPLLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 74 KMNDEQLTVFRRRnIGFVFQN-Y-NLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHL----EEKLDNLPNNLSGGQ 147
Cdd:COG4608 84 GLSGRELRPLRRR-MQMVFQDpYaSLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELvglrPEHADRYPHEFSGGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 148 QQRVAIARALASKPAIILADEPTGNLDskTSLE--VMQLLKMTSTEFGQTLVMITHNpeLA---QIADRMIHIEDGKIVE 222
Cdd:COG4608 163 RQRIGIARALALNPKLIVCDEPVSALD--VSIQaqVLNLLEDLQDELGLTYLFISHD--LSvvrHISDRVAVMYLGKIVE 238
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
1.82e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.09 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKmndeql 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tvfRRRNIGFVFQNYNL---VPIlNVYQnIVL-------PIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQR 150
Cdd:COG1121 73 ---ARRRIGYVPQRAEVdwdFPI-TVRD-VVLmgrygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 151 VAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGKI 220
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREGKTILVVTHDLGaVREYFDRVLLLNRGLV 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-220 |
3.02e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 156.78 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDeqltvfR 84
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNI-----VLP--IELDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARAL 157
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIafgltVLPrrERPNAAAIKAK-VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 158 ASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKI 220
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAmEVADRVVVMSQGNI 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-220 |
3.03e-46 |
|
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: 151.01 E-value: 3.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfr 84
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIvlpieldgntidrtyvdkiihllhleekldnlpnNLSGGQQQRVAIARALASKPAII 164
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKI 220
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLR-ELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-221 |
7.63e-46 |
|
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: 152.89 E-value: 7.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TvfrRRNIGFVFQNYNLVPILNVYQNIVL-----------------PIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNL 143
Cdd:COG0411 77 A---RLGIARTFQNPRLFPELTVLENVLVaaharlgrgllaallrlPRARREEREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 144 SGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKIV 221
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLvMGLADRIVVLDFGRVI 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-223 |
3.68e-45 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 151.17 E-value: 3.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfr 84
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 rrniGFVFQNYNLVPILNVYQNIVLPIELDG-NTIDRTYV-DKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGvPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 163 IILADEPTGNLDSKTSlEVMQ--LLKMtSTEFGQTLVMITHNPELAQ-IADRMIHIED--GKIVER 223
Cdd:COG4525 155 FLLMDEPFGALDALTR-EQMQelLLDV-WQRTGKGVFLITHSVEEALfLATRLVVMSPgpGRIVER 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-223 |
5.17e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 157.63 E-value: 5.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 21 TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlVPI 100
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQD---TFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 101 LN--VYQNIVLpieldGN-TIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILA 166
Cdd:COG1132 426 FSgtIRENIRY-----GRpDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILIL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 167 DEPTGNLDSKTSLEVMQ-LLKMTStefGQTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:COG1132 501 DEATSALDTETEALIQEaLERLMK---GRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-213 |
7.64e-45 |
|
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: 149.51 E-value: 7.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfr 84
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID------------RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVA 152
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLllararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 153 IARALASKPAIILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNPEL-AQIADRMI 213
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIR-ELRERGITVLLVEHDMDVvMSLADRVT 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-222 |
1.23e-44 |
|
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: 151.88 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 39 IIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfrRRNIGFVFQNYNLVPILNVYQNIVLPIELDG--- 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKvpr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 116 NTIDrTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSlEVMQL-LKMTSTEFGQ 194
Cdd:TIGR01187 75 AEIK-PRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLR-DQMQLeLKTIQEQLGI 152
|
170 180
....*....|....*....|....*....
gi 517425933 195 TLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:TIGR01187 153 TFVFVTHDQEEAmTMSDRIAIMRKGKIAQ 181
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-170 |
1.84e-44 |
|
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: 145.87 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNYNLVPILNV 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 104 YQNIVLPIELDGNTiDRTYVDKIIHLLH-------LEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPT 170
Cdd:pfam00005 77 RENLRLGLLLKGLS-KREKDARAEEALEklglgdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-222 |
3.83e-44 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 148.21 E-value: 3.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLL---NMLGGLdIPS---SGSVKIRGKEI--GKM 75
Cdd:TIGR00972 1 AIEIENLNLFYGEK----EALKNINLDIPKNQVTALIGPSGCGKSTLLrslNRMNDL-VPGvriEGKVLFDGQDIydKKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 NDEQLtvfrRRNIGFVFQNYNLVPiLNVYQNIVLPIELDGnTIDRTYVDKII-HLL-------HLEEKLDNLPNNLSGGQ 147
Cdd:TIGR00972 76 DVVEL----RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHG-IKDKKELDEIVeESLkkaalwdEVKDRLHDSALGLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 148 QQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFgqTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:TIGR00972 150 QQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNmQQAARISDRTAFFYDGELVE 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
6.93e-44 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.88 E-value: 6.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL--DIPS---SGSVKIRGKEI--G 73
Cdd:COG1117 8 LEPKIEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIydP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 74 KMNDEQLtvfrRRNIGFVFQNYNLVPiLNVYQNIVLPIELDGNTiDRTYVDKIIhllhlEE-------------KLDNLP 140
Cdd:COG1117 84 DVDVVEL----RRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIK-SKSELDEIV-----EEslrkaalwdevkdRLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 141 NNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSL---EVMQLLKmtsTEFgqTLVMITHNpeLAQ---IADRMIH 214
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAkieELILELK---KDY--TIVIVTHN--MQQaarVSDYTAF 225
|
....*...
gi 517425933 215 IEDGKIVE 222
Cdd:COG1117 226 FYLGELVE 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-220 |
1.59e-43 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 150.10 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQlt 81
Cdd:PRK09452 12 SPLVELRGISKSFDG----KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 82 vfrrRNIGFVFQNYNLVPILNVYQNIV--LPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALAS 159
Cdd:PRK09452 86 ----RHVNTVFQSYALFPHMTVFENVAfgLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 160 KPAIILADEPTGNLDSKTSLEvMQL-LKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKI 220
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQ-MQNeLKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-221 |
1.96e-43 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 145.79 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvFRRRNIGFVFQNYNLVPIL 101
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVP-FLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 NVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSL 179
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDdiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517425933 180 EVMQLLKmtstEF---GQTLVMITHNPEL-AQIADRMIHIEDGKIV 221
Cdd:PRK10908 175 GILRLFE----EFnrvGVTVLMATHDIGLiSRRSYRMLTLSDGHLH 216
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-221 |
2.17e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 145.88 E-value: 2.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 28 DVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigkmnDEQLTVFRRRNIGFVFQNYNLVPILNVYQNI 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ------DHTTTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 108 VLPIE--LDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLL 185
Cdd:PRK10771 93 GLGLNpgLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 517425933 186 KMTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGKIV 221
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEdAARIAPRSLVVADGRIA 209
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-222 |
7.03e-43 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 145.33 E-value: 7.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRrNIGFVFQN-YNLV-PIL 101
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRR-DVQLVFQDsPSAVnPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 NVYQNIVLPIE----LDGNTIDRtyvdKIIHLLHL----EEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNL 173
Cdd:TIGR02769 106 TVRQIIGEPLRhltsLDESEQKA----RIAELLDMvglrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517425933 174 DSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQsFCQRVAVMDKGQIVE 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-221 |
3.19e-42 |
|
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: 142.26 E-value: 3.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNItkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfr 84
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARLKGlpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQI-ADRMIHIEDGKIV 221
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-221 |
4.25e-42 |
|
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: 141.96 E-value: 4.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 12 KYYGQEpniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFV 91
Cdd:cd03245 11 SYPNQE---IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNYNLVpILNVYQNIVLpieldGNT-IDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALAS 159
Cdd:cd03245 84 PQDVTLF-YGTLRDNITL-----GAPlADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-223 |
5.76e-42 |
|
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: 149.06 E-value: 5.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKS----TLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQ 79
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 LTVFRRRNIGFVFQ------NynlvPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHL------EEKLDNLPNNLSGGQ 147
Cdd:COG4172 86 LRRIRGNRIAMIFQepmtslN----PLHTIGKQIAEVLRLHRGLSGAAARARALELLERvgipdpERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 148 QQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNpeL---AQIADRMIHIEDGKIVER 223
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD--LgvvRRFADRVAVMRQGEIVEQ 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-223 |
1.10e-41 |
|
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: 148.29 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYY-------GQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPSSGSVKIRGKEIGKMN 76
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 DEQLTVFRRRnIGFVFQN-YN-LVPILNVYQNI-----VLPIELDGNTIDrtyvDKIIHLLH----LEEKLDNLPNNLSG 145
Cdd:COG4172 354 RRALRPLRRR-MQVVFQDpFGsLSPRMTVGQIIaeglrVHGPGLSAAERR----ARVAEALEevglDPAARHRYPHEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 146 GQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNpeLA---QIADRMIHIEDGKIVE 222
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD--LAvvrALAHRVMVMKDGKVVE 506
|
.
gi 517425933 223 R 223
Cdd:COG4172 507 Q 507
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-219 |
1.76e-41 |
|
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: 139.92 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfR 84
Cdd:COG4133 3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-----Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQiADRMIHIEDGK 219
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELA-AARVLDLGDFK 206
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-220 |
3.54e-41 |
|
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: 139.61 E-value: 3.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 28 DVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigkmnDEQLTVFRRRNIGFVFQNYNLVPILNVYQNI 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ------SHTGLAPYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 108 VLPIE--LDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLL 185
Cdd:TIGR01277 92 GLGLHpgLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 517425933 186 KMTSTEFGQTLVMITHNP-ELAQIADRMIHIEDGKI 220
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLsDARAIASQIAVVSQGKI 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-221 |
8.55e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 139.84 E-value: 8.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQE-PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltv 82
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 fRRRNIGFVFQNYNL--VPILNVYQNIV----------LPIELDGNTIDRtYVDKIIHL-LHLEEKLDNLPNNLSGGQQQ 149
Cdd:COG1101 78 -RAKYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrrgLRRGLTKKRREL-FRELLATLgLGLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAlDYGNRLIMMHEGRII 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-222 |
1.08e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 142.67 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYY-GQEpnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltv 82
Cdd:PRK11607 19 LLEIRNLTKSFdGQH-----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 frrRNIGFVFQNYNLVPILNVYQNIVLPIELD----GNTIDRtyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA 158
Cdd:PRK11607 91 ---RPINMMFQSYALFPHMTVEQNIAFGLKQDklpkAEIASR--VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 159 SKPAIILADEPTGNLDSK----TSLEVMQLLKmtstEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKlrdrMQLEVVDILE----RVGVTCVMVTHDQEEAMtMAGRIAIMNRGKFVQ 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-216 |
1.80e-40 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 141.52 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDeqltvfR 84
Cdd:PRK11650 4 LKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIV--LPIE-LDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAygLKIRgMPKAEIEER-VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 162 AIILADEPTGNLDSK----TSLEVMQL---LKMTStefgqtlVMITHNP-ELAQIADRMI-----HIE 216
Cdd:PRK11650 154 AVFLFDEPLSNLDAKlrvqMRLEIQRLhrrLKTTS-------LYVTHDQvEAMTLADRVVvmnggVAE 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-222 |
1.83e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.77 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLK-KYYGQEpniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEigkMNDEq 79
Cdd:PRK13635 2 KEEIIRVEHISfRYPDAA---TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 lTVFR-RRNIGFVFQNY-NLVPILNVYQNIVLPIELDG----NTIDRtyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAI 153
Cdd:PRK13635 75 -TVWDvRRQVGMVFQNPdNQFVGATVQDDVAFGLENIGvpreEMVER--VDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 154 ARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-220 |
4.09e-40 |
|
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: 135.42 E-value: 4.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLK-KYYGQEPNItkaLDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvf 83
Cdd:cd03246 1 LEVENVSfRYPGAEPPV---LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQNYNLvpilnvyqnivlpieLDGNTIDrtyvdkiihllhleekldnlpNNLSGGQQQRVAIARALASKPAI 163
Cdd:cd03246 75 -GDHVGYLPQDDEL---------------FSGSIAE---------------------NILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 164 ILADEPTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHNPELAQIADRMIHIEDGKI 220
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-221 |
6.79e-40 |
|
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: 145.01 E-value: 6.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 12 KYYGQEPnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFV 91
Cdd:TIGR03375 472 AYPGQET---PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL----RRNIGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNynlvPIL---NVYQNIvlpieldgnTIDRTYVD-----KIIHLLHLEEKLDNLPN-----------NLSGGQQQRVA 152
Cdd:TIGR03375 545 PQD----PRLfygTLRDNI---------ALGAPYADdeeilRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVA 611
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 153 IARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLDLVDRIIVMDNGRIV 678
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-220 |
1.17e-39 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 136.73 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfr 84
Cdd:PRK11247 13 LLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 rrnIGFVFQNYNLVPILNVYQNIVLPieLDGNTidRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:PRK11247 83 ---TRLMFQDARLLPWKKVIDNVGLG--LKGQW--RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKI 220
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-222 |
1.39e-39 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 137.13 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYY------GQEPNITkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMND 77
Cdd:PRK10419 3 LLNVSGLSHHYahgglsGKHQHQT-VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 78 EQLTVFRRrNIGFVFQN----YNlvPILNVYQNIVLPIE--LDGNTIDRTY-VDKIIHLLHL-EEKLDNLPNNLSGGQQQ 149
Cdd:PRK10419 82 AQRKAFRR-DIQMVFQDsisaVN--PRKTVREIIREPLRhlLSLDKAERLArASEMLRAVDLdDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVErFCQRVMVMDNGQIVE 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-221 |
1.60e-39 |
|
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: 135.88 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvf 83
Cdd:COG0410 3 MLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQNYNLVPILNVYQNIVLPIEL--DGNTIDRTyVDKIIHLL-HLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:COG0410 77 -RLGIGYVPEGRRIFPSLTVEENLLLGAYArrDRAEVRAD-LERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFAlEIADRAYVLERGRIV 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-220 |
2.32e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 139.01 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 8 KNLKKYYGqEPNITKaldGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigKMNDEQLTvfrRRN 87
Cdd:PRK11000 7 RNVTKAYG-DVVISK---DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPA---ERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 88 IGFVFQNYNLVPILNVYQNIVLPIELDG---NTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGakkEEINQR-VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 165 LADEPTGNLDS----KTSLEVMQLLKmtstEFGQTLVMITHNP-ELAQIADRMIHIEDGKI 220
Cdd:PRK11000 156 LLDEPLSNLDAalrvQMRIEISRLHK----RLGRTMIYVTHDQvEAMTLADKIVVLDAGRV 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-222 |
1.09e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 134.33 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIG--KMNDEQLTV 82
Cdd:PRK10619 6 LNVIDLHKRYGEH----EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvRDKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 FR-------RRNIGFVFQNYNLVPILNVYQNIV-LPIELDG--NTIDRTYVDKIIHLLHLEEKL-DNLPNNLSGGQQQRV 151
Cdd:PRK10619 82 ADknqlrllRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGlsKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 152 AIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARhVSSHVIFLHQGKIEE 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-222 |
1.16e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 134.20 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL-----DIPSSGSVKIRGKEIGKM 75
Cdd:PRK14267 1 MKFAIETVNLRVYYGS----NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 NDEQLTVfrRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLL--------HLEEKLDNLPNNLSGGQ 147
Cdd:PRK14267 77 DVDPIEV--RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 148 QQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFgqTLVMITHNP-ELAQIADRMIHIEDGKIVE 222
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPaQAARVSDYVAFLYLGKLIE 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-221 |
1.52e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.35 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 6 ETKNLK-KYYGQEPNitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:PRK13632 9 KVENVSfSYPNSENN---ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNlvpilnvYQNIVLPIE------LDGNTIDRTYVDKII----HLLHLEEKLDNLPNNLSGGQQQRVAIA 154
Cdd:PRK13632 82 RKKIGIIFQNPD-------NQFIGATVEddiafgLENKKVPPKKMKDIIddlaKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 155 RALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-221 |
1.88e-38 |
|
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: 132.88 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKmndEQLTVfr 84
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR---EPREV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYIHARLYGvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRII 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-222 |
1.95e-38 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.00 E-value: 1.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQl 80
Cdd:COG1129 1 AEPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tvFRRRNIGFVFQNYNLVPILNVYQNIVLPIEL-DGNTIDRTYV----DKIIHLLHLEEKLDNLPNNLSGGQQQRVAIAR 155
Cdd:COG1129 76 --AQAAGIAIIHQELNLVPNLSVAENIFLGREPrRGGLIDWRAMrrraRELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 156 ALASKPAIILADEPTGNLDSKTS---LEVMQLLKmtstEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVerlFRIIRRLK----AQGVAIIYISHRlDEVFEIADRVTVLRDGRLVG 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-215 |
5.09e-38 |
|
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: 131.50 E-value: 5.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 6 ETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMndeqltvfrR 85
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---------R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 86 RNIGFVFQNYNL---VPIlNVYQNIVLPieLDG--------NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIA 154
Cdd:cd03235 68 KRIGYVPQRRSIdrdFPI-SVRDVVLMG--LYGhkglfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 155 RALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHI 215
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLeYFDRVLLL 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-221 |
9.57e-38 |
|
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: 130.45 E-value: 9.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 21 TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNdeqltvfRRRNIGFVFQN--YNLV 98
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RRKSIGYVMQDvdYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 PIlNVYQNIVLPIELDGNTIDRtyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTS 178
Cdd:cd03226 86 TD-SVREELLLGLKELDAGNEQ--AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517425933 179 LEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHIEDGKIV 221
Cdd:cd03226 163 ERVGELIRELAAQ-GKAVIVITHDYEFLAkVCDRVLLLANGAIV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-220 |
1.14e-37 |
|
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: 134.08 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDgIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigKMNDEQLTVF---RRRNIGFVFQNYNLVP 99
Cdd:TIGR02142 13 SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR---TLFDSRKGIFlppEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 ILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSL 179
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517425933 180 EVMQLLKMTSTEFGQTLVMITHNP-ELAQIADRMIHIEDGKI 220
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLqEVLRLADRVVVLEDGRV 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
2.40e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 128.70 E-value: 2.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:PRK13647 1 MDNIIEVEDLHFRY---KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tvfrRRNIGFVFQNynlvPILNVYQNIV--------LPIELDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVA 152
Cdd:PRK13647 78 ----RSKVGLVFQD----PDDQVFSSTVwddvafgpVNMGLDKDEVERR-VEEALKAVRMWDFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 153 IARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAaEWADQVIVLKEGRVL 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-223 |
3.52e-36 |
|
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: 127.26 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfr 84
Cdd:TIGR03410 1 LEVSNLNVYYGQ----SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGnTIDRTYVDKIIHLLH-LEEKLDNLPNNLSGGQQQRVAIARALASKPAI 163
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGLAALP-RRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 164 ILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVER 223
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFArELADRYYVMERGRVVAS 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-221 |
