|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-215 |
1.29e-92 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 275.00 E-value: 1.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG1136 85 RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRMLPMADRVVEL 215
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTtIVMVTHDPELAARADRVIRL 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-215 |
4.84e-86 |
|
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: 258.19 E-value: 4.84e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRMLPMADRVVEL 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTtIVVVTHDPELAEYADRIIEL 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-215 |
2.38e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 202.98 E-value: 2.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:COG2884 2 IRFENVSKRYPGGREALS---DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG2884 79 R-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLP-MADRVVEL 215
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDrMPKRVLEL 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
24-213 |
2.43e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 198.29 E-value: 2.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 24 NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtLQGAELANYRRnKVGIVFQAFNLVPSLTAV 103
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRR-KVGMVFQQFNLFPHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 104 ENVMV-PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:COG1126 96 ENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEV 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 183 LRLIRELADGERVVVVATHDsrmlpM------ADRVV 213
Cdd:COG1126 176 LDVMRDLAKEGMTMVVVTHE-----MgfarevADRVV 207
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-238 |
2.93e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 190.65 E-value: 2.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVS---LEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMV-------PLRS-AGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVA 155
Cdd:COG3638 80 R-RIGMIFQQFNLVPRLSVLTNVLAgrlgrtsTWRSlLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVAT-HDsrmlpmadrvVELTPDFAetnrpPETVHLQAG 234
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNlHQ----------VDLARRYA-----DRIIGLRDG 223
|
....
gi 15607215 235 EVLF 238
Cdd:COG3638 224 RVVF 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-215 |
3.20e-58 |
|
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: 187.26 E-value: 3.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMsrRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG4181 89 ARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELAD--GERVVVVaTHDSRMLPMADRVVEL 215
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLV-THDPALAARCDRVLRL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-213 |
7.32e-58 |
|
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: 185.81 E-value: 7.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVvEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtLQGAELANYR 83
Cdd:cd03262 1 IEIKNLH-KSFGDFHVLK---GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPLRSA-GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDP 162
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDsrmlpM------ADRVV 213
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE-----MgfarevADRVI 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-213 |
2.82e-55 |
|
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: 180.01 E-value: 2.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANY 82
Cdd:cd03261 1 IELRGLTKSF--GG---RTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRnKVGIVFQAFNLVPSLTAVENVMVPLRSAG-MSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALD 161
Cdd:cd03261 76 RR-RMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 162 PPLILADEPTAHLDFIQVEEVLRLIRELAD--GERVVVVaTHD-SRMLPMADRVV 213
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMV-THDlDTAFAIADRIA 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-242 |
3.33e-55 |
|
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: 180.07 E-value: 3.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:cd03256 1 IEVENLSKTYPNGKKAL---KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMV-------PLRS-AGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVA 155
Cdd:cd03256 78 R-QIGMIFQQFNLIERLSVLENVLSgrlgrrsTWRSlFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVAT-HDsrmlpmadrvVELTPDFAetnrpPETVHLQAG 234
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSlHQ----------VDLAREYA-----DRIVGLKDG 221
|
....*...
gi 15607215 235 EVLFEQST 242
Cdd:cd03256 222 RIVFDGPP 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-213 |
5.58e-55 |
|
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: 179.40 E-value: 5.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANY 82
Cdd:COG1127 6 IEVRNLTKSF--GD---RVVlDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRnKVGIVFQA---FNlvpSLTAVENVMVPLR-SAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAI 158
Cdd:COG1127 81 RR-RIGMLFQGgalFD---SLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD-SRMLPMADRVV 213
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLtSVVVTHDlDSAFAIADRVA 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-217 |
6.53e-54 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 177.20 E-value: 6.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGaelanyr 83
Cdd:COG1116 8 LELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 rnKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG1116 81 --DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 164 LILADEPTAHLDFI-----QvEEVLRLIRELadgERVVVVATHDsrmLP----MADRVVELTP 217
Cdd:COG1116 159 VLLMDEPFGALDALtrerlQ-DELLRLWQET---GKTVLFVTHD---VDeavfLADRVVVLSA 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-215 |
1.02e-53 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 175.62 E-value: 1.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:TIGR02211 2 LKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRMLPMADRVVEL 215
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKKLDRVLEM 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-213 |
1.46e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 179.14 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgaELA 80
Cdd:COG3842 3 MPALELENVSK-RYGDVTALD---DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 NYRRNkVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIAL 160
Cdd:COG3842 74 PEKRN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 161 DPPLILADEPTAHLD-FIQVE---EVLRLIRELadgERVVVVATHD-SRMLPMADRVV 213
Cdd:COG3842 153 EPRVLLLDEPLSALDaKLREEmreELRRLQREL---GITFIYVTHDqEEALALADRIA 207
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
23-215 |
4.26e-53 |
|
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: 173.19 E-value: 4.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQAFNLVPSLTA 102
Cdd:TIGR03608 14 LDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENETV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:TIGR03608 94 EENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEV 173
|
170 180 190
....*....|....*....|....*....|...