4.33e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 128.28 E-value: 4.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYY--GQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEigkMNDE 78
Cdd:PRK13633 1 MNEMIKCKNVSYKYesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD---TSDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 79 QLTVFRRRNIGFVFQNY-NLVPILNVYQNI--------VLPIELdgntidRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQ 149
Cdd:PRK13633 78 ENLWDIRNKAGMVFQNPdNQIVATIVEEDVafgpenlgIPPEEI------RERVDESLKKVGMYEYRRHAPHLLSGGQKQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
6.74e-36 |
|
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: 126.39 E-value: 6.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKY---YGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKE----IG 73
Cdd:COG4778 1 MTTLLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 74 KMNDEQLTVFRRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNL-PNNLSGGQQQR 150
Cdd:COG4778 81 QASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREeaRARARELLARLNLPERLWDLpPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 151 VAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPEL-AQIADRMIHIEDG 218
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVrEAVADRVVDVTPF 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-221 |
1.05e-35 |
|
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: 126.35 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSG-SVKIRGKEIGKMNDEQL 80
Cdd:COG1119 1 DPLLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tvfrRRNIGFV---FQNYNLV--PILNV-----YQNIVLPIELDgnTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQR 150
Cdd:COG1119 77 ----RKRIGLVspaLQLRFPRdeTVLDVvlsgfFDSIGLYREPT--DEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 151 VAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPE--LAQIaDRMIHIEDGKIV 221
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeiPPGI-THVLLLKDGRVV 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-221 |
1.06e-35 |
|
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: 123.69 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmndEQLTVF- 83
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-----SFASPRd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 -RRRNIGFVFQnynlvpilnvyqnivlpieldgntidrtyvdkiihllhleekldnlpnnLSGGQQQRVAIARALASKPA 162
Cdd:cd03216 72 aRRAGIAMVYQ-------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-223 |
1.19e-35 |
|
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: 125.56 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKmndEQLTVf 83
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---EPAEA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQNYNLVPILNVYQNIVLPIELDG----NTIDRtyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALAS 159
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYGlkgdELTAR--LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 160 KPAIILADEPTGNLD---SKTSLEVMQLLKmtstEFGQTLVMITHN-PELAQIADRMIHIEDGKIVER 223
Cdd:cd03266 154 DPPVLLLDEPTTGLDvmaTRALREFIRQLR----ALGKCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-222 |
1.97e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.80 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL-----DIPSSGSVKIRGKEIGKMNDEQ 79
Cdd:PRK14247 4 IEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 LtvfrRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID--------RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRV 151
Cdd:PRK14247 80 L----RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkkelqervRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 152 AIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFgqTLVMITHNP-ELAQIADRMIHIEDGKIVE 222
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPqQAARISDYVAFLYKGQIVE 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-221 |
2.05e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 125.58 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 6 ETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrr 85
Cdd:COG4604 3 EIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 86 RNIGFVFQNYNLVPILNVYqnivlpiELDG-----------NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIA 154
Cdd:COG4604 75 KRLAILRQENHINSRLTVR-------ELVAfgrfpyskgrlTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 155 RALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQI-ADRMIHIEDGKIV 221
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVV 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
2.92e-35 |
|
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: 130.69 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKK-YYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIR-GKEIGKMNDEQLT 81
Cdd:TIGR03269 279 IIKVRNVSKrYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 82 VFRR--RNIGFVFQNYNLVPILNVYQNIVLPIELDgnTIDRTYVDKIIHLLHL--------EEKLDNLPNNLSGGQQQRV 151
Cdd:TIGR03269 359 GRGRakRYIGILHQEYDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMvgfdeekaEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 152 AIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVK 508
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-215 |
3.35e-35 |
|
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: 130.48 E-value: 3.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNYNL 97
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQHPFL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 VP--ILNvyqNIVL------PIELDgNTIDRTYVDKIIHLL--HLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILAD 167
Cdd:TIGR02857 408 FAgtIAE---NIRLarpdasDAEIR-EALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517425933 168 EPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHI 215
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-221 |
3.52e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.96 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVf 83
Cdd:PRK13639 1 ILETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQNYN---LVPilNVYQNIV---LPIELDGNTIDRTYVD--KIIHLLHLEEKldnLPNNLSGGQQQRVAIAR 155
Cdd:PRK13639 77 -RKTVGIVFQNPDdqlFAP--TVEEDVAfgpLNLGLSKEEVEKRVKEalKAVGMEGFENK---PPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 156 ALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQI-ADRMIHIEDGKIV 221
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVyADKVYVMSDGKII 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-223 |
7.51e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 124.43 E-value: 7.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvf 83
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rrrniGFVFQNYNLVPILNVYQNIVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 162 AIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIE--DGKIVER 223
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVfMATELVLLSpgPGRVVER 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
22-223 |
1.31e-34 |
|
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: 123.11 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlVPIL 101
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQD---TVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 N--VYQNIVLPiELDGNTIDrtyVDKIIHLLHLEEKLDNLPNN-----------LSGGQQQRVAIARALASKPAIILADE 168
Cdd:cd03253 88 NdtIGYNIRYG-RPDATDEE---VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 169 PTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNpeLAQI--ADRMIHIEDGKIVER 223
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSK--GRTTIVIAHR--LSTIvnADKIIVLKDGRIVER 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
1.39e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 124.14 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 3 YILETKNLKKYYGQEpniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtv 82
Cdd:PRK13652 2 HLIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 frRRNIGFVFQNYN-LVPILNVYQNIVL-PIE--LDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA 158
Cdd:PRK13652 77 --RKFVGLVFQNPDdQIFSPTVEQDIAFgPINlgLDEETVAHR-VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKIV 221
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKGRIV 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-222 |
1.44e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 123.73 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLL---NMLGGL--DIPSSGSVKIRGKEIGKM 75
Cdd:PRK14239 2 TEPILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 NDEqlTVFRRRNIGFVFQNYNLVPiLNVYQNIVLPIELDG----NTIDRTYVDKIIHLLHLEEKLDNLPNN---LSGGQQ 148
Cdd:PRK14239 78 RTD--TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGikdkQVLDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 149 QRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFgqTLVMITHNPELA-QIADRMIHIEDGKIVE 222
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQAsRISDRTGFFLDGDLIE 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
8-221 |
1.94e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.00 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 8 KNLKKYYGQE-PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNdEQLTVFRRR 86
Cdd:PRK13637 6 ENLTHIYMEGtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK-VKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 87 nIGFVFQ--NYNLVPiLNVYQNIVL-PIEL---DGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:PRK13637 85 -VGLVFQypEYQLFE-ETIEKDIAFgPINLglsEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGKIV 221
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCE 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-222 |
3.24e-34 |
|
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: 121.95 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 19 NITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNYNLV 98
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 PilnvyQNIVLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILAD 167
Cdd:cd03254 90 S-----GTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 168 EPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
3.39e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.30 E-value: 3.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLK-KYYGQEPNITkaLDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQ 79
Cdd:PRK13650 1 MSNIIEVKNLTfKYKEDQEKYT--LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 LtvfrRRNIGFVFQNY-NLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARA 156
Cdd:PRK13650 79 I----RHKIGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEemKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 157 LASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKI 220
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
4.03e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.07 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKE--IGKMNDE 78
Cdd:COG3845 2 MPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 79 qltvfRRRNIGFVFQNYNLVPILNVYQNIVLPIE-LDGNTID----RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAI 153
Cdd:COG3845 78 -----IALGIGMVHQHFMLVPNLTVAENIVLGLEpTKGGRLDrkaaRARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 154 ARALASKPAIILADEPTGNLdskTSLEVMQLL----KMTSTefGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:COG3845 153 LKALYRGARILILDEPTAVL---TPQEADELFeilrRLAAE--GKSIIFITHKlREVMAIADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-221 |
7.37e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.82 E-value: 7.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 13 YYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI-GKMNDEQLTVFRRRnIGFV 91
Cdd:PRK13634 12 YQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKK-VGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQnynlVPILNVYQNIVL------PIELDGNTID-RTYVDKIIHLLHLEEK-LDNLPNNLSGGQQQRVAIARALASKPAI 163
Cdd:PRK13634 91 FQ----FPEHQLFEETVEkdicfgPMNFGVSEEDaKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 164 ILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGKIV 221
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEdAARYADQIVVMHKGTVF 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-222 |
1.25e-33 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 123.15 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYY------GQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGK 74
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 75 mNDEQLTVFRRRNIGFVFQNynlvPI--LNVYQNI--VLPIELDGNTID-----RTYVDKIIHLLHLE-EKLDNLPNNLS 144
Cdd:PRK11308 82 -ADPEAQKLLRQKIQIVFQN----PYgsLNPRKKVgqILEEPLLINTSLsaaerREKALAMMAKVGLRpEHYDRYPHMFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 145 GGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNpeLA---QIADRMIHIEDGKIV 221
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD--LSvveHIADEVMVMYLGRCV 234
|
.
gi 517425933 222 E 222
Cdd:PRK11308 235 E 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-221 |
1.30e-33 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 123.45 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 19 NITKALDGIDVKVE---PGEFVS-IIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigKMNDEQLTVF---RRRNIGFV 91
Cdd:PRK11144 5 NFKQQLGDLCLTVNltlPAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAEKGIClppEKRRIGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNYNLVPILNVYQNIVLPIeldgNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTG 171
Cdd:PRK11144 82 FQDARLFPHYKVRGNLRYGM----AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517425933 172 NLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINIPILYVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-223 |
1.34e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 121.48 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYG-----QEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKM 75
Cdd:COG4167 1 MSALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 NDEQltvfRRRNIGFVFQNYN--LVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLH----LEEKLDNLPNNLSGGQQQ 149
Cdd:COG4167 81 DYKY----RCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRlvglLPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVER 223
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKhISDKVLVMHQGEVVEY 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
3.13e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 121.88 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLK-KYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:PRK13631 19 DIILRVKNLYcVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVFR------------RRNIGFVFQ--NYNLVPIlNVYQNIVL-PIELDGNTID-RTYVDKIIHLLHLEEK-LDNLPNNL 143
Cdd:PRK13631 99 LITNpyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFgPVALGVKKSEaKKLAKFYLNKMGLDDSyLERSPFGL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 144 SGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGKIV 221
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEhVLEVADEVIVMDKGKIL 255
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-222 |
7.71e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 121.37 E-value: 7.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNItkalDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfr 84
Cdd:PRK11432 7 VVLKNITKRFGSNTVI----DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 rRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:PRK11432 78 -RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDqSEAFAVSDTVIVMNKGKIMQ 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-221 |
1.39e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.81 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQE-PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSV---------KIRGKEIGK 74
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 75 MNDE---QLTVFR--------RRNIGFVFQnynlvpiLNVYQNIVLPIELD--------GNTIDRTY--VDKIIHLLHL- 132
Cdd:PRK13651 83 VLEKlviQKTRFKkikkikeiRRRVGVVFQ-------FAEYQLFEQTIEKDiifgpvsmGVSKEEAKkrAAKYIELVGLd 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 133 EEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELA-QIADR 211
Cdd:PRK13651 156 ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVlEWTKR 234
|
250
....*....|
gi 517425933 212 MIHIEDGKIV 221
Cdd:PRK13651 235 TIFFKDGKII 244
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-217 |
1.42e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.20 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL---DIPSSGSVKIRGKEIGKMNDEQlt 81
Cdd:COG4136 2 LSLENLTITLGGRP----LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEVLLNGRRLTALPAEQ-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 82 vfrrRNIGFVFQNYNLVPILNVYQNIV--LPieldgNTIDRTYVDKIIhllhlEEKLDNL---------PNNLSGGQQQR 150
Cdd:COG4136 76 ----RRIGILFQDDLLFPHLSVGENLAfaLP-----PTIGRAQRRARV-----EQALEEAglagfadrdPATLSGGQRAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 151 VAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIED 217
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-219 |
1.81e-32 |
|
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: 116.80 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 21 TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLN-MLGGLDiPSSGSVKIRGKeigkmndeqltvfrrrnIGFVFQnynlVP 99
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELE-KLSGSVSVPGS-----------------IAYVSQ----EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 -ILN--VYQNIVLpieldGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIIL 165
Cdd:cd03250 76 wIQNgtIRENILF-----GKPFDEERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517425933 166 ADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGK 219
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-222 |
2.21e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.78 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQE-PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI----GKMNDEQ 79
Cdd:PRK13641 3 IKFENVDYIYSPGtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 LtvfrRRNIGFVFQnynlVPILNVYQNIVL------PIELdGNTID--RTYVDKIIHLLHLEEKL-DNLPNNLSGGQQQR 150
Cdd:PRK13641 83 L----RKKVSLVFQ----FPEAQLFENTVLkdvefgPKNF-GFSEDeaKEKALKWLKKVGLSEDLiSKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 151 VAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHGKLIK 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-222 |
2.98e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 117.72 E-value: 2.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNI-----GFVFQN--YNLVPILNVYQNIVLPIELDGN----TIDRTYVDkiiHLLHLE---EKLDNLPNNLSGGQQQ 149
Cdd:PRK11701 82 ERRRLlrtewGFVHQHprDGLRMQVSAGGNIGERLMAVGArhygDIRATAGD---WLERVEidaARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQI-ADRMIHIEDGKIVE 222
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVE 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-221 |
5.66e-32 |
|
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: 115.34 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPS--SGSVKIRGKEIGKMNdeqltvFRRRnIGFVFQNYNLVPIL 101
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRS------FRKI-IGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 NVYQNIVLPIELDGntidrtyvdkiihllhleekldnlpnnLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEV 181
Cdd:cd03213 98 TVRETLMFAAKLRG---------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517425933 182 MQLLK-MTSTefGQTLVMITHNP--ELAQIADRMIHIEDGKIV 221
Cdd:cd03213 151 MSLLRrLADT--GRTIICSIHQPssEIFELFDKLLLLSQGRVI 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-220 |
1.43e-31 |
|
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: 115.33 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNdeqltVFR 84
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP-----MHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 R--RNIGFVFQNYNLVPILNVYQNI--VLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:cd03218 72 RarLGIGYLPQEASIFRKLTVEENIlaVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLK-MTSTEFGqtlVMIT-HN-PELAQIADRMIHIEDGKI 220
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKiLKDRGIG---VLITdHNvRETLSITDRAYIIYEGKV 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-223 |
1.88e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 120.72 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDG-IDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNYNLvPI 100
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESW----RKHLSWVGQNPQL-PH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 101 LNVYQNIVL------PIELDgNTIDRTYVDKIIHllHLEEKLDNLPNN----LSGGQQQRVAIARALASKPAIILADEPT 170
Cdd:PRK11174 437 GTLRDNVLLgnpdasDEQLQ-QALENAWVSEFLP--LLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517425933 171 GNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQ 564
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-223 |
1.98e-31 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 120.59 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlVPIL 101
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL----RRQVALVSQD---VVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 N--VYQNIVLPielDGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILADE 168
Cdd:TIGR02203 419 NdtIANNIAYG---RTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 169 PTGNLDSKTSLEVMQLLK--MTstefGQTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:TIGR02203 496 ATSALDNESERLVQAALErlMQ----GRTTLVIAHRLSTIEKADRIVVMDDGRIVER 548
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-223 |
2.76e-31 |
|
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: 114.64 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 12 KYYGQEPNItkaLDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFV 91
Cdd:cd03251 9 RYPGDGPPV---LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNynlvPIL---NVYQNIVLpieldGNT-IDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARA 156
Cdd:cd03251 82 SQD----VFLfndTVAENIAY-----GRPgATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 157 LASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
12-222 |
3.27e-31 |
|
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: 114.51 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 12 KYYGQEPNItkaLDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFV 91
Cdd:cd03252 9 RYKPDGPVI---LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNyNLVPILNVYQNIVLPIEldgnTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASK 160
Cdd:cd03252 82 LQE-NVLFNRSIRDNIALADP----GMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQllKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMR--NMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-223 |
4.05e-31 |
|
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: 114.17 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 6 ETKNLKKYYGQEPNItKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrR 85
Cdd:cd03249 2 EFKNVSFRYPSRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 86 RNIGFVFQNynlvPIL---NVYQNIVLPIeldgNTIDRTYVDKIIHLLHLEEKLDNLPNN-----------LSGGQQQRV 151
Cdd:cd03249 77 SQIGLVSQE----PVLfdgTIAENIRYGK----PDATDEEVEEAAKKANIHDFIMSLPDGydtlvgergsqLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 152 AIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQ 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-220 |
6.26e-31 |
|
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: 118.99 E-value: 6.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrrRNIGFVFQNYNLVPiLNV 103
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELFP-GTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 104 YQNIVlpiELDGNTIDRtyvdKIIH---LLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILADEP 169
Cdd:TIGR01842 409 AENIA---RFGENADPE----KIIEaakLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517425933 170 TGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQIADRMIHIEDGKI 220
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-222 |
7.35e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 115.96 E-value: 7.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYG---------QEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGK 74
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 75 MNDEQLTVfRRRNIGFVFQN--YNLVPILNVYQNIVLPIELDGNTIDRTYV-DKIIHLLHLEEKLDNL----PNNLSGGQ 147
Cdd:PRK15079 88 MKDDEWRA-VRSDIQMIFQDplASLNPRMTIGEIIAEPLRTYHPKLSRQEVkDRVKAMMLKVGLLPNLinryPHEFSGGQ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 148 QQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHnpELA---QIADRMIHIEDGKIVE 222
Cdd:PRK15079 167 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAH--DLAvvkHISDRVLVMYLGHAVE 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-221 |
8.25e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 114.31 E-value: 8.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrRRNIGFVFQNYNL 97
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGI---RKLVGIVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 VPILNVY--------QNIVL-PIELdgntidRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADE 168
Cdd:PRK13644 89 QFVGRTVeedlafgpENLCLpPIEI------RKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517425933 169 PTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-221 |
1.28e-30 |
|
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: 117.93 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNYNLVPIlNV 103
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL----GRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 104 YQNIVLPIELDgntidrtyVDKIIH---LLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILADEP 169
Cdd:COG4618 423 AENIARFGDAD--------PEKVVAaakLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 170 TGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-220 |
1.57e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 7 TKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIR-GKEIGKMN-----DEQL 80
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLPqepplDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVFrrrniGFVFQNYN-LVPILNVYQNIVLPI------------------ELDGNTIDRTyVDKIIHLLHL-EEKLDNLP 140
Cdd:COG0488 77 TVL-----DTVLDGDAeLRALEAELEELEAKLaepdedlerlaelqeefeALGGWEAEAR-AEEILSGLGFpEEDLDRPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 141 NNLSGGQQQRVAIARALASKPAIILADEPTGNLD--SKTSLEvmQLLKmtstEFGQTLVMITHNPE-LAQIADRMIHIED 217
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDleSIEWLE--EFLK----NYPGTVLVVSHDRYfLDRVATRILELDR 224
|
...
gi 517425933 218 GKI 220
Cdd:COG0488 225 GKL 227
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-222 |
2.27e-30 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 112.62 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:TIGR02323 3 LLQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNI-----GFVFQNynlvpilnVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEE--------------KLDNLPNNLS 144
Cdd:TIGR02323 79 ERRRLmrtewGFVHQN--------PRDGLRMRVSAGANIGERLMAIGARHYGNIRAtaqdwleeveidptRIDDLPRAFS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 145 GGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVVE 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
3.58e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 113.02 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYgqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI-----GKMN 76
Cdd:PRK13636 3 DYILKVEELNYNY---SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 deqltvfRRRNIGFVFQNY-NLVPILNVYQNI---VLPIELDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVA 152
Cdd:PRK13636 80 -------LRESVGMVFQDPdNQLFSASVYQDVsfgAVNLKLPEDEVRKR-VDNALKRTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 153 IARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQI-ADRMIHIEDGKIV 221
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLyCDNVFVMKEGRVI 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-220 |
8.06e-30 |
|
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: 109.06 E-value: 8.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKkyygqepnITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvF 83
Cdd:cd03215 4 VLEVRGLS--------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFV---FQNYNLVPILNVYQNIVLPIELdgntidrtyvdkiihllhleekldnlpnnlSGGQQQRVAIARALASK 160
Cdd:cd03215 73 IRAGIAYVpedRKREGLVLDLSVAENIALSSLL------------------------------SGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMI-THNPELAQIADRMIHIEDGKI 220
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLIsSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-222 |
8.15e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.36 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPN-----ITKALD----------GIDVK-----VEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGS 64
Cdd:PRK10070 5 LEIKNLYKIFGEHPQrafkyIEQGLSkeqilektglSLGVKdaslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 65 VKIRGKEIGKMNDEQLTVFRRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNN 142
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEerREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 143 LSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVV 244
|
.
gi 517425933 222 E 222
Cdd:PRK10070 245 Q 245
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-220 |
1.10e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 111.26 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL---DIPSSGSVKIRGKEIGKMND 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 78 EQLTVFRRR-NIGFVFQNYNLVPILNVYQNIVLPiELDGNTIDRTYVdKIIHLLHLEEKLDNLP------------NNLS 144
Cdd:PRK09984 77 LARDIRKSRaNTGYIFQQFNLVNRLSVLENVLIG-ALGSTPFWRTCF-SWFTREQKQRALQALTrvgmvhfahqrvSTLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 145 GGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKI 220
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHV 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-221 |
2.03e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.25 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfR 84
Cdd:PRK13548 3 LEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RR-------NIGFVFqnynLVpilnvyQNIV----LPIELdGNTIDRTYVDKIIH---LLHLEEKLdnLPNnLSGGQQQR 150
Cdd:PRK13548 77 RRavlpqhsSLSFPF----TV------EEVVamgrAPHGL-SRAEDDALVAAALAqvdLAHLAGRD--YPQ-LSGGEQQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 151 VAIARALA------SKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:PRK13548 143 VQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAaRYADRIVLLHQGRLV 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-222 |
2.09e-29 |
|
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: 108.17 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKkyYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfR 84
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNynlvpilnvyqnivlpIELDGNTIdrtyvdkiihllhleekLDNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:cd03247 74 SSLISVLNQR----------------PYLFDTTL-----------------RNNLGRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLkMTSTEfGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLI-FEVLK-DKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-223 |
2.35e-29 |
|
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: 108.84 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKmNDEQLtvfr 84
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEAL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 rRNIGFVFQNYNLVPILNVYQNIVLPIELDGntIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:cd03268 72 -RRIGALIEAPGFYPNLTARENLRLLARLLG--IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLkMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVER 223
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELI-LSLRDQGITVLISSHLlSEIQKVADRIGIINKGKLIEE 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-222 |
2.42e-29 |
|
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: 114.13 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDI--PSSGSV----------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 66 ------KIRGKEIGKMN------DEQLTVFRRRNIGFVFQ-NYNLVPILNVYQNIVLPIELDG----NTIDRTYvdKIIH 128
Cdd:TIGR03269 77 kvgepcPVCGGTLEPEEvdfwnlSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGyegkEAVGRAV--DLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 129 LLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPE-LAQ 207
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEvIED 234
|
250
....*....|....*
gi 517425933 208 IADRMIHIEDGKIVE 222
Cdd:TIGR03269 235 LSDKAIWLENGEIKE 249
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-221 |
3.90e-29 |
|
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: 108.43 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVsIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvFR 84
Cdd:cd03264 1 LQLENLTKRYGK----KRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRnIGFVFQNYNLVPILNVYQNIVLPIELDG--NTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:cd03264 72 RR-IGYLPQEFGVYPNFTVREFLDYIAWLKGipSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLkmtsTEFGQTLVMI--THNPE-LAQIADRMIHIEDGKIV 221
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLL----SELGEDRIVIlsTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-210 |
6.56e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.10 E-value: 6.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLL---NMLGGLdIPS---SGSVKIRGKEIGKM 75
Cdd:PRK14243 8 ETVLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDL-IPGfrvEGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 NDEQLTVfrRRNIGFVFQNYNLVPiLNVYQNIVLPIELDGNTID-RTYVDKIIHLLHL----EEKLDNLPNNLSGGQQQR 150
Cdd:PRK14243 83 DVDPVEV--RRRIGMVFQKPNPFP-KSIYDNIAYGARINGYKGDmDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 151 VAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFgqTLVMITHN-PELAQIAD 210
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNmQQAARVSD 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-221 |
8.10e-29 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 108.19 E-value: 8.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrrRNIGFVFQN-----YNL 97
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-----RRIGVVFGQktqlwWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 VPI--LNVYQNI--VLPIELdgntidRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNL 173
Cdd:cd03267 111 PVIdsFYLLAAIydLPPARF------KKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517425933 174 DSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRLL 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-211 |
9.70e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.55 E-value: 9.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigkmndeqltvfrrRNIGFVFQNYNLV---P 99
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------------ARVAYVPQRSEVPdslP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 I-------LNVYQNIVLPIELDGNtiDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGN 172
Cdd:NF040873 72 LtvrdlvaMGRWARRGLWRRLTRD--DRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 517425933 173 LDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQIADR 211
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADP 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-222 |
9.97e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.10 E-value: 9.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI-GKMNDEQLTVFRRRnIGFVFQnynlVP- 99
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRKR-IGMVFQ----FPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 -----------ILNVYQNIVLPIEldgNTIDRTYvDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADE 168
Cdd:PRK13646 96 sqlfedtvereIIFGPKNFKMNLD---EVKNYAH-RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 169 PTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-221 |
1.64e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.89 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfRRR-------NIGFVFqnyn 96
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA--RRRavlpqhsSLAFPF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 97 lvpilNVYQnIVLpIELDGNTIDRTYVDKIIH-------LLHLEEKLdnlPNNLSGGQQQRVAIARALA-------SKPA 162
Cdd:COG4559 91 -----TVEE-VVA-LGRAPHGSSAAQDRQIVRealalvgLAHLAGRS---YQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLK-MTSTEFGqtLVMITHNPEL-AQIADRMIHIEDGKIV 221
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARqLARRGGG--VVAVLHDLNLaAQYADRILLLHQGRLV 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-222 |
2.04e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 107.83 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL------DIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNYNL 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKL----RKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 VPILNVYQNIVLPIELDGnTIDRTYVDKIIH--------LLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEP 169
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHG-IKEKREIKKIVEeclrkvglWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517425933 170 TGNLDSKTSLEVMQLLKMTSTEFgqTLVMITHNP-ELAQIADRMIHIEDGKIVE 222
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPqQVARVADYVAFLYNGELVE 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-221 |
2.24e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 108.29 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRRNIGFVFQnynlVPIL 101
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 NVYQNIVLP-----------IELDGNTIDRtyvdKIIHLLHLEEKL-DNLPNNLSGGQQQRVAIARALASKPAIILADEP 169
Cdd:PRK13649 97 QLFEETVLKdvafgpqnfgvSQEEAEALAR----EKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517425933 170 TGNLDSKTSLEVMQLLKMTStEFGQTLVMITH-NPELAQIADRMIHIEDGKIV 221
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHlMDDVANYADFVYVLEKGKLV 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-210 |
2.82e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 107.43 E-value: 2.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYgqepNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDiPSSGSVKIRGK-EIGKMN--DEQLT 81
Cdd:PRK14258 8 IKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGRvEFFNQNiyERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 82 VFR-RRNIGFVFQNYNLVPiLNVYQNIVL---------PIELDG----NTIDRTYVDKIIHLLHlEEKLDnlpnnLSGGQ 147
Cdd:PRK14258 83 LNRlRRQVSMVHPKPNLFP-MSVYDNVAYgvkivgwrpKLEIDDivesALKDADLWDEIKHKIH-KSALD-----LSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 148 QQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIAD 210
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSD 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-221 |
3.33e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.02 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvf 83
Cdd:PRK11231 2 TLRTENLTVGYGT----KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rrRNIGFVFQN--------------YNLVPILNVYQNIvlpieldgNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQ 149
Cdd:PRK11231 76 --RRLALLPQHhltpegitvrelvaYGRSPWLSLWGRL--------SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQAsRYCDHLVVLANGHVM 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-222 |
4.10e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.07 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:PRK11160 339 LTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNynlVPILN--VYQNIVLPIEldgNTIDrtyvDKIIHLLH---LEEKLDNLP----------NNLSGGQQQ 149
Cdd:PRK11160 413 RQAISVVSQR---VHLFSatLRDNLLLAAP---NASD----EALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKmtstEFGQ--TLVMITHN-PELAQIaDRMIHIEDGKIVE 222
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA----EHAQnkTVLMITHRlTGLEQF-DRICVMDNGQIIE 553
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-222 |
4.14e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 108.29 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKS-TLLNMLGGLDIP---SSGSVKIRGKEIGKMNDEQ 79
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 ltvfRRRNIG----FVFQN--YNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHL------EEKLDNLPNNLSGGQ 147
Cdd:PRK11022 83 ----RRNLVGaevaMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQvgipdpASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 148 QQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKIVE 222
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQVVE 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-221 |
5.08e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.51 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 13 YYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRRNIGFVF 92
Cdd:PRK13643 11 YQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 93 QnynlVPILNVYQNIVLPIELDGNT---IDRTYVDKI----IHLLHLEEKL-DNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:PRK13643 91 Q----FPESQLFEETVLKDVAFGPQnfgIPKEKAEKIaaekLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITH-NPELAQIADRMIHIEDGKIV 221
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHII 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-222 |
1.85e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.56 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEPNITKaLDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tvfrRRNIGFVFQNY-NLVPILNVYQNIVLPIELDG----NTIDRtyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIAR 155
Cdd:PRK13642 80 ----RRKIGMVFQNPdNQFVGATVEDDVAFGMENQGipreEMIKR--VDEALLAVNMLDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 156 ALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIK 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-221 |
2.00e-27 |
|
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: 104.28 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPS---SGSVKIRGKEigkMNDEQLtvfrRRNIGFVFQNYNLV 98
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP---RKPDQF----QKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 PILNVYQ------NIVLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGN 172
Cdd:cd03234 94 PGLTVREtltytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517425933 173 LDSKTSLEVMQLLKMTSTEfGQTLVMITHNP--ELAQIADRMIHIEDGKIV 221
Cdd:cd03234 174 LDSFTALNLVSTLSQLARR-NRIVILTIHQPrsDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-227 |
3.61e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 13 YYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFR-RRNIGFV 91
Cdd:PRK13645 16 YAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlRKEIGLV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQnynlVPILNVYQNIVL------PIELdGNTIDRTYvDKIIHLLHL----EEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:PRK13645 96 FQ----FPEYQLFQETIEkdiafgPVNL-GENKQEAY-KKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 162 AIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVERKESF 227
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-222 |
4.41e-27 |
|
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: 103.34 E-value: 4.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLK-KYYGQEPNitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvf 83
Cdd:cd03244 3 IEFKNVSlRYRPNLPP---VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQN---------YNLVPiLNVYQnivlpielDG---NTIDRTYVDKII--HLLHLEEKLDNLPNNLSGGQQQ 149
Cdd:cd03244 77 -RSRISIIPQDpvlfsgtirSNLDP-FGEYS--------DEelwQALERVGLKEFVesLPGGLDTVVEEGGENLSVGQRQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKmtsTEF-GQTLVMITHnpELAQIA--DRMIHIEDGKIVE 222
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIR---EAFkDCTVLTIAH--RLDTIIdsDRILVLDKGRVVE 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-223 |
6.20e-27 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 107.98 E-value: 6.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlvPIL-N 102
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQD----TVLfN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 103 --VYQNIVLpieldGNT-IDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILADE 168
Cdd:COG5265 446 dtIAYNIAY-----GRPdASEEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 169 PTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHnpELAQI--ADRMIHIEDGKIVER 223
Cdd:COG5265 521 ATSALDSRTERAIQAALREVAR--GRTTLVIAH--RLSTIvdADEILVLEAGRIVER 573
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-169 |
8.29e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.80 E-value: 8.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKmndeqLTVF 83
Cdd:COG1137 3 TLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH-----LPMH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RR--RNIGF------VFQNynlvpiLNVYQNIVLPIELdgNTIDRTY----VDKIIHLLHLEEKLDNLPNNLSGGQQQRV 151
Cdd:COG1137 74 KRarLGIGYlpqeasIFRK------LTVEDNILAVLEL--RKLSKKEreerLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170
....*....|....*...