gi 15607215 183 LRLIRELADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:TIGR03608 174 LDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-217 |
7.93e-53 |
|
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: 173.04 E-value: 7.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevdittlqGAELANyR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD--------GEPVTG-P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 164 LILADEPTAHLDF-----IQvEEVLRLIRELadgERVVVVATHD-SRMLPMADRVVELTP 217
Cdd:cd03293 152 VLLLDEPFSALDAltreqLQ-EELLDIWRET---GKTVLLVTHDiDEAVFLADRVVVLSA 207
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-215 |
1.51e-52 |
|
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: 172.05 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 6 IQNLVVEYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRn 85
Cdd:TIGR02673 4 FHNVSKAYPGGVAAL---HDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 86 KVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLI 165
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 166 LADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLP-MADRVVEL 215
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDrVAHRVIIL 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
23-213 |
4.50e-52 |
|
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: 170.78 E-value: 4.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaelANYRRNkVGIVFQAFNLVPSLTA 102
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-----PPERRN-IGMVFQDYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:cd03259 90 AENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREEL 169
|
170 180 190
....*....|....*....|....*....|...
gi 15607215 183 LRLIREL-ADGERVVVVATHD-SRMLPMADRVV 213
Cdd:cd03259 170 REELKELqRELGITTIYVTHDqEEALALADRIA 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-215 |
9.03e-52 |
|
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: 169.96 E-value: 9.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 5 SIQNLVVEYYSGG-YALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyr 83
Cdd:cd03225 1 ELKNLSFSYPDGArPALD---DISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQA-----FNLvpslTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAI 158
Cdd:cd03225 74 RRKVGLVFQNpddqfFGP----TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVVEL 215
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELADRVIVL 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-215 |
1.66e-51 |
|
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: 170.07 E-value: 1.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:cd03258 82 R-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD--------SRMLPMAD-RVVEL 215
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLtIVLITHEmevvkricDRVAVMEKgEVVEE 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-215 |
1.57e-50 |
|
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: 167.20 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 10 VVEYYSGGYAlrPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRnKVGI 89
Cdd:cd03292 6 VTKTYPNGTA--ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 90 VFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15607215 170 PTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRML-PMADRVVEL 215
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVdTTRHRVIAL 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-213 |
1.77e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 170.64 E-value: 1.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG1135 82 R-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDsrmlpM------ADRVV 213
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLtIVLITHE-----MdvvrriCDRVA 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-202 |
1.79e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 165.27 E-value: 1.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevDITTLQGAELANYRRNKVGIVFQAFNLVPSLTA 102
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD--GLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMV-PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:PRK09493 95 LENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHE 174
|
170 180
....*....|....*....|.
gi 15607215 182 VLRLIRELADGERVVVVATHD 202
Cdd:PRK09493 175 VLKVMQDLAEEGMTMVIVTHE 195
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-213 |
2.54e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 2.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgaELANYR 83
Cdd:COG1131 1 IEVRGLTK-RYGDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG1131 73 R-RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVV 213
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVA 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-213 |
3.04e-49 |
|
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: 164.22 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqGAELANYR 83
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKL-SRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQ----AFNlvPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNL---AERMNHRPGDLSGGQQQRVAVAR 156
Cdd:cd03257 81 RKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 157 AIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRML-PMADRVV 213
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLtLLFITHDLGVVaKIADRVA 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-213 |
5.04e-49 |
|
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: 171.24 E-value: 5.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGY-ALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANY 82
Cdd:COG1123 261 LEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRnKVGIVFQ----AFNlvPSLTAVENVMVPLRSAGMSRRASRRRA-EELLARVNLAERMNHR-PGDLSGGQQQRVAVAR 156
Cdd:COG1123 341 RR-RVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLLSRAERRERvAELLERVGLPPDLADRyPHELSGGQRQRVAIAR 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 157 AIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD-SRMLPMADRVV 213
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLtYLFISHDlAVVRYIADRVA 476
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-213 |
5.70e-49 |
|
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: 164.06 E-value: 5.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELAny 82
Cdd:COG1120 2 LEAENLSVGY--GG---RPVlDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRnkVGIVFQAFNLVPSLTAVENVMV---PLRSA-GMSRRASRRRAEELLARVNLAErMNHRP-GDLSGGQQQRVAVARA 157
Cdd:COG1120 75 RR--IAYVPQEPPAPFGLTVRELVALgryPHLGLfGRPSAEDREAVEEALERTGLEH-LADRPvDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 158 IALDPPLILADEPTAHLDFIQVEEVLRLIRELADGE-RVVVVATHDsrmLPMA----DRVV 213
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVMVLHD---LNLAaryaDRLV 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-215 |
7.45e-49 |
|
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: 163.27 E-value: 7.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyr 83
Cdd:COG1122 1 IELENLSFSYPGGTPALD---DVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQafN----LVpSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIA 159
Cdd:COG1122 74 RRKVGLVFQ--NpddqLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 160 LDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRML-PMADRVVEL 215
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVaELADRVIVL 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-239 |
1.26e-48 |
|
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: 163.24 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNIN---LNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPLRSA--------GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVA 155
Cdd:TIGR02315 79 R-RIGMIFQHYNLIERLTVLENVLHGRLGYkptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVAT-HDsrmlpmadrvVELTPDFAetnrpPETVHLQAG 234
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINlHQ----------VDLAKKYA-----DRIVGLKAG 222
|
....*
gi 15607215 235 EVLFE 239
Cdd:TIGR02315 223 EIVFD 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-213 |
1.60e-47 |
|
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: 159.91 E-value: 1.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGyaLRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaelaNYR 83
Cdd:cd03219 1 LEVRGLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-----PHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIV--FQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEE----------LLARVNLAERMNHRPGDLSGGQQQR 151
Cdd:cd03219 72 IARLGIGrtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREereareraeeLLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 152 VAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVV 213
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDmDVVMSLADRVT 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-213 |
4.73e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 156.83 E-value: 4.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTL----QGAELANYRRNKVGIVFQAFNLVP 98
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsQQKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 99 SLTAVENVMV-PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFI 177
Cdd:PRK11264 99 HRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 178 QVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVV 213
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKRTMVIVTHEmSFARDVADRAI 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-213 |
1.61e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 158.31 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAEla 80
Cdd:COG3839 1 MASLELENVSK-SYGGVEALK---DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNkVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIAL 160
Cdd:COG3839 75 ---RN-IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 161 DPPLILADEPTAHLDF---IQV-EEVLRLIRELAdgeRVVVVATHDSR-MLPMADRVV 213
Cdd:COG3839 151 EPKVFLLDEPLSNLDAklrVEMrAEIKRLHRRLG---TTTIYVTHDQVeAMTLADRIA 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-213 |
1.76e-45 |
|
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: 152.73 E-value: 1.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 10 VVEYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANyrRNKVGI 89
Cdd:cd03229 6 VSKRYGQKTVL---NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL--RRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 90 VFQAFNLVPSLTAVENVMVPlrsagmsrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15607215 170 PTAHLDFIQVEEVLRLIRELADGERV-VVVATHD-SRMLPMADRVV 213
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGItVVLVTHDlDEAARLADRVV 172
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-215 |
3.61e-45 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 162.97 E-value: 3.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-213 |
4.96e-45 |
|
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: 151.82 E-value: 4.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 5 SIQNLVVEYysGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANyrr 84
Cdd:cd03214 1 EVENLSVGY--GGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 85 nKVGIVFQAfnlvpsltavenvmvplrsagmsrrasrrraeelLARVNLAErMNHRP-GDLSGGQQQRVAVARAIALDPP 163
Cdd:cd03214 74 -KIAYVPQA----------------------------------LELLGLAH-LADRPfNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGE-RVVVVATHD-SRMLPMADRVV 213
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERgKTVVMVLHDlNLAARYADRVI 169
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-213 |
3.88e-44 |
|