gi 517425933 152 AIARALASKPAIILADEP 169
Cdd:COG1137 146 EIARALATNPKFILLDEP 163
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-203 |
1.64e-26 |
|
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: 106.29 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:TIGR02868 335 LELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPIlNVYQNIVLPielDGNTIDrtyvDKIIHLLH---LEEKLDNLPNNL-----------SGGQQQR 150
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDT-TVRENLRLA---RPDATD----EELWAALErvgLADWLRALPDGLdtvlgeggarlSGGERQR 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517425933 151 VAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNP 203
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-223 |
1.65e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.58 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNYNL 97
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 vpiLN--VYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLP-------NNLSGGQQQRVAIARALASKPAIILADE 168
Cdd:PRK13657 421 ---FNrsIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 169 PTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHnpELAQI--ADRMIHIEDGKIVER 223
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMK--GRTTFIIAH--RLSTVrnADRILVFDNGRVVES 550
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-221 |
3.39e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 103.24 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYY---GQEPN--------------ITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVK 66
Cdd:COG4586 1 IIEVENLSKTYrvyEKEPGlkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 67 IRGkeigkmndeqLTVFRRR-----NIGFVFQN-----YNLVPI--LNVYQNIVlpiELDGNTIDRTyVDKIIHLLHLEE 134
Cdd:COG4586 81 VLG----------YVPFKRRkefarRIGVVFGQrsqlwWDLPAIdsFRLLKAIY---RIPDAEYKKR-LDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 135 KLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPE-LAQIADRMI 213
Cdd:COG4586 147 LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdIEALCDRVI 226
|
....*...
gi 517425933 214 HIEDGKIV 221
Cdd:COG4586 227 VIDHGRII 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-224 |
6.90e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 6.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmndEQLTVF 83
Cdd:PRK13537 7 PIDFRNVEKRYGD----KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFVFQNYNLVPILNVYQNIVL---PIELDGNTIdRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVfgrYFGLSAAAA-RALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHIEDG-KIVERK 224
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAErLCDRLCVIEEGrKIAEGA 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-221 |
7.59e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 99.66 E-value: 7.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigkmndeQLTVFR 84
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK--------PLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEeaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 163 IILADEPTGNLDSkTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIV 221
Cdd:cd03269 149 LLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEeLCDRVLLLNKGRAV 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-219 |
1.39e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.06 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrRRNIGFVFQNYNLVPILN 102
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 103 VYQNIVLPIELDGNT--------------IDRTYVDKIIHLLH---LEEKLDNLPNNLSGGQQQRVAIARALASKPAIIL 165
Cdd:PRK11300 97 VIENLLVAQHQQLKTglfsgllktpafrrAESEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 166 ADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGK 219
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMgISDRIYVVNQGT 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
3.51e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.44 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLK-KYYGQEPnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:PRK13648 5 NSIIVFKNVSfQYQSDAS---FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tvfrRRNIGFVFQNynlvPILNVYQNIV---LPIELDGNTID----RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAI 153
Cdd:PRK13648 82 ----RKHIGIVFQN----PDNQFVGSIVkydVAFGLENHAVPydemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 154 ARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-218 |
4.29e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKI-RGKEIgkMndeqltvfrrrnigFVFQN-YnlVPIL 101
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV--L--------------FLPQRpY--LPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 NVYQNIVLPieLDGNTIDRTYVDKIIH---LLHLEEKLD---NLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDS 175
Cdd:COG4178 441 TLREALLYP--ATAEAFSDAELREALEavgLGHLAERLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517425933 176 KTSLEVMQLLKmtSTEFGQTLVMITHNPELAQIADRMIHIEDG 218
Cdd:COG4178 519 ENEAALYQLLR--EELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-222 |
4.30e-25 |
|
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: 97.87 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGqePNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:cd03369 7 IEVENLSVRYA--PDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNynlvpilnvyqnivlPIELDG---NTIDR--TYVD-KIIHLLHLEEKldnlPNNLSGGQQQRVAIARALA 158
Cdd:cd03369 81 RSSLTIIPQD---------------PTLFSGtirSNLDPfdEYSDeEIYGALRVSEG----GLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKmtsTEF-GQTLVMITHnpELAQIA--DRMIHIEDGKIVE 222
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIR---EEFtNSTILTIAH--RLRTIIdyDKILVMDAGEVKE 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-222 |
5.27e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKiRGKeigkmndeqlTVf 83
Cdd:COG0488 315 VLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGE----------TV- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rrrNIGFVFQNY-NLVPILNVYQNI--VLPielDGNTID-RTY----------VDKIIHllhleekldnlpnNLSGGQQQ 149
Cdd:COG0488 379 ---KIGYFDQHQeELDPDKTVLDELrdGAP---GGTEQEvRGYlgrflfsgddAFKPVG-------------VLSGGEKA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 150 RVAIARALASKPAIILADEPTGNLD--SKTSLEvmQLLKmtstEFGQTLVMITHNPE-LAQIADRMIHIEDGKIVE 222
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDieTLEALE--EALD----DFPGTVLLVSHDRYfLDRVATRILEFEDGGVRE 509
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-219 |
9.26e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.16 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPS---SGSVKIRGKEIGKMN- 76
Cdd:PRK13549 2 MEYLLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 -DEQltvfrRRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTI---DRTYV--DKIIHLLHLEEKLDNLPNNLSGGQQQR 150
Cdd:PRK13549 77 rDTE-----RAGIAIIHQELALVKELSVLENIFLGNEITPGGImdyDAMYLraQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 151 VAIARALASKPAIILADEPTGNL-DSKTS--LEVMQLLKmtstEFGQTLVMITHN-PELAQIADRMIHIEDGK 219
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLtESETAvlLDIIRDLK----AHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-221 |
1.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.33 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQEPNitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIP---SSGSVKIRGKEIGkmnde 78
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLT----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 79 QLTVFR-RRNIGFVFQNY-NLVPILNVYQNIVLPIELDGntIDRTYVDKIIHL----LHLEEKLDNLPNNLSGGQQQRVA 152
Cdd:PRK13640 76 AKTVWDiREKVGIVFQNPdNQFVGATVGDDVAFGLENRA--VPRPEMIKIVRDvladVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 153 IARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-222 |
1.20e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.03 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPS---SGSVKIRGKEIGKMND 77
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 78 EQLTVFRRRNIGFVFQN--YNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLL------HLEEKLDNLPNNLSGGQQQ 149
Cdd:PRK09473 89 KELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLdavkmpEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGRTME 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-221 |
2.67e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLkkyygqepNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmndeqltvf 83
Cdd:COG1129 256 VLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV----------- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNI------GFVF-----QNYNLVPILNVYQNIVLPIeLD----GNTID----RTYVDKIIHLLHLeeK---LDNLPN 141
Cdd:COG1129 317 RIRSPrdairaGIAYvpedrKGEGLVLDLSIRENITLAS-LDrlsrGGLLDrrreRALAEEYIKRLRI--KtpsPEQPVG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 142 NLSGGQQQRVAIARALASKPAIILADEPTGNLD--SKTslEVMQLLK----------MTSTEFgqtlvmithnPELAQIA 209
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKA--EIYRLIRelaaegkaviVISSEL----------PELLGLS 461
|
250
....*....|..
gi 517425933 210 DRMIHIEDGKIV 221
Cdd:COG1129 462 DRILVMREGRIV 473
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-223 |
2.72e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.16 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKS-TLLNMLGGLDIPS----SGSVKIRGKEIGKMNDE 78
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 79 QLTVFRRRNIGFVFQN--YNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLL------HLEEKLDNLPNNLSGGQQQR 150
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLdrvgirQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 151 VAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIVER 223
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQ 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-222 |
6.21e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.16 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKST-------LLNMLGGLdiPSSGSVKIRGK-----E 71
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGL--VQCDKMLLRRRsrqviE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 72 IGKMNDEQLTVFRRRNIGFVFQN--YNLVPILNVYQNIVLPIEL-DGNTIDRTYVD--KIIHLLHLEEK---LDNLPNNL 143
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEakRMLDQVRIPEAqtiLSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 144 SGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGEAVE 249
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-222 |
6.97e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.53 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGK-----EIGK-MNDEqLTVfrRRNIGFVFQnyn 96
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallELGAgFHPE-LTG--RENIYLNGR--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 97 lvpILNvyqnivlpieLDGNTIDRtYVDKIIHLLHLEEKLDnLP-NNLSGGQQQRVAIARALASKPAIILADEPTGNLDS 175
Cdd:COG1134 115 ---LLG----------LSRKEIDE-KFDEIVEFAELGDFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517425933 176 ---KTSLEVMQllkmtstEF---GQTLVMITHNPE-LAQIADRMIHIEDGKIVE 222
Cdd:COG1134 180 afqKKCLARIR-------ELresGRTVIFVSHSMGaVRRLCDRAIWLEKGRLVM 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-221 |
1.42e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.22 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 25 DGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRRnIGFVFQNYNLVPILNVY 104
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 105 QNIVLPIELDGN---TIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEV 181
Cdd:PRK11831 103 DNVAYPLREHTQlpaPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517425933 182 MQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIV 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-222 |
1.49e-23 |
|
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: 94.14 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGK-----EIGkmndeqltvfrrrnIGFvfqnynl 97
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllGLG--------------GGF------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 VPILNVYQNIVLPIELDGNTID--RTYVDKIIHLLHLEEKLDnLP-NNLSGGQQQRVAIARALASKPAIILADEPTGNLD 174
Cdd:cd03220 96 NPELTGRENIYLNGRLLGLSRKeiDEKIDEIIEFSELGDFID-LPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517425933 175 SKTSLEVMQLLK-MTSTefGQTLVMITHNPE-LAQIADRMIHIEDGKIVE 222
Cdd:cd03220 175 AAFQEKCQRRLReLLKQ--GKTVILVSHDPSsIKRLCDRALVLEKGKIRF 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-221 |
1.75e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 94.52 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPSSGSVKIRGKEIGKMNDEQLTVFRrrniGFVFQNYNLVPILNV 103
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 104 YQNIVL--PIELDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA-------SKPAIILADEPTGNLD 174
Cdd:COG4138 87 FQYLALhqPAGASSEAVEQL-LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 175 SKTSLEVMQLLKmtstEF---GQTLVMITH--NPELAQiADRMIHIEDGKIV 221
Cdd:COG4138 166 VAQQAALDRLLR----ELcqqGITVVMSSHdlNHTLRH-ADRVWLLKQGKLV 212
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-222 |
1.93e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.87 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlvPIL-- 101
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQE----PVLfs 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 -NVYQNIvlpieldGNTIDRTYVDKII---HLLHLEEKLDNLPNN-----------LSGGQQQRVAIARALASKPAIILA 166
Cdd:TIGR00958 569 gSVRENI-------AYGLTDTPDEEIMaaaKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 167 DEPTGNLDSktslEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:TIGR00958 642 DEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-225 |
2.20e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKST----LLNMlggldIPSSGSVKIRGKEIGKMNDEQLTVFRRRnIGFVFQNYN-- 96
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRL-----INSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 97 LVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEKLD-----NLPNNLSGGQQQRVAIARALASKPAIILADEPTG 171
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDpetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 172 NLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVERKE 225
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRaLCHQVIVLRQGEVVEQGD 509
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-223 |
4.09e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 96.71 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlvPIL-- 101
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQD----PVVla 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 -NVYQNIVLpieldGNTIDRTYVDKIIHLLHLEEKLDNLP-----------NNLSGGQQQRVAIARALASKPAIILADEP 169
Cdd:PRK10790 429 dTFLANVTL-----GRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 170 TGNLDSKTSLEVMQLLKMTSTEfgQTLVMITHnpELAQI--ADRMIHIEDGKIVER 223
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH--TTLVVIAH--RLSTIveADTILVLHRGQAVEQ 555
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-215 |
7.02e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.47 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 21 TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlvPI 100
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQT----PT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 101 L---NVYQNIVLPIELDGNTIDRTYVDKIIHLLHL-EEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSK 176
Cdd:PRK10247 92 LfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 517425933 177 TSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHI 215
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-221 |
8.15e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNML-----GGLDIpsSGSVKIRGKeigKMNDEQLtvfrRRNIGFVFQNYNLV 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrspKGVKG--SGSVLLNGM---PIDAKEM----RAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 PILNVYQNIVLPIEL-----DGNTIDRTYVDKIIHLLHLEEKLD------NLPNNLSGGQQQRVAIARALASKPAIILAD 167
Cdd:TIGR00955 112 PTLTVREHLMFQAHLrmprrVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 168 EPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNP--ELAQIADRMIHIEDGKIV 221
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQPssELFELFDKIILMAEGRVA 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-221 |
9.37e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 92.74 E-value: 9.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 27 IDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrrRNIGFVFQNYNLVPILNVyQN 106
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDITV-QE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 107 IVL-------PIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSL 179
Cdd:PRK10253 101 LVArgryphqPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517425933 180 EVMQLLKMTSTEFGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIV 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-220 |
9.59e-23 |
|
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: 92.15 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNiTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvf 83
Cdd:cd03248 11 IVKFQNVTFAYPTRPD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQNynlvPIL---NVYQNIV-----LPIELDGNTIDRTYVDKIIHLLHLE--EKLDNLPNNLSGGQQQRVAI 153
Cdd:cd03248 87 -HSKVSLVGQE----PVLfarSLQDNIAyglqsCSFECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 154 ARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfgQTLVMITHNPELAQIADRMIHIEDGKI 220
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-203 |
2.31e-22 |
|
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: 90.00 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKkYYGQEPNITKA-LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPS--SGSVKIRGKEIGKmndeql 80
Cdd:cd03232 3 VLTWKNLN-YTVPVKGGKRQlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tVFRRRnIGFVFQNYNLVPILNVYQNIVLPIELDGntidrtyvdkiihllhleekldnlpnnLSGGQQQRVAIARALASK 160
Cdd:cd03232 76 -NFQRS-TGYVEQQDVHSPNLTVREALRFSALLRG---------------------------LSVEQRKRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNP 203
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQP 168
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
4.62e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmNDEQL 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVFRRRNIGFVFQNYNLVPILNVYQNIVlpieLDGNTIDRT-YVDKIIHLL----HLEEKLDNLPNNLSGGQQQRVAIAR 155
Cdd:PRK11614 75 AKIMREAVAIVPEGRRVFSRMTVEENLA----MGGFFAERDqFQERIKWVYelfpRLHERRIQRAGTMSGGEQQMLAIGR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 156 ALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQAlKLADRGYVLENGHVV 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-222 |
5.00e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.77 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRrNIGFVFQN--YNLVPI 100
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 101 LNVYQNIVLPIELDGNTIDRTYVDKIIHLLH----LEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSK 176
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAAARVAWLLErvglLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517425933 177 TSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKIVE 222
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVErISHRVAVMYLGQIVE 544
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-221 |
6.73e-22 |
|
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: 93.35 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPS---SGSVKIRGKEIGKMNdeqL 80
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASN---I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVFRRRNIGFVFQNYNLVPILNVYQNIVL--PIELDGNTIDRTYVDKIIHLLHLEEKLDNLPN-----NLSGGQQQRVAI 153
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtrpvgDYGGGQQQLVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 154 ARALASKPAIILADEPTGNLDSKTS---LEVMQLLKmtstEFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETeilLDIIRDLK----AHGVACVYISHKlNEVKAVCDTICVIRDGQHV 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-220 |
6.93e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 21 TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrRRnigfvfqnynlvpI 100
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RR-------------V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 101 LNVYQNIVLPIELDGNTI------------------DRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPA 162
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVvemgrtphrsrfdtwtetDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKI 220
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVR-RLVDDGKTAVAAIHDLDLaARYCDELVLLADGRV 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-219 |
8.68e-22 |
|
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: 87.12 E-value: 8.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKiRGKEIgkmndeqltvfr 84
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-WGSTV------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 rrNIGFVFQnynlvpilnvyqnivlpieldgntidrtyvdkiihllhleekldnlpnnLSGGQQQRVAIARALASKPAII 164
Cdd:cd03221 64 --KIGYFEQ-------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 165 LADEPTGNLD--SKTSLEvmQLLKmtstEFGQTLVMITHNPE-LAQIADRMIHIEDGK 219
Cdd:cd03221 93 LLDEPTNHLDleSIEALE--EALK----EYPGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-221 |
1.01e-21 |
|
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: 88.47 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 8 KNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL---DIPSSGSVKIRGKEIGKMNDeqltvFR 84
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAE-----KY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRtyvdkiihllhleekldnlpnNLSGGQQQRVAIARALASKPAII 164
Cdd:cd03233 82 PGEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVR---------------------GISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITH--NPELAQIADRMIHIEDGKIV 221
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-221 |
1.10e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMndeQLTVF 83
Cdd:PRK10895 3 TLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---PLHAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNIGFVFQNYNLVPILNVYQNI--VLPIELDGNTIDRT-YVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:PRK10895 76 ARRGIGYLPQEASIFRRLSVYDNLmaVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNvRETLAVCERAYIVSQGHLI 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-223 |
1.61e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.46 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEPNI-----TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIrgkeigkm 75
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 NDEQLTV----FRRRNIGFVFQN--YNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLH----LEEKLDNLPNNLSG 145
Cdd:PRK15112 73 DDHPLHFgdysYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRqvglLPDHASYYPHMLAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 146 GQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMIT-HNPELAQIADRMIHIEDGKIVER 223
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEVVER 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-221 |
3.47e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGqepnITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMnDEQLTVfr 84
Cdd:PRK09700 6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYNLVPILNVYQNIV---LPIE--LDGNTID----RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIAR 155
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYigrHLTKkvCGVNIIDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 156 ALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKlAEIRRICDRYTVMKDGSSV 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-222 |
4.18e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.50 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmnDEQLTVFR 84
Cdd:PRK13536 42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRnIGFVFQNYNLVPILNVYQNIVL---PIELDGNTIDrTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKP 161
Cdd:PRK13536 114 AR-IGVVPQFDNLDLEFTVRENLLVfgrYFGMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 162 AIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IADRMIHIEDG-KIVE 222
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAErLCDRLCVLEAGrKIAE 253
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-222 |
5.10e-21 |
|
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: 90.95 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlvPIL 101
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL----RQFINYLPQE----PYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 ---NVYQNIVLPIElDGNTIDRtyVDKIIHLLHLEEKLDNLP-----------NNLSGGQQQRVAIARALASKPAIILAD 167
Cdd:TIGR01193 560 fsgSILENLLLGAK-ENVSQDE--IWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 168 EPTGNLDSKTSLEVMQ-LLKMTStefgQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNnLLNLQD----KTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-217 |
1.41e-20 |
|
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: 84.51 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEigkmndeqltvfrrrNIGFVFQnynlvpilnv 103
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------DLLFLPQ---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 104 yqnivlpieldgntidRTYV------DKIIHLLHLEekldnlpnnLSGGQQQRVAIARALASKPAIILADEPTGNLDSKT 177
Cdd:cd03223 72 ----------------RPYLplgtlrEQLIYPWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517425933 178 SLEVMQLLKmtstEFGQTLVMITHNPELAQIADRMIHIED 217
Cdd:cd03223 127 EDRLYQLLK----ELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-219 |
1.84e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 89.17 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 9 NLKKYYGQEPNITKA---------LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGldipssgsvKIRGKEI-GKM--N 76
Cdd:PLN03211 60 NIKRILGHKPKISDEtrqiqertiLNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---------RIQGNNFtGTIlaN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 DEQLTVFRRRNIGFVFQNYNLVPILNVYQNIV------LPIELDGNtiDRTYV-DKIIHLLHLEEKLDNLPNN-----LS 144
Cdd:PLN03211 131 NRKPTKQILKRTGFVTQDDILYPHLTVRETLVfcsllrLPKSLTKQ--EKILVaESVISELGLTKCENTIIGNsfirgIS 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 145 GGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLkMTSTEFGQTLVMITHNP--ELAQIADRMIHIEDGK 219
Cdd:PLN03211 209 GGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL-GSLAQKGKTIVTSMHQPssRVYQMFDSVLVLSEGR 284
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-223 |
3.16e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.54 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYY-GQEpniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL-DIpSSGSVKIRGKEIgkmNDEQLTV 82
Cdd:PRK11176 342 IEFRNVTFTYpGKE---VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFyDI-DEGEILLDGHDL---RDYTLAS 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 FRRrNIGFVFQNynlVPILN--VYQNIVLPIEldgNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQ 149
Cdd:PRK11176 415 LRN-QVALVSQN---VHLFNdtIANNIAYART---EQYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQ 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKT------SLEVMQLLKmtstefgqTLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESeraiqaALDELQKNR--------TSLVIAHRLSTIEKADEILVVEDGEIVER 559
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-222 |
3.61e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.30 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLD-----IPSSGSVKIRGKEIgkMNDEQLTVFRRRnIGFVFQNYNLV 98
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSI--FNYRDVLEFRRR-VGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 PiLNVYQNIVLPI---------ELDGntIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEP 169
Cdd:PRK14271 114 P-MSIMDNVLAGVrahklvprkEFRG--VAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517425933 170 TGNLDSKTSLEVMQLLKMTSTEFgqTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRL--TVIIVTHNlAQAARISDRAALFFDGRLVE 242
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-222 |
1.40e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmndeqltVFRR------RNIGFVFQNY 95
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM---------RFASttaalaAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 96 NLVPILNVYQNIVL---PIEldGNTIDRT--YVDKIIHLLHLEEKLDnlPN----NLSGGQQQRVAIARALASKPAIILA 166
Cdd:PRK11288 89 HLVPEMTVAENLYLgqlPHK--GGIVNRRllNYEAREQLEHLGVDID--PDtplkYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 167 DEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRmEEIFALCDAITVFKDGRYVA 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-218 |
1.80e-19 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 86.70 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGG---LDIPSSGSVKIRGKEIgkmnDEQltvFRRRnIGFVFQNYNLVPI 100
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPL----DSS---FQRS-IGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 101 LNVYQNIV------LPIELDGNTIDRtYVDKIIHLLHLEEKLDNLPN----NLSGGQQQRVAIARALASKPAIIL-ADEP 169
Cdd:TIGR00956 851 STVRESLRfsaylrQPKSVSKSEKME-YVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517425933 170 TGNLDSKTSLEVMQLLKMTStEFGQTLVMITHNPE--LAQIADRMIHIEDG 218
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-216 |
2.08e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMN-DEQLTVF 83
Cdd:PRK13539 3 LEGEDLACVRGGRV----LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRNigfvfqnyNLVPILNVYQNIVLPIELDGNtidrtyvdkiiHLLHLEEKLD--------NLP-NNLSGGQQQRVAIA 154
Cdd:PRK13539 79 GHRN--------AMKPALTVAENLEFWAAFLGG-----------EELDIAAALEavglaplaHLPfGYLSAGQKRRVALA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 155 RALASKPAIILADEPTGNLDSKTS---LEVMQllkmTSTEFGQTLVMITHNPeLAQIADRMIHIE 216
Cdd:PRK13539 140 RLLVSNRPIWILDEPTAALDAAAValfAELIR----AHLAQGGIVIAATHIP-LGLPGARELDLG 199
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-222 |
2.30e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 86.00 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYgqePNItKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL--------DIPSSGSV----KIRGKE 71
Cdd:NF040905 1 ILEMRGITKTF---PGV-KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGEVcrfkDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 72 igkmndeqltvfrRRNIGFVFQNYNLVPILNVYQNIVLpieldGNTI--------DRTYVdKIIHLLH---LEEKLDNLP 140
Cdd:NF040905 77 -------------ALGIVIIHQELALIPYLSIAENIFL-----GNERakrgvidwNETNR-RARELLAkvgLDESPDTLV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 141 NNLSGGQQQRVAIARALASKPAIILADEPTGNL---DSKTSLEVMQLLKmtstEFGQTLVMITH--NpELAQIADRMIHI 215
Cdd:NF040905 138 TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSAALLDLLLELK----AQGITSIIISHklN-EIRRVADSITVL 212
|
....*..
gi 517425933 216 EDGKIVE 222
Cdd:NF040905 213 RDGRTIE 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-224 |
2.75e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYgqePNItKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIG----KMN 76
Cdd:PRK10762 1 MQALLQLKGIDKAF---PGV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 DEQltvfrrrNIGFVFQNYNLVPILNVYQNIVLPIELDG--NTID--RTY--VDKIIHLLHLEEKLDNLPNNLSGGQQQR 150
Cdd:PRK10762 77 QEA-------GIGIIHQELNLIPQLTIAENIFLGREFVNrfGRIDwkKMYaeADKLLARLNLRFSSDKLVGELSIGEQQM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 151 VAIARALASKPAIILADEPTgnlDSKTSLEVMQLLKMTS--TEFGQTLVMITHN-PELAQIADRMIHIEDGK-IVERK 224
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPT---DALTDTETESLFRVIRelKSQGRGIVYISHRlKEIFEICDDVTVFRDGQfIAERE 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-215 |
3.27e-19 |
|
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: 82.02 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfRRRNIGFVFQNYNLVPILN 102
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 103 VYQNIVLPIELDGNTiDRTYVDKI--IHLLHLEekldNLP-NNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSL 179
Cdd:TIGR01189 90 ALENLHFWAAIHGGA-QRTIEDALaaVGLTGFE----DLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 517425933 180 EVMQLLKmTSTEFGQTLVMITHNPeLAQIADRMIHI 215
Cdd:TIGR01189 165 LLAGLLR-AHLARGGIVLLTTHQD-LGLVEARELRL 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-220 |
4.00e-19 |
|
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: 85.84 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 8 KNLKKYYgqEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmnDEQLTVFrRRN 87
Cdd:TIGR01257 932 KNLVKIF--EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAV-RQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 88 IGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRTYV--DKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIIL 165
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLemEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 166 ADEPTGNLDSKTSLEVMQ-LLKMTStefGQTLVMITHNPELAQI-ADRMIHIEDGKI 220
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDlLLKYRS---GRTIIMSTHHMDEADLlGDRIAIISQGRL 1138
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-222 |
1.01e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.67 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 25 DGIDVKVEPGEFVSIIGTSGSGKStlLNMLGGLDI-P-----SSGSVKIRGKEIgkmndeQLTVFRRRNIGFVFQN---- 94
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGIlPagvrqTAGRVLLDGKPV------APCALRGRKIATIMQNprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 95 YNlvPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEK---LDNLPNNLSGGQQQRVAIARALASKPAIILADEPTG 171
Cdd:PRK10418 92 FN--PLHTMHTHARETCLALGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 172 NLDSKTSLEVMQLLKMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRIVE 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-222 |
2.05e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.10 E-value: 2.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYgQEPNItkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmNDEQLTVFR 84
Cdd:PRK10522 323 LELRNVTFAY-QDNGF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRnIGFVFQNYNLVPILnvyqnivlpIELDGNTIDRTYVDKIIHLLHLEEKLD-------NLpnNLSGGQQQRVAIARAL 157
Cdd:PRK10522 397 KL-FSAVFTDFHLFDQL---------LGPEGKPANPALVEKWLERLKMAHKLEledgrisNL--KLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 158 ASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-222 |
3.70e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.86 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLN-MLGGLDIPSSGSVKIRGkeigkmndeqlTVFRRRNIGFVFQnynlvpiLN 102
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-----------TVAYVPQVSWIFN-------AT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 103 VYQNIvlpieLDGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILADEPTG 171
Cdd:PLN03130 695 VRDNI-----LFGSPFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 172 NLDSKTSLEVMQllKMTSTEFGQ-TLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PLN03130 770 ALDAHVGRQVFD--KCIKDELRGkTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-222 |
4.11e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.11 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPSSGSVK-----IRGKEIGKMNDEQLTVFRRRNIGFVFQNYN 96
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTadrfrWNGIDLLKLSPRERRKIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 97 --LVPILNVYQNI--VLP-IELDGNTIDRTYVDK--IIHLLHL------EEKLDNLPNNLSGGQQQRVAIARALASKPAI 163
Cdd:COG4170 100 scLDPSAKIGDQLieAIPsWTFKGKWWQRFKWRKkrAIELLHRvgikdhKDIMNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 164 ILADEPTGNLDSKTSLEVMQLL-KMTSTEfGQTLVMITHNPE-LAQIADRMIHIEDGKIVE 222
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLaRLNQLQ-GTSILLISHDLEsISQWADTITVLYCGQTVE 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-221 |
4.13e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvFRRRNIGFV---FQNYNLVP 99
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE---RRRLGVAYIpedRLGRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 ILNVYQNIVL------PIE----LDGNTIdRTYVDKIIhllhleEKLD------NLP-NNLSGGQQQRVAIARALASKPA 162
Cdd:COG3845 350 DMSVAENLILgryrrpPFSrggfLDRKAI-RAFAEELI------EEFDvrtpgpDTPaRSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 163 IILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDlDEILALSDRIAVMYEGRIV 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-221 |
5.64e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.59 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 31 VEPGEFVSIIGTSGSGKSTLLNMLGGLdIPSSGSVKIRGKEIGKMNDEQLTVFRrrniGFVFQNYNLVPILNVYQNIVL- 109
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQYLTLh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 110 -PielDGNTID--RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARA-LASKPAI------ILADEPTGNLD--SKT 177
Cdd:PRK03695 94 qP---DKTRTEavASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDvaQQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517425933 178 SLEvmQLLKMTStEFGQTLVMITH--NPELAQiADRMIHIEDGKIV 221
Cdd:PRK03695 171 ALD--RLLSELC-QQGIAVVMSSHdlNHTLRH-ADRVWLLKQGKLL 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-225 |
7.12e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 7.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 21 TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGG--LDIPSSGSVKIRGKEIGkmndeqltvfrrrnigfvfQNYNLV 98
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG-------------------REASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 PILNVYQNIVLPIELDGNTidrTYVDKIIHLlhleekldNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTS 178
Cdd:COG2401 104 DAIGRKGDFKDAVELLNAV---GLSDAVLWL--------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517425933 179 LEVMQLLKMTSTEFGQTLVMITHNPELAQ--IADRMIHIEDGKIVERKE 225
Cdd:COG2401 173 KRVARNLQKLARRAGITLVVATHHYDVIDdlQPDLLIFVGYGGVPEEKR 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-219 |
1.94e-17 |
|
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: 78.22 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 16 QEPNITKALDGIDVKVEPGEF-----VSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGkmndeqltvFRRRNIGF 90
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 91 VFQnynlvpiLNVYQniVLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALaSKPA-IILADEP 169
Cdd:cd03237 73 DYE-------GTVRD--LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACL-SKDAdIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517425933 170 TGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIhIEDGK 219
Cdd:cd03237 143 SAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDyLADRLI-VFEGE 192
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-222 |
2.07e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 80.23 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 27 IDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNYNLVPILnvyqn 106
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY----RQLFSAVFSDFHLFDRL----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 107 ivlpIELDGNTIDRTyVDKIIHLLHLEEKL----DNLPN-NLSGGQQQRVAIARALASKPAIILADE------P------ 169
Cdd:COG4615 422 ----LGLDGEADPAR-ARELLERLELDHKVsvedGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPefrrvf 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517425933 170 -TgnldsktslEVMQLLKmtstEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:COG4615 497 yT---------ELLPELK----ARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-221 |
2.08e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:PRK15439 11 LLCARSISKQYSGVE----VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rrrNIGFVFQNYNLVPILNVYQNIVLpiELDGNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAI 163
Cdd:PRK15439 87 ---GIYLVPQEPLLFPNLSVKENILF--GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 164 ILADEPTGNLdskTSLEVMQLLKMTST--EFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:PRK15439 162 LILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKlPEIRQLADRISVMRDGTIA 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-221 |
3.06e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNdeqltvf 83
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFvfqnynlvpilnvyqnivLPIE---------------------LDGNTIDRtyvdKIIHLL---HLEEKLDNL 139
Cdd:COG4152 70 -RRRIGY------------------LPEErglypkmkvgeqlvylarlkgLSKAEAKR----RADEWLerlGLGDRANKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 140 PNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSktsleV-MQLLKMTSTEF---GQTLVMITHNPELAQ-IADRMIH 214
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP-----VnVELLKDVIRELaakGTTVIFSSHQMELVEeLCDRIVI 201
|
....*..