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: 154.42 E-value: 3.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYsggyALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAela 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyRRNkVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIAL 160
Cdd:TIGR03265 75 --KRD-YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 161 DPPLILADEPTAHLDfIQVEEVLRliRELADGERVV----VVATHDS-RMLPMADRVV 213
Cdd:TIGR03265 152 SPGLLLLDEPLSALD-ARVREHLR--TEIRQLQRRLgvttIMVTHDQeEALSMADRIV 206
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-213 |
6.30e-44 |
|
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: 150.46 E-value: 6.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 14 YSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgaELANYRRNkVGIVFQA 93
Cdd:cd03300 10 YGGFVAL---DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHKRP-VNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 94 FNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAH 173
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15607215 174 LDF-----IQVeEVLRLIRELadGERVVVVaTHD-SRMLPMADRVV 213
Cdd:cd03300 161 LDLklrkdMQL-ELKRLQKEL--GITFVFV-THDqEEALTMSDRIA 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-213 |
8.54e-44 |
|
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: 150.02 E-value: 8.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGIL-----RPKSGAIKFDEVDITTLQGAE 78
Cdd:cd03260 1 IELRDLNV-YYGDKHALK---DISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LAnyRRNKVGIVFQAFNLVPsLTAVENVMVPLRSAGMSRRASR-RRAEELLARVNLAERMNHR--PGDLSGGQQQRVAVA 155
Cdd:cd03260 77 LE--LRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADgERVVVVATHD----SRmlpMADRVV 213
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNmqqaAR---VADRTA 211
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
4-213 |
1.14e-43 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 149.48 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:NF038007 2 LNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:NF038007 82 RELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVV 213
Cdd:NF038007 162 LLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRII 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-213 |
2.44e-43 |
|
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: 151.36 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPK---SGAIKFDEVDITTLQGAELA 80
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 NYRRNKVGIVFQ----AFNlvPSLTAVENVMVPLRS-AGMSRRASRRRAEELLARVNL---AERMNHRPGDLSGGQQQRV 152
Cdd:COG0444 82 KIRGREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 153 AVARAIALDPPLILADEPTAHLDF-IQVeEVLRLIRELADgERV--VVVATHDsrmLP----MADRVV 213
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVtIQA-QILNLLKDLQR-ELGlaILFITHD---LGvvaeIADRVA 222
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-217 |
6.12e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 148.86 E-value: 6.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlQGAEla 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGAD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRnkvGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIAL 160
Cdd:COG4525 78 ---R---GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 161 DPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD-SRMLPMADRVVELTP 217
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKgVFLITHSvEEALFLATRLVVMSP 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-213 |
6.67e-43 |
|
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: 148.65 E-value: 6.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGyaLRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaelANYR 83
Cdd:COG0411 5 LEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL-----PPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIV--FQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEE---------------LLARVNLAERMNHRPGDLSG 146
Cdd:COG0411 76 IARLGIArtFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPrarreereareraeeLLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 147 GQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRMLpM--ADRVV 213
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGItILLIEHDMDLV-MglADRIV 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-213 |
7.58e-43 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 148.08 E-value: 7.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDIttlqgAELANYR 83
Cdd:COG4555 2 IEVENLSK-KYGKVPAL---KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-----RKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVV 213
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHImQEVEALCDRVV 203
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-213 |
3.42e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 149.14 E-value: 3.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAelanyR 83
Cdd:COG1118 3 IEVRNISKRF--GSFTL--LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPP-----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15607215 164 LILADEPTAHLDfIQVEEVLR--LIRELADGERVVVVATHDsRM--LPMADRVV 213
Cdd:COG1118 154 VLLLDEPFGALD-AKVRKELRrwLRRLHDELGGTTVFVTHD-QEeaLELADRVV 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-218 |
4.21e-42 |
|
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: 147.02 E-value: 4.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQAFNLVPSLTA 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD-FIQVE- 180
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpLIRREm 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15607215 181 --EVLRLIRELadgERVVVVATHD--------SRMLPMAD-RVVEL-TPD 218
Cdd:cd03294 200 qdELLRLQAEL---QKTIVFITHDldealrlgDRIAIMKDgRLVQVgTPE 246
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-215 |
4.55e-42 |
|
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: 146.10 E-value: 4.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqGAELANYR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQ----AFNlvPSLTAVENVMVPLRSAGMSRRASRRRAeeLLARVNLAERMNHR-PGDLSGGQQQRVAVARAI 158
Cdd:COG1124 79 R-RVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPDREERIAE--LLEQVGLPPSFLDRyPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIREL-ADGERVVVVATHDSRMLP-MADRVVEL 215
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAhLCDRVAVM 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-217 |
5.18e-42 |
|
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: 144.54 E-value: 5.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgAELANY 82
Cdd:COG4133 3 LEAENLSCRR--GE---RLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----DAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRNkVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAeeLLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDP 162
Cdd:COG4133 74 RRR-LAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPmADRVVELTP 217
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA-AARVLDLGD 204
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-202 |
6.05e-42 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 146.10 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 25 GLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQG----AELANYR-----RNKVGIVFQAFN 95
Cdd:COG4598 26 GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgeLVPADRRqlqriRTRLGMVFQSFN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVENVM-VPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHL 174
Cdd:COG4598 106 LWSHMTVLENVIeAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180
....*....|....*....|....*...