gi 517425933 215 IEDGKIV 221
Cdd:COG4152 202 INKGRKV 208
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-221 |
3.40e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 33 PGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrrRNIGFVFQNynlvpilnvyqnivLPiE 112
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQ--------------LP-A 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 113 LDGNTI---------------------DRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTG 171
Cdd:PRK10575 97 AEGMTVrelvaigrypwhgalgrfgaaDREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517425933 172 NLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKIV 221
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMaARYCDYLVALRGGEMI 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-218 |
1.02e-16 |
|
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: 75.83 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 13 YYGQEPNITkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRRNIGFVF 92
Cdd:cd03290 7 YFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 93 QNYNLvpiLN--VYQNIVLpieldGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALAS 159
Cdd:cd03290 86 QKPWL---LNatVEENITF-----GSPFNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQ--LLKMTSTEfGQTLVMITHNPELAQIADRMIHIEDG 218
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-201 |
1.37e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.05 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQEPNItkalDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVkirgkEIGKmndeqlT 81
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLI----DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-----EIGE------T 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 82 VfrrrNIGFVFQNY-NLVPILNVYQNIVlpielDGNTI---------DRTYV--------DKiihllhlEEKLDnlpnNL 143
Cdd:TIGR03719 385 V----KLAYVDQSRdALDPNKTVWEEIS-----GGLDIiklgkreipSRAYVgrfnfkgsDQ-------QKKVG----QL 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 144 SGGQQQRVAIARALASKPAIILADEPTGNLDsktsLEVMQLLKMTSTEFGQTLVMITH 201
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISH 498
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-201 |
1.57e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.67 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 3 YILETKNLKKYYGQEPNItkaLDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIR-GKEIGKMN----- 76
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKKEI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLPqepql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 DEQLTVFRR-----RNIGFVFQNYNlvpilNVYQNIVLP-----------------IE-LDGNTIDRTyVDKIIHLLHLE 133
Cdd:TIGR03719 80 DPTKTVRENveegvAEIKDALDRFN-----EISAKYAEPdadfdklaaeqaelqeiIDaADAWDLDSQ-LEIAMDALRCP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 134 EKlDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKmtstEFGQTLVMITH 201
Cdd:TIGR03719 154 PW-DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTH 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-220 |
1.66e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.56 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQEPNItKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNML-GGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:TIGR02633 255 DVILEARNLTCWDVINPHR-KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TvfrRRNIGFVFQN---YNLVPILNVYQNIVLPIELDGNTIDRT-------YVDKIIHLLHLEEKLDNLP-NNLSGGQQQ 149
Cdd:TIGR02633 334 I---RAGIAMVPEDrkrHGIVPILGVGKNITLSVLKSFCFKMRIdaaaelqIIGSAIQRLKVKTASPFLPiGRLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKI 220
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSElAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-221 |
1.87e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.68 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLnmlggldipssgsvKIRGKEI----GKMNDEQ-LTVFR-----RRNI-GFVF 92
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLM--------------KILNGEVllddGRIIYEQdLIVARlqqdpPRNVeGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 93 qNY------NLVPILNVYQNIVLPIELDgntidrtYVDKIIH-LLHLEEKLDNLP-----------------------NN 142
Cdd:PRK11147 85 -DFvaegieEQAEYLKRYHDISHLVETD-------PSEKNLNeLAKLQEQLDHHNlwqlenrinevlaqlgldpdaalSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 143 LSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKmtstEFGQTLVMITHNPELAQ-IADRMIHIEDGKIV 221
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRSFIRnMATRIVDLDRGKLV 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-218 |
3.79e-16 |
|
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: 76.87 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 20 ITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigkmndeqltvfrrrnIGFVFQNYNLVP 99
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 iLNVYQNIVLpieldGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILADE 168
Cdd:TIGR01271 501 -GTIKDNIIF-----GLSYDEYRYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 169 PTGNLDSKTSLEVMQ--LLKMTSTefgQTLVMITHNPELAQIADRMIHIEDG 218
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEscLCKLMSN---KTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-215 |
6.96e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 6.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 25 DGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEqltvfRRRNIGFV------------F 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-----YHQDLLYLghqpgikteltaL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 93 QNynlvpiLNVYQNIvlpieldGNTIDRtyvDKIIHLLH---LEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEP 169
Cdd:PRK13538 93 EN------LRFYQRL-------HGPGDD---EALWEALAqvgLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517425933 170 TGNLDsKTSLEVMQLLKMTSTEFGQTLVMITHNPeLAQIADRMIHI 215
Cdd:PRK13538 157 FTAID-KQGVARLEALLAQHAEQGGMVILTTHQD-LPVASDKVRKL 200
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-223 |
1.06e-15 |
|
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: 72.56 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLD--IPSSGSVKIRGKEIGKMNDEQltvfR-RRNIGFVFQNynlvpi 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEE----RaRLGIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 101 lnvyqnivlPIELDGNTidrtyvdkiihllhLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPtgnlDSKTSLE 180
Cdd:cd03217 86 ---------PPEIPGVK--------------NADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEP----DSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517425933 181 VMQLLKMTSTEF---GQTLVMITHNPELAQ--IADRMIHIEDGKIVER 223
Cdd:cd03217 139 ALRLVAEVINKLreeGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKS 186
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-221 |
1.13e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGlDIPSS---------GSVKIRGKEIGKMNDEQLTvfRRRNI------ 88
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLA--RLRAVlpqaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 89 -GFVFQNYNLVpILNVYQNIVLPIELDGNtiDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA--------- 158
Cdd:PRK13547 94 pAFAFSAREIV-LLGRYPHARRAGALTHR--DGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKIV 221
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRIAMLADGAIV 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-220 |
1.21e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQEPNItKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNML-GGLDIPSSGSVKIRGKEIGKMNDEQL 80
Cdd:PRK13549 257 EVILEVRNLTAWDPVNPHI-KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TvfrRRNIGFVFQN---YNLVPILNVYQNIVLPIeLD----GNTIDR----TYVDKIIHLLHLEEKLDNLP-NNLSGGQQ 148
Cdd:PRK13549 336 I---AQGIAMVPEDrkrDGIVPVMGVGKNITLAA-LDrftgGSRIDDaaelKTILESIQRLKVKTASPELAiARLSGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 149 QRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKI 220
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSElPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-203 |
2.34e-15 |
|
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: 71.76 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfrRRNIGFVFQNYNLVPILNV 103
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-----ARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 104 YQNIvlpieldgntidrtyvdKIIHLLH----LEEKLD--------NLP-NNLSGGQQQRVAIARALASKPAIILADEPT 170
Cdd:cd03231 91 LENL-----------------RFWHADHsdeqVEEALArvglngfeDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|...
gi 517425933 171 GNLDSKTSLEVMQLLKmTSTEFGQTLVMITHNP 203
Cdd:cd03231 154 TALDKAGVARFAEAMA-GHCARGGMVVLTTHQD 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
2.90e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 1 MDYILETKNLKKYYGQEpnitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKirgkeigkmNDEQL 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 tvfrrrNIGFVFQNYNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHLeekLDNLPNNLSGGQQQRVAIARALASK 160
Cdd:PRK09544 68 ------RIGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHL---IDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPEL 205
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-197 |
4.34e-15 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 72.01 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 31 VEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSsgsvkiRGKEIGKMN-DEQLTVFRrrniGFVFQNY-------NLVPILN 102
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPN------LGKFDDPPDwDEILDEFR----GSELQNYftkllegDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 103 VYQNIVLPIELDGNTI-------DRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDS 175
Cdd:cd03236 93 PQYVDLIPKAVKGKVGellkkkdERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|..
gi 517425933 176 KTSLEVMQLLKMTSTEFGQTLV 197
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLV 194
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-220 |
5.33e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.13 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGlDIPSSGSvkirgkeigkmNDeqLTVF-RRR-----------NIGFV 91
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYS-----------ND--LTLFgRRRgsgetiwdikkHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNYNL-----VPILNV-----------YQNIvlpieldgNTIDRTYVDKIIHLLHLEEKLDNLP-NNLSGGQQQRVAIA 154
Cdd:PRK10938 342 SSSLHLdyrvsTSVRNVilsgffdsigiYQAV--------SDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 155 RALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQT-LVMITHNPELAQ--IADRMIHIEDGKI 220
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISE-GETqLLFVSHHAEDAPacITHRLEFVPDGDI 481
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-218 |
9.58e-15 |
|
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: 71.43 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 20 ITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKeigkmndeqltvfrrrnIGFVFQNYNLVP 99
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 iLNVYQNIVLpieldGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILADE 168
Cdd:cd03291 112 -GTIKENIIF-----GVSYDEYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 169 PTGNLDSKTSLEVMQ--LLKMTSTefgQTLVMITHNPELAQIADRMIHIEDG 218
Cdd:cd03291 186 PFGYLDVFTEKEIFEscVCKLMAN---KTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-170 |
1.54e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI--GKMNdeqlTvfrRRNIGFVFQNYNLVPI 100
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIA----T---RRRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 101 LNVYQNIVLP---IELDGNTIDRtYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPT 170
Cdd:NF033858 354 LTVRQNLELHarlFHLPAAEIAA-RVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-222 |
1.58e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 13 YYGQEPNITK-ALDGIDVKVEPGEFVSIIGTSGSGKSTLLN-MLGGLDIPSSGSVKIRGkeigkmndeqlTVFRRRNIGF 90
Cdd:PLN03232 621 YFSWDSKTSKpTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-----------SVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 91 VFQnynlvpiLNVYQNIVLpieldGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALAS 159
Cdd:PLN03232 690 IFN-------ATVRENILF-----GSDFESERYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLkMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDSC-MKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-221 |
2.02e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 22 KALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIG-KMNDEQLtvfrRRNIGFVFQNYNLVPI 100
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEAL----ENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 101 LNVYQNIVL-PIELDGNTID--RTYVDKIIHLLHLEEKLDnlPN----NLSGGQQQRVAIARALASKPAIILADEPTGNL 173
Cdd:PRK10982 88 RSVMDNMWLgRYPTKGMFVDqdKMYRDTKAIFDELDIDID--PRakvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517425933 174 DSKtslEVMQLLKMTST--EFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:PRK10982 166 TEK---EVNHLFTIIRKlkERGCGIVYISHKmEEIFQLCDEITILRDGQWI 213
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-205 |
2.06e-14 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 71.80 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 33 PGEFVSIIGTSGSGKSTLLNMLGGLDIPS--SGSVKIRGkeigkMNDEQLTvFRRRNiGFVFQNYNLVPILNVYQNIV-- 108
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG-----FPKKQET-FARIS-GYCEQNDIHSPQVTVRESLIys 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 109 ----LPIELdGNTIDRTYVDKIIHLLHLEEKLD---NLP--NNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSL 179
Cdd:PLN03140 978 aflrLPKEV-SKEEKMMFVDEVMELVELDNLKDaivGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
170 180
....*....|....*....|....*.
gi 517425933 180 EVMQLLKMTsTEFGQTLVMITHNPEL 205
Cdd:PLN03140 1057 IVMRTVRNT-VDTGRTVVCTIHQPSI 1081
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-201 |
3.73e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQepnitKAL-DGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIrGKeigkmndeql 80
Cdd:PRK11819 322 DKVIEAENLSKSFGD-----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE---------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 81 TVfrrrNIGFVFQNY-NLVPILNVYQNIVlpielDGNTI---------DRTYV----------DKIIhllhleekldnlp 140
Cdd:PRK11819 386 TV----KLAYVDQSRdALDPNKTVWEEIS-----GGLDIikvgnreipSRAYVgrfnfkggdqQKKV------------- 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 141 NNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKT--SLEVmQLLkmtstEFGQTLVMITH 201
Cdd:PRK11819 444 GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETlrALEE-ALL-----EFPGCAVVISH 500
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-222 |
3.77e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDI--PSSGSVKIRGKEIGKMN-DEqltvfR-RRNIGFVFQNYNLVP 99
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSpDE-----RaRAGIFLAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 ILNVYQ------NIVLPIELDGNTIDRTyVDKIIHLLHLEEKLDNLPNN--LSGGQQQRVAIARALASKPAIILADEPTG 171
Cdd:COG0396 91 GVSVSNflrtalNARRGEELSAREFLKL-LKEKMKELGLDEDFLDRYVNegFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 172 NLDsktsLEVMQLL-----KMTSTEFGqtLVMITHNPELAQI--ADRMIHIEDGKIVE 222
Cdd:COG0396 170 GLD----IDALRIVaegvnKLRSPDRG--ILIITHYQRILDYikPDFVHVLVDGRIVK 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-213 |
5.48e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPG-----EFVSIIGTSGSGKSTLLNMLGGLDIPSSGSV----KIRGK--EIGkmNDEQLTV--FR 84
Cdd:COG1245 345 PDLTKSYGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlKISYKpqYIS--PDYDGTVeeFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNynlvpilNVYQNivlpieldgntidrtyvdKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:COG1245 423 RSANTDDFGS-------SYYKT------------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMI 213
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDyISDRLM 527
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-201 |
1.22e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 3 YILETKNLKKYYGQEPNItkaLDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIR-GKEIGKMN----- 76
Cdd:PRK11819 5 YIYTMNRVSKVVPPKKQI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVGYLPqepql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 DEQLTVfrRRNI--GF-----VFQNYNlvpilNVYQNIVLPIELDGNTIDR--TYVDKIIHL-LH-LEEKLD------NL 139
Cdd:PRK11819 82 DPEKTV--RENVeeGVaevkaALDRFN-----EIYAAYAEPDADFDALAAEqgELQEIIDAAdAWdLDSQLEiamdalRC 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 140 P------NNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKmtstEFGQTLVMITH 201
Cdd:PRK11819 155 PpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLH----DYPGTVVAVTH 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-222 |
1.49e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYgqepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIG--------KM 75
Cdd:PRK09700 265 VFEVRNVTSRD------RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 NDEQLTVFRRRNiGFvFQNYNLVPILNVYQNIVL-----PIELDGNTIDRTYVDKIIHLLHLE-EKLDNLPNNLSGGQQQ 149
Cdd:PRK09700 339 GMAYITESRRDN-GF-FPNFSIAQNMAISRSLKDggykgAMGLFHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 150 RVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKIVE 222
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSElPEIITVCDRIAVFCEGRLTQ 489
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-222 |
1.59e-13 |
|
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: 69.20 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGkeigkmndeqltvfrrrNIGFV-----FQNYNLv 98
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------------SVAYVpqqawIQNDSL- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 pilnvYQNIVLpieldGNTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILAD 167
Cdd:TIGR00957 716 -----RENILF-----GKALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 168 EPTGNLDSKTSLEV-------MQLLKmtstefGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:TIGR00957 786 DPLSAVDAHVGKHIfehvigpEGVLK------NKTRILVTHGISYLPQVDVIIVMSGGKISE 841
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-221 |
2.23e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 20 ITKALDGIdvkVEPGEFVSIIGTSGSGKSTLLNMLG----GLDIPSSGSVKIRGkeIGKmndEQLTVFRRRNIGFVFQNY 95
Cdd:TIGR00956 76 ILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG--ITP---EEIKKHYRGDVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 96 NLVPILNVYQNIVLPIELDG-----NTIDR-TYVDKIIHLLHLEEKLDNLPNN---------LSGGQQQRVAIARALASK 160
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCKTpqnrpDGVSReEYAKHIADVYMATYGLSHTRNTkvgndfvrgVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 161 PAIILADEPTGNLDSKTSLEVMQLLKmTSTEFGQTLVMIT---HNPELAQIADRMIHIEDGKIV 221
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALK-TSANILDTTPLVAiyqCSQDAYELFDKVIVLYEGYQI 290
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-220 |
2.44e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 27 IDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQltvfrRRNIGFVF-----QNYNLVPIL 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 NVYQNIV------LPIELDGN----TIDRTYVDKIIHLLHLEEKLdnlpNNLSGGQQQRVAIARALASKPAIILADEPTG 171
Cdd:PRK15439 357 PLAWNVCalthnrRGFWIKPArenaVLERYRRALNIKFNHAEQAA----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517425933 172 NLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKI 220
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQ-NVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
19-216 |
3.54e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 19 NITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNdeqltvfRRRNIGFVFQNYNLV 98
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 PILNVYQNIVLPIELDGNTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDskts 178
Cdd:PRK13543 95 ADLSTLENLHFLCGLHGRRAKQM-PGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD---- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517425933 179 LEVMQLL-KMTSTEF---GQTLVMiTHNPELA-QIADRMIHIE 216
Cdd:PRK13543 170 LEGITLVnRMISAHLrggGAALVT-THGAYAApPVRTRMLTLE 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-197 |
4.59e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmnDEQLTVF 83
Cdd:PRK13540 1 MLDVIELDFDYHDQP----LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RRRnIGFVFQNYNLVPILNVYQNIVLPIELDGNTIDrtyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAI 163
Cdd:PRK13540 73 QKQ-LCFVGHRSGINPYLTLRENCLYDIHFSPGAVG---ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....
gi 517425933 164 ILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLV 197
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLL 182
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-202 |
5.34e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.44 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKmndeqltVFRRRNIGFVFQNYNL---VP 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVdwsFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 100 ILnvYQNIVLPIELD-------GNTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGN 172
Cdd:PRK15056 95 VL--VEDVVMMGRYGhmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|
gi 517425933 173 LDSKTSLEVMQLLKMTSTEfGQTLVMITHN 202
Cdd:PRK15056 173 VDVKTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-221 |
6.07e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEigkmndeqltvfr 84
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA------------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 rrNIGFVFQNY--------NLVPILNVYQNivlpiELDGNTIDRTYVDKiihLLHLEEKLDNLPNNLSGGQQQRVAIARA 156
Cdd:PRK15064 383 --NIGYYAQDHaydfendlTLFDWMSQWRQ-----EGDDEQAVRGTLGR---LLFSQDDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 157 LASKPAIILADEPTGNLDsktsLEVMQLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKIV 221
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMD----MESIESLNMALEKYEGTLIFVSHDREFvSSLATRIIEITPDGVV 514
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-213 |
6.50e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPG-----EFVSIIGTSGSGKSTLLNMLGGLDIPSSGSV----KIRGK--EIGkmNDEQLTV--FR 84
Cdd:PRK13409 344 PDLTKKLGDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKISYKpqYIK--PDYDGTVedLL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNYnlvpilnvYQNivlpieldgntidrtyvdKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:PRK13409 422 RSITDDLGSSY--------YKS------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517425933 165 LADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMI 213
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDyISDRLM 525
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-222 |
7.03e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.36 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL--DIPSSGSVKIRGKEIGKMndeQLT 81
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkDNWRVTADRMRFDDIDLL---RLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 82 VFRRR-----NIGFVFQNYN--LVPILNVYQNIVLPIEldGNTIDRTYVDKI-------IHLLHL------EEKLDNLPN 141
Cdd:PRK15093 80 PRERRklvghNVSMIFQEPQscLDPSERVGRQLMQNIP--GWTYKGRWWQRFgwrkrraIELLHRvgikdhKDAMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 142 NLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGKI 220
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmLSQWADKINVLYCGQT 237
|
..
gi 517425933 221 VE 222
Cdd:PRK15093 238 VE 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-204 |
9.74e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.96 E-value: 9.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIgkmndeqLTvf 83
Cdd:TIGR01257 1937 ILRLNELTKVYSGTS--SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-------LT-- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rrrNIGFVFQNYNLVP-------ILNVYQNIVLPIELDGntIDRTYVDKI----IHLLHLEEKLDNLPNNLSGGQQQRVA 152
Cdd:TIGR01257 2006 ---NISDVHQNMGYCPqfdaiddLLTGREHLYLYARLRG--VPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLS 2080
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517425933 153 IARALASKPAIILADEPTGNLDSKTSLEVMQLLkMTSTEFGQTLVMITHNPE 204
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI-VSIIREGRAVVLTSHSME 2131
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-221 |
1.19e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 4 ILETKNLKKYYGQEPnitkALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVf 83
Cdd:PRK13638 1 MLATSDLWFRYQDEP----VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 rRRNIGFVFQNYNL-VPILNVYQNIVLPIELDG---NTIDRTyVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALAS 159
Cdd:PRK13638 76 -RQQVATVFQDPEQqIFYTDIDSDIAFSLRNLGvpeAEITRR-VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELA-QIADRMIHIEDGKIV 221
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIyEISDAVYVLRQGQIL 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-222 |
1.25e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQN--- 94
Cdd:PLN03130 1249 PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQApvl 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 95 ------YNLVPiLNVYQNIVLpieldGNTIDRTYVDKII--HLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILA 166
Cdd:PLN03130 1325 fsgtvrFNLDP-FNEHNDADL-----WESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 167 DEPTGNLDSKTSlEVMQllKMTSTEFGQ-TLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PLN03130 1399 DEATAAVDVRTD-ALIQ--KTIREEFKScTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-221 |
1.62e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.34 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 13 YYGQEPNitKALDGIDVKVEPGEFVSIIGTSGSGKSTLL-NMLGGLDIpSSGSVkirgkeigkmndeqltvFRRRNIGFV 91
Cdd:PTZ00243 667 FFELEPK--VLLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFEI-SEGRV-----------------WAERSIAYV 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNynlVPILN--VYQNIVLPIELDGNTIDrtyvdKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALA 158
Cdd:PTZ00243 727 PQQ---AWIMNatVRGNILFFDEEDAARLA-----DAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVY 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517425933 159 SKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:PTZ00243 799 ANRDVYLLDDPLSALDAHVGERVVEECFLGALA-GKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-213 |
2.00e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNITKALDgIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGL-DIPSSGSVKIRGKEIGKMNDEQ---- 79
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEHTNDMTNEQdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 ----------LTVFRRRNIG------FVFQN-------------YNLV------------PIL---NVYQNIVLPIEldg 115
Cdd:PTZ00265 1245 deeqnvgmknVNEFSLTKEGgsgedsTVFKNsgkilldgvdicdYNLKdlrnlfsivsqePMLfnmSIYENIKFGKE--- 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 116 nTIDRTYVDKIIHLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQL 184
Cdd:PTZ00265 1322 -DATREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260
....*....|....*....|....*....
gi 517425933 185 LKMTSTEFGQTLVMITHNPELAQIADRMI 213
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-186 |
4.48e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 4.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 31 VEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVkirGKEIGKmnDEQLTVFRrrniGFVFQNYnlvpILNVYQNIV-- 108
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSW--DEVLKRFR----GTELQNY----FKKLYNGEIkv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 109 ---------LPIELDGNTID-------RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGN 172
Cdd:PRK13409 163 vhkpqyvdlIPKVFKGKVREllkkvdeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170
....*....|....
gi 517425933 173 LDSKTSLEVMQLLK 186
Cdd:PRK13409 243 LDIRQRLNVARLIR 256
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-215 |
7.09e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 32 EPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVkirGKEIGKmnDEQLTVFRrrniGFVFQNYnLVPILN-----VY-- 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSW--DEVLKRFR----GTELQDY-FKKLANgeikvAHkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 105 QNI-VLPIELDGNTID-------RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSK 176
Cdd:COG1245 167 QYVdLIPKVFKGTVREllekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517425933 177 TSLEVMQLLKMTSTEfGQTLVMITHnpELA---QIADrMIHI 215
Cdd:COG1245 247 QRLNVARLIRELAEE-GKYVLVVEH--DLAildYLAD-YVHI 284
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-222 |
7.61e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynl 97
Cdd:PLN03232 1246 PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQS--- 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 vPIL---NVYQNIVlPIElDGNTIDrtyVDKIIHLLHLEEKLDNLP-----------NNLSGGQQQRVAIARALASKPAI 163
Cdd:PLN03232 1319 -PVLfsgTVRFNID-PFS-EHNDAD---LWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 164 ILADEPTGNLDSKTSLEVMQLLKmtsTEFGQ-TLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIR---EEFKScTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-223 |
9.62e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLG-GLDIpSSGSVKIRGKEIGKMndeQLTVFRRRnigfvFQNYNLVPIL 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDV-SEGDIRFHDIPLTKL---QLDSWRSR-----LAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 ---NVYQNIVLpieldGN-TIDRTYVDKIIHLLHLEEKLDNLPNN-----------LSGGQQQRVAIARALASKPAIILA 166
Cdd:PRK10789 401 fsdTVANNIAL-----GRpDATQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 167 DEPTGNLDSKTSLEVMQLLKmtstEFGQ--TLVMITHNPELAQIADRMIHIEDGKIVER 223
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLR----QWGEgrTVIISAHRLSALTEASEILVMQHGHIAQR 530
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-196 |
1.10e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 61.43 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 33 PGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTvfrrrnigFVFQNYNLVPILNVYQNIVLPIE 112
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT--------YIGHNLGLKLEMTVFENLKFWSE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 113 LDGNTidrTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEF 192
Cdd:PRK13541 97 IYNSA---ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSG 173
|
....
gi 517425933 193 GQTL 196
Cdd:PRK13541 174 GIVL 177
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-222 |
1.73e-11 |
|
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: 63.43 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynl 97
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQD--- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 98 vPILNvyqNIVLPIELDGNTidrTYVDKII----HLLHLEEKLDNLPN-----------NLSGGQQQRVAIARALASKPA 162
Cdd:TIGR00957 1369 -PVLF---SGSLRMNLDPFS---QYSDEEVwwalELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517425933 163 IILADEPTGNLDsktsLEVMQLLKMT-STEFGQ-TLVMITHnpELAQIAD--RMIHIEDGKIVE 222
Cdd:TIGR00957 1442 ILVLDEATAAVD----LETDNLIQSTiRTQFEDcTVLTIAH--RLNTIMDytRVIVLDKGEVAE 1499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2-226 |
4.52e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 4.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYygQEPNITKaldgIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQ-- 79
Cdd:PRK10982 248 EVILEVRNLTSL--RQPSIRD----VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEai 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 80 -----LTVFRRRNIGfVFQNYN-----LVPILNVYQNivlPIELDGNT---------IDRTYVDKIIHLLHLeekldnlp 140
Cdd:PRK10982 322 nhgfaLVTEERRSTG-IYAYLDigfnsLISNIRNYKN---KVGLLDNSrmksdtqwvIDSMRVKTPGHRTQI-------- 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 141 NNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLkMTSTEFGQTLVMITHN-PELAQIADRMIHIEDGK 219
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEmPELLGITDRILVMSNGL 468
|
250
....*....|
gi 517425933 220 ---IVERKES 226
Cdd:PRK10982 469 vagIVDTKTT 478
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-220 |
1.37e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQ--------LTVFRRRNigfvfqny 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRD-------- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 96 NLVPILNVYQNIVLpieldgnTIDRTYVDKIIHLLHLEEKL----------------DNLPNNLSGGQQQRVAIARALAS 159
Cdd:PRK10762 340 GLVLGMSVKENMSL-------TALRYFSRAGGSLKHADEQQavsdfirlfniktpsmEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517425933 160 KPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKI 220
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEmPEVLGMSDRILVMHEGRI 473
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-220 |
1.45e-10 |
|
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: 59.48 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:cd03289 3 MTVKDLTAKYTEGGN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKW---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIGFVFQNY---------NLVP--------ILNVYQNIVL-------PIELDGNTIDRTYVdkiihllhleekldnlp 140
Cdd:cd03289 76 RKAFGVIPQKVfifsgtfrkNLDPygkwsdeeIWKVAEEVGLksvieqfPGQLDFVLVDGGCV----------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 141 nnLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTefGQTLVMITHNPELAQIADRMIHIEDGKI 220
Cdd:cd03289 139 --LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-215 |
3.69e-10 |
|
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: 56.95 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNmlggldipssgsvKIRGKEIGKMNDEQLTVFRRRNIGFVFQNYNLVpiln 102
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNKLIFIDQLQFLI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 103 vyqnivlpieldgntidrtyvDKIIHLLHLEEKLdnlpNNLSGGQQQRVAIARALAS--KPAIILADEPTGNLDSKTSLE 180
Cdd:cd03238 73 ---------------------DVGLGYLTLGQKL----STLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|....*
gi 517425933 181 VMQLLKmTSTEFGQTLVMITHNPELAQIADRMIHI 215
Cdd:cd03238 128 LLEVIK-GLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-222 |
4.23e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYgqepNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdiPS----SGSVKIRGKEIGKMND 77
Cdd:CHL00131 5 KPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PAykilEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 78 EQLTvfrRRNIGFVFQNynlvpilnvyqnivlPIELDG-NTID--------------RTYVDKIIHLLHLEEKLD----- 137
Cdd:CHL00131 79 EERA---HLGIFLAFQY---------------PIEIPGvSNADflrlaynskrkfqgLPELDPLEFLEIINEKLKlvgmd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 138 ------NLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQ-IAD 210
Cdd:CHL00131 141 psflsrNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDyIKP 219
|
250
....*....|...
gi 517425933 211 RMIHI-EDGKIVE 222
Cdd:CHL00131 220 DYVHVmQNGKIIK 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-224 |
8.34e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.46 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 33 PGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVkirgkeigkmndeqltvfrrrnigfvfqnynlvpilnvyqnivlpIE 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---------------------------------------------IY 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 113 LDGNTIDRTYVDKIIHLLHLEEKLdnlpnNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQL----LKMT 188
Cdd:smart00382 36 IDGEDILEEVLDQLLLIIVGGKKA-----SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrLLLL 110
|
170 180 190
....*....|....*....|....*....|....*.
gi 517425933 189 STEFGQTLVMITHNPELAQIADRMIHIEDGKIVERK 224
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLL 146
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-222 |
8.65e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 57.23 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 17 EPNITKALDGIDVKVEPGEFVSIIGTSGSGKSTL-LNMLGGLDIpSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNy 95
Cdd:cd03288 30 ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDI-FDGKIVIDGIDISKLPLHTL----RSRLSIILQD- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 96 nlvPILnVYQNIVLPIELDGNTIDRTYVDKIiHLLHLEEKLDNLP-----------NNLSGGQQQRVAIARALASKPAII 164
Cdd:cd03288 104 ---PIL-FSGSIRFNLDPECKCTDDRLWEAL-EIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517425933 165 LADEPTGNLDSKTSlEVMQLLKMTSTEfGQTLVMITHNPELAQIADRMIHIEDGKIVE 222
Cdd:cd03288 179 IMDEATASIDMATE-NILQKVVMTAFA-DRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-219 |
2.15e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.68 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 18 PNITKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPSSGSVkirgkeigkmndeqLTVFRRRNIGFVFQN-YN 96
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGR--------------LTKPAKGKLFYVPQRpYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 97 LVPILNvyQNIVLPIELDgNTIDRTYVDK----IIHLLHLEEKLD---------NLPNNLSGGQQQRVAIARALASKPAI 163
Cdd:TIGR00954 527 TLGTLR--DQIIYPDSSE-DMKRRGLSDKdleqILDNVQLTHILEreggwsavqDWMDVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517425933 164 ILADEPTgnldSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIeDGK 219
Cdd:TIGR00954 604 AILDECT----SAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYM-DGR 654
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-222 |
3.08e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLTVFRRRNIGFVFQNYNLVPILNV 103
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 104 YQNIVLPIElDGNTIDRTY--VDKI---------IHLLH----LEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADE 168
Cdd:PRK10636 97 QLHDANERN-DGHAIATIHgkLDAIdawtirsraASLLHglgfSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 169 PTGNLDSKTSLEVMQLLKmtstEFGQTLVMITHNPE-LAQIADRMIHIEDGKIVE 222
Cdd:PRK10636 176 PTNHLDLDAVIWLEKWLK----SYQGTLILISHDRDfLDPIVDKIIHIEQQSLFE 226
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
17-216 |
3.70e-09 |
|
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: 54.12 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 17 EPNITKALDGIDVKVEPGEF-----VSIIGTSGSGKSTLLNMLGGLDIPSSGSvkirgkeigkmndeqltvfrrrnigfv 91
Cdd:cd03222 3 YPDCVKRYGVFFLLVELGVVkegevIGIVGPNGTGKTTAVKILAGQLIPNGDN--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 fqnynlvpilnvyqnivlpIELDGNTIdrTYVDKIIhllhleekldnlpnNLSGGQQQRVAIARALASKPAIILADEPTG 171
Cdd:cd03222 56 -------------------DEWDGITP--VYKPQYI--------------DLSGGELQRVAIAAALLRNATFYLFDEPSA 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517425933 172 NLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIE 216
Cdd:cd03222 101 YLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDyLSDRIHVFE 146
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-221 |
4.05e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQepniTKALDGIDVKVEPGEFVSIIGTSGSG--KSTLLNMLGGldiPSSGSVKIRGKEIGKmNDEQLtv 82
Cdd:NF000106 14 VEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCA-NRRAL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 83 frRRNIGF-----VFQNYNLVPILNVYqniVLPIELDGNTID-RTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARA 156
Cdd:NF000106 84 --RRTIG*hrpvr*GRRESFSGRENLY---MIGR*LDLSRKDaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517425933 157 LASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIEDGKIV 221
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-221 |
7.95e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 27 IDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEI-----------GKMndeqLTVFRRRNIGfvfqny 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirsprdairaGIM----LCPEDRKAEG------ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 96 nLVPILNVYQNI-------VLPIeldGNTIDRTY----VDKIIHLLHLEEK-LDNLPNNLSGGQQQRVAIARALASKPAI 163
Cdd:PRK11288 342 -IIPVHSVADNInisarrhHLRA---GCLINNRWeaenADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 164 ILADEPTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHN-PELAQIADRMIHIEDGKIV 221
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDlPEVLGVADRIVVMREGRIA 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-174 |
4.21e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLtvfrRRNIGFVFQNynlvPIL-- 101
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL----RRQFSMIPQD----PVLfd 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 -NVYQNiVLPIeLDGNTIDrtyVDKIIHLLHLEEKLDNLP-----------NNLSGGQQQRVAIARALASK-PAIILADE 168
Cdd:PTZ00243 1398 gTVRQN-VDPF-LEASSAE---VWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARALLKKgSGFILMDE 1472
|
....*.