gi 15607215 175 DFIQVEEVLRLIRELADGERVVVVATHD 202
Cdd:COG4598 186 DPELVGEVLKVMRDLAEEGRTMLVVTHE 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-215 |
2.13e-41 |
|
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: 150.82 E-value: 2.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGgyALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPK---SGAIKFDEVDITTLQGAEla 80
Cdd:COG1123 5 LEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyRRNKVGIVFQ--AFNLVPsLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAI 158
Cdd:COG1123 81 --RGRRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD-SRMLPMADRVVEL 215
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITHDlGVVAEIADRVVVM 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-215 |
3.02e-41 |
|
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: 141.23 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 5 SIQNLVVEYYsGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrR 84
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVS---LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 85 NKVGIVFQafnlvpsltavenvmvplrsagmsrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALDPPL 164
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15607215 165 ILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMA-DRVVEL 215
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-172 |
5.50e-41 |
|
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: 140.09 E-value: 5.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrRNKVGIVFQAFNLVPSLTA 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNL----AERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTA 172
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-213 |
1.94e-40 |
|
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: 141.67 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 10 VVEYYSGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrRNKVGI 89
Cdd:cd03295 6 VTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL----RRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 90 VFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNL--AERMNHRPGDLSGGQQQRVAVARAIALDPPLILA 167
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15607215 168 DEPTAHLDFI-----QvEEVLRLIRELAdgeRVVVVATHD-SRMLPMADRVV 213
Cdd:cd03295 160 DEPFGALDPItrdqlQ-EEFKRLQQELG---KTIVFVTHDiDEAFRLADRIA 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-213 |
4.23e-40 |
|
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: 140.08 E-value: 4.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 10 VVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAElanyrRNkVGI 89
Cdd:cd03301 6 VTKRFGNVTALD---DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 90 VFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 170 PTAHLD-FIQVE---EVLRLIRELadgERVVVVATHD-SRMLPMADRVV 213
Cdd:cd03301 157 PLSNLDaKLRVQmraELKRLQQRL---GTTTIYVTHDqVEAMTMADRIA 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-215 |
5.81e-40 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 138.30 E-value: 5.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgaELANYR 83
Cdd:cd03230 1 IEVRNLSK-RYGKKTAL---DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVmvplrsagmsrrasrrraeellarvnlaermnhrpgDLSGGQQQRVAVARAIALDPP 163
Cdd:cd03230 73 R-RIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLP-MADRVVEL 215
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAErLCDRVAIL 168
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-215 |
1.83e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgaelanyR 83
Cdd:COG1121 7 IELENLTV-SYGGRPVLE---DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPS--LTAVENVMVPLRSA----GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARA 157
Cdd:COG1121 74 RRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 158 IALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVVEL 215
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDlGAVREYFDRVLLL 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-214 |
2.90e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 138.61 E-value: 2.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQ-NLVVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAI-----KFD-EVDITTLQG 76
Cdd:COG4161 1 MSIQlKNINCFYGSHQALFDIN---LECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghQFDfSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 AELanyrRNKVGIVFQAFNLVPSLTAVENVM-VPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVA 155
Cdd:COG4161 78 RLL----RQKVGMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD--------SRMLPMAD-RVVE 214
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEvefarkvaSQVVYMEKgRIIE 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-214 |
3.78e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 138.22 E-value: 3.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQ-NLVVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAI-----KFD-EVDITTLQG 76
Cdd:PRK11124 1 MSIQlNGINCFYGAHQALFDIT---LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDfSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 AELanyrRNKVGIVFQAFNLVPSLTAVENVM-VPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVA 155
Cdd:PRK11124 78 REL----RRNVGMVFQQYNLWPHLTVQQNLIeAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD--------SRMLPMAD-RVVE 214
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEvevarktaSRVVYMENgHIVE 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-213 |
4.40e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 139.84 E-value: 4.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyRRNkVGIVFQAFNLVPSLTA 102
Cdd:COG1125 18 VDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RRR-IGYVIQQIGLFPHMTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNL-AERMNHR-PGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFI--- 177
Cdd:COG1125 94 AENIATVPRLLGWDKERIRARVDELLELVGLdPEEYRDRyPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPItre 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 178 --QvEEVLRLIRELadGERVVVVaTHDsrM---LPMADRVV 213
Cdd:COG1125 174 qlQ-DELLRLQREL--GKTIVFV-THD--IdeaLKLGDRIA 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-189 |
4.43e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 141.09 E-value: 4.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 6 IQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRn 85
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 86 KVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLI 165
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180
....*....|....*....|....