gi 517425933 169 PTGNLD 174
Cdd:PTZ00243 1473 ATANID 1478
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-216 |
4.50e-08 |
|
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: 51.45 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 39 IIGTSGSGKSTLLNML-------------GGLDIPS-------SGSVKIRGKEIgkmNDEQLTVFRRrnigfvfqnynlv 98
Cdd:cd03240 27 IVGQNGAGKTTIIEALkyaltgelppnskGGAHDPKliregevRAQVKLAFENA---NGKKYTITRS------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 99 piLNVYQNIVLpieldgntidrtyvdkiihlLHLEEKLDNLPNN---LSGGQQQ------RVAIARALASKPAIILADEP 169
Cdd:cd03240 91 --LAILENVIF--------------------CHQGESNWPLLDMrgrCSGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517425933 170 TGNLDS---KTSLEvmQLLKMTSTEFGQTLVMITHNPELAQIADRMIHIE 216
Cdd:cd03240 149 TTNLDEeniEESLA--EIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-201 |
4.69e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNITKALDgIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEigKMNDEQLTVFR 84
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKD-LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRnIGFVFQNynlvPIL---NVYQNIVLPI-------------ELDGNT----------------------IDRTYVDKI 126
Cdd:PTZ00265 460 SK-IGVVSQD----PLLfsnSIKNNIKYSLyslkdlealsnyyNEDGNDsqenknkrnscrakcagdlndmSNTTDSNEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 127 IH--------------------LLH-----LEEKLDNL----PNNLSGGQQQRVAIARALASKPAIILADEPTGNLDSKT 177
Cdd:PTZ00265 535 IEmrknyqtikdsevvdvskkvLIHdfvsaLPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260
....*....|....*....|....
gi 517425933 178 SLEVMQLLKMTSTEFGQTLVMITH 201
Cdd:PTZ00265 615 EYLVQKTINNLKGNENRITIIIAH 638
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
19-201 |
7.65e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 19 NIT-----KAL-DGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKI-RGKEIGKMNDEQltvfrrrnigFV 91
Cdd:PRK15064 6 NITmqfgaKPLfENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQ----------FA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 92 FQNYNLVPIL---------------NVYQNI--------------VLPIELDGNTIDRTYVDKIIHLLHLEEKLDNLPNN 142
Cdd:PRK15064 76 FEEFTVLDTVimghtelwevkqerdRIYALPemseedgmkvadleVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLMSE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517425933 143 LSGGQQQRVAIARALASKPAIILADEPTGNLDSKTslevMQLLKMTSTEFGQTLVMITH 201
Cdd:PRK15064 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISH 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-188 |
7.67e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 5 LETKNLKKYYGQEPNitKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLdIPSSGSVKIRGKEIGKMNDEQLtvfr 84
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTW---- 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 85 RRNIG------FVFQN---YNLVP--------ILNVYQNIVL-------PIELDGNTIDRTYVdkiihllhleekldnlp 140
Cdd:TIGR01271 1291 RKAFGvipqkvFIFSGtfrKNLDPyeqwsdeeIWKVAEEVGLksvieqfPDKLDFVLVDGGYV----------------- 1353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517425933 141 nnLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMT 188
Cdd:TIGR01271 1354 --LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS 1399
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-213 |
1.10e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.08 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLN---------MLGGLDIPSSGSVKIRGKE-IGKMND-EQLTVFR--RRN--- 87
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypalarRLHLKKEQPGNHDRIEGLEhIDKVIViDQSPIGRtpRSNpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 88 -IGfVFQnynlvPILNV---------YQNIVLPIELDGNTIDR-------------TYVDKIIHLLHL--EEKLDNLP-- 140
Cdd:cd03271 91 yTG-VFD-----EIRELfcevckgkrYNRETLEVRYKGKSIADvldmtveealeffENIPKIARKLQTlcDVGLGYIKlg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 141 ---NNLSGGQQQRVAIARALaSKPA----IILADEPTGNL---DSKTSLEVMQLLkmtsTEFGQTLVMITHNPELAQIAD 210
Cdd:cd03271 165 qpaTTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLhfhDVKKLLEVLQRL----VDKGNTVVVIEHNLDVIKCAD 239
|
...
gi 517425933 211 RMI 213
Cdd:cd03271 240 WII 242
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-69 |
1.11e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 1.11e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRG 69
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-220 |
1.12e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKI-RGKEIGKMNDEQLTVFRRrnigfvfqnyNLVPILN 102
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQLEFLRA----------DESPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 103 VYQniVLPIELDGNTidRTYVDKiihLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDsktsLEVM 182
Cdd:PRK10636 398 LAR--LAPQELEQKL--RDYLGG---FGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMR 466
|
170 180 190
....*....|....*....|....*....|....*....
gi 517425933 183 QLLKMTSTEFGQTLVMITHNPELAQ-IADRMIHIEDGKI 220
Cdd:PRK10636 467 QALTEALIDFEGALVVVSHDRHLLRsTTDDLYLVHDGKV 505
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-221 |
1.35e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 2 DYILETKNLKKYYGQEPNiTKALDGIDVKVEPGEFVSIIGTSGSGKsTLLNM--LG---GLDIpsSGSVKIRGKEIgkmn 76
Cdd:NF040905 255 EVVFEVKNWTVYHPLHPE-RKVVDDVSLNVRRGEIVGIAGLMGAGR-TELAMsvFGrsyGRNI--SGTVFKDGKEV---- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 77 dEQLTVFR--RRNIGFVFQN---YNLVPILNVYQNIVLPiELDGNTiDRTYVDKIIHLLHLEEKLDNL----PN------ 141
Cdd:NF040905 327 -DVSTVSDaiDAGLAYVTEDrkgYGLNLIDDIKRNITLA-NLGKVS-RRGVIDENEEIKVAEEYRKKMniktPSvfqkvg 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 142 NLSGGQQQRVAIARALASKPAIILADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHN-PELAQIADRMIHIEDGKI 220
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSElPELLGMCDRIYVMNEGRI 482
|
.
gi 517425933 221 V 221
Cdd:NF040905 483 T 483
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-215 |
2.23e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 2.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 143 LSGGQQQRVAIARALAS---KPA-IILADEPTGNLDSKTSLEVMQLLKMTSTEFGQTLVmITHNPELAQIADRMIHI 215
Cdd:cd03227 78 LSGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAELADKLIHI 153
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-170 |
2.56e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 14 YGQepniTKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGkeiGKMNDEQltvFRRRN---IGF 90
Cdd:NF033858 11 YGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG---GDMADAR---HRRAVcprIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 91 VFQNY--NLVPILNVYQNIVLPIELDGntIDRTYVD-KIIHLLH---LEEKLDNLPNNLSGGQQQRVAIARALASKPAII 164
Cdd:NF033858 81 MPQGLgkNLYPTLSVFENLDFFGRLFG--QDAAERRrRIDELLRatgLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
....*.
gi 517425933 165 LADEPT 170
Cdd:NF033858 159 ILDEPT 164
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-215 |
8.75e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 136 LDNLP-----NNLSGGQQQRVAIARALAS---KPAIILADEPTGNL---DSKTSLEVMQLLkmtsTEFGQTLVMITHNPE 204
Cdd:PRK00635 798 LDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSL----THQGHTVVIIEHNMH 873
|
90
....*....|.
gi 517425933 205 LAQIADRMIHI 215
Cdd:PRK00635 874 VVKVADYVLEL 884
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-215 |
9.57e-07 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.02 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLL---------------------NMLGGLDIPS-------SGSVKIRGKEIGKM 75
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsieglSPAIAIDQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 76 NdeqltvfrRRNIGFVFQNYNLVPILnvYQNIVLpieldgntidRTYVDKIIH--LLHLeeKLDNLPNNLSGGQQQRVAI 153
Cdd:cd03270 91 P--------RSTVGTVTEIYDYLRLL--FARVGI----------RERLGFLVDvgLGYL--TLSRSAPTLSGGEAQRIRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 154 ARALASKPAIIL--ADEPTGNL---DSKTSLEVMQLLKmtstEFGQTLVMITHNPELAQIADRMIHI 215
Cdd:cd03270 149 ATQIGSGLTGVLyvLDEPSIGLhprDNDRLIETLKRLR----DLGNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
37-220 |
9.86e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 37 VSIIGTSGSGKSTLLNMLGGLDIPSSGsvkirgkeigkmndeqlTVFRRRNIGFVFQNYNLVPILNVYQNIVLpieldgn 116
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSG-----------------TVFRSAKVRMAVFSQHHVDGLDLSSNPLL------- 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 117 TIDRTYVDKiihllhLEEKL----------DNLP----NNLSGGQQQRVAIARALASKPAIILADEPTGNLDsktsLEVM 182
Cdd:PLN03073 594 YMMRCFPGV------PEQKLrahlgsfgvtGNLAlqpmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAV 663
|
170 180 190
....*....|....*....|....*....|....*....
gi 517425933 183 QLLKMTSTEFGQTLVMITHNPEL-AQIADRMIHIEDGKI 220
Cdd:PLN03073 664 EALIQGLVLFQGGVLMVSHDEHLiSGSVDELWVVSEGKV 702
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
141-224 |
1.98e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 141 NNLSGGQQQRVAIARALASKPAIILADEPTGNLDsktsLEVMQLLKMTSTEFGQTLVMITHNPE-LAQIADRMIHIEDGK 219
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYLLKWPKTFIVVSHAREfLNTVVTDILHLHGQK 418
|
....*
gi 517425933 220 IVERK 224
Cdd:PLN03073 419 LVTYK 423
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-174 |
2.02e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLD--IPSSGSVKIRGKEIGKMNDEQltvfrRRNIGFVFQNYNLVPIL 101
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED-----RAGEGIFMAFQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 102 NVYQNIVLPIELDG-------NTIDR----TYVDKIIHLLHLEEKLDNLPNNL--SGGQQQRVAIARALASKPAIILADE 168
Cdd:PRK09580 92 GVSNQFFLQTALNAvrsyrgqEPLDRfdfqDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDE 171
|
....*.
gi 517425933 169 PTGNLD 174
Cdd:PRK09580 172 SDSGLD 177
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-213 |
2.83e-06 |
|
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: 47.70 E-value: 2.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517425933 143 LSGGQQQRVAIARALASK---PAIILADEPTGNL---DSKTSLEVMQLLKmtstEFGQTLVMITHNPELAQIADRMI 213
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLV----DKGNTVVVIEHNLDVIKTADYII 902
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-199 |
4.33e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 21 TKALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRGKEIGKMNDEQLT-----VFRRRNigfvfqNY 95
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQklvsdEWQRNN------TD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 96 NLVPILNVYQNIVLPIELDGnTIDRTYVDKIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALASKPAIILADEPTGNLDS 175
Cdd:PRK10938 90 MLSPGEDDTGRTTAEIIQDE-VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180
....*....|....*....|....
gi 517425933 176 KTSLEVMQLLKMTSTEfGQTLVMI 199
Cdd:PRK10938 169 ASRQQLAELLASLHQS-GITLVLV 191
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-218 |
2.28e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 141 NNLSGGQQQRVAIARALASKPAII--LADEPTGNLDSKTSLEVMQLLKMTSTEfGQTLVMITHNPELAQIADRMIHIEDG 218
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-69 |
3.16e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 3.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 517425933 23 ALDGIDVKVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSVKIRG 69
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
28-222 |
4.55e-05 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 43.34 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 28 DVKVEPGE-FVSIIGTSGSGKSTLLNMLGGL-----------------------DIPSSGSVKIRGKEIGKMNDEQLTVF 83
Cdd:cd03241 14 ELELDFEEgLTVLTGETGAGKSILLDALSLLlggrasadlirsgaekavvegvfDISDEEEAKALLLELGIEDDDDLIIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 84 RR-----RNIGFVfqNYNLVPILNVYQNIVLPIELDGNTIDRTYVDKIIHLLHLEEKLDNL-----PN----------NL 143
Cdd:cd03241 94 REisrkgRSRYFI--NGQSVTLKLLRELGSLLVDIHGQHDHQNLLNPERQLDLLDGGLDDVeflfsTNpgeplkplakIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 144 SGGQQQRV--AIARALASK---PAIILaDEPTGNLDSKTSLEVMQLLKMTStEFGQTLVmITHNPELAQIADRMIHIEdg 218
Cdd:cd03241 172 SGGELSRLmlALKAILARKdavPTLIF-DEIDTGISGEVAQAVGKKLKELS-RSHQVLC-ITHLPQVAAMADNHFLVE-- 246
|
....
gi 517425933 219 KIVE 222
Cdd:cd03241 247 KEVE 250
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-201 |
5.75e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 31 VEPGEFVSIIGTSGSGKSTLLN-MLGGLDiPSSGSVKIRGK-EIGkmndeqltvfrrrnigfVFQNY--NLVPILNVYQN 106
Cdd:PRK11147 342 VQRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHCGTKlEVA-----------------YFDQHraELDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 107 IVlpielDG------NTIDRtyvdkiiHLL-HLEEKLDNlPNN-------LSGGQQQRVAIARaLASKPA--IILaDEPT 170
Cdd:PRK11147 404 LA-----EGkqevmvNGRPR-------HVLgYLQDFLFH-PKRamtpvkaLSGGERNRLLLAR-LFLKPSnlLIL-DEPT 468
|
170 180 190
....*....|....*....|....*....|.
gi 517425933 171 GNLDsktsLEVMQLLKMTSTEFGQTLVMITH 201
Cdd:PRK11147 469 NDLD----VETLELLEELLDSYQGTVLLVSH 495
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
143-221 |
7.01e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 143 LSGGQQQRVAIARALaSKPA-----IILaDEPTGNL---DSKTSLEVMQLLkmtsTEFGQTLVMITHNPELAQIADrmiH 214
Cdd:COG0178 827 LSGGEAQRVKLASEL-SKRStgktlYIL-DEPTTGLhfhDIRKLLEVLHRL----VDKGNTVVVIEHNLDVIKTAD---W 897
|
90
....*....|....*.
gi 517425933 215 IED---------GKIV 221
Cdd:COG0178 898 IIDlgpeggdggGEIV 913
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
24-52 |
1.55e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.55e-04
10 20
....*....|....*....|....*....
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLN 52
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-52 |
6.05e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 6.05e-04
10 20
....*....|....*....|....*....
gi 517425933 24 LDGIDVKVEPGEFVSIIGTSGSGKSTLLN 52
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-51 |
1.24e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 1.24e-03
10 20
....*....|....*....|....*..
gi 517425933 25 DGIDVKVEPGEFVSIIGTSGSGKSTLL 51
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
143-221 |
2.30e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 143 LSGGQQQRVAIARALaSKPAI-----ILaDEPTGNL---DSKTSLEVMQLLkmtsTEFGQTLVMITHNPELAQIADrmiH 214
Cdd:PRK00349 831 LSGGEAQRVKLAKEL-SKRSTgktlyIL-DEPTTGLhfeDIRKLLEVLHRL----VDKGNTVVVIEHNLDVIKTAD---W 901
|
90
....*....|....*.
gi 517425933 215 IED---------GKIV 221
Cdd:PRK00349 902 IIDlgpeggdggGEIV 917
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
25-65 |
2.46e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.38 E-value: 2.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 517425933 25 DGIDV---KVEPGEFVSIIGTSGSGKSTLLNMLGGLDIPSSGSV 65
Cdd:PRK01889 183 EGLDVlaaWLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
37-55 |
4.61e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 36.62 E-value: 4.61e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-215 |
4.84e-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: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 136 LDNLPNNLSGGQQQRVAIARALASKPAIIL--ADEPTGNLDSKTSLEVMQLLKMTStEFGQTLVMITHNPELAQIADRMI 213
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLR-DLGNTLIVVEHDEDTIRAADYVI 560
|
..
gi 517425933 214 HI 215
Cdd:TIGR00630 561 DI 562
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
39-65 |
6.83e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 35.78 E-value: 6.83e-03
10 20
....*....|....*....|....*..
gi 517425933 39 IIGTSGSGKSTLLNMLGGLDIPSSGSV 65
Cdd:cd11383 2 LMGKTGAGKSSLCNALFGTEVAAVGDR 28
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
125-212 |
8.81e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 36.47 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517425933 125 KIIHLLHLEEKLDNLPNNLSGGQQQRVAIARALA---SKPA-IILADEPTGNLDSKTSLEVMQLLKMTS--TEFGQTlvm 198
Cdd:cd03272 141 KINSLTNMKQDEQQEMQQLSGGQKSLVALALIFAiqkCDPApFYLFDEIDAALDAQYRTAVANMIKELSdgAQFITT--- 217
|
90
....*....|....
gi 517425933 199 iTHNPELAQIADRM 212
Cdd:cd03272 218 -TFRPELLEVADKF 230
|
|
| |