gi 15607215 166 LADEPTAHLDFIQVEEVLRLIREL 189
Cdd:PRK11153 163 LCDEATSALDPATTRSILELLKDI 186
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-213 |
5.25e-39 |
|
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: 137.18 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgaeLANYR 83
Cdd:cd03224 1 LEVENLNA-GYGKSQILF---GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-----LPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVF--QAFNLVPSLTAVENvmvpLRSAGMSRRASRRRAEelLARV-----NLAERMNHRPGDLSGGQQQRVAVAR 156
Cdd:cd03224 72 RARAGIGYvpEGRRIFPELTVEEN----LLLGAYARRRAKRKAR--LERVyelfpRLKERRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 157 AIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRM-LPMADRVV 213
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFaLEIADRAY 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-210 |
5.91e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 137.64 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:PRK11629 86 NQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIREL--ADGERVVVVaTHD-------SRMLPMAD 210
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVV-THDlqlakrmSRQLEMRD 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-213 |
1.22e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 136.81 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGYALRpingLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaelANYR 83
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-----PPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:COG3840 71 R-PVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADgER--VVVVATHDSR-MLPMADRVV 213
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCR-ERglTVLMVTHDPEdAARIADRVL 201
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-217 |
2.11e-38 |
|
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: 136.02 E-value: 2.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 16 GGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD----EVDITTLQGAELANYRRNKVGIVF 91
Cdd:COG4778 20 GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREILALRRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 92 QAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNH-RPGDLSGGQQQRVAVARAIALDPPLILADEP 170
Cdd:COG4778 100 QFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15607215 171 TAHLDFIQVEEVLRLIREL-ADGERVVVVATHDSRMLPMADRVVELTP 217
Cdd:COG4778 180 TASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-213 |
6.98e-38 |
|
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: 134.72 E-value: 6.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaelANYR 83
Cdd:COG0410 4 LEVENLHA-GYGGIHVLH---GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-----PPHR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVF--QAFNLVPSLTAVENVMVPLRSAGMSRRASRRraeelLARV-----NLAERMNHRPGDLSGGQQQRVAVAR 156
Cdd:COG0410 75 IARLGIGYvpEGRRIFPSLTVEENLLLGAYARRDRAEVRAD-----LERVyelfpRLKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 157 AIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRM-LPMADRVV 213
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFaLEIADRAY 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-230 |
8.51e-38 |
|
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: 137.24 E-value: 8.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 38 LLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgaELANYRRNkVGIVFQAFNLVPSLTAVENVMVPLRSAGMSR 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRH-INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 118 RASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDF-----IQvEEVLRLIRELadG 192
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKklrdqMQ-LELKTIQEQL--G 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 15607215 193 ERVVVVaTHDSR-MLPMADRVVELTPDFAETNRPPETVH 230
Cdd:TIGR01187 152 ITFVFV-THDQEeAMTMSDRIAIMRKGKIAQIGTPEEIY 189
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-215 |
1.88e-37 |
|
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: 140.66 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 3 DLSIQNLVVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELany 82
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLS---LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW--- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 rRNKVGIVFQ---------AFNL-----VPSLTAVENVmvpLRSAGMsrrasrrraEELLARvnLAERMNHRPGD----L 144
Cdd:COG4988 410 -RRQIAWVPQnpylfagtiRENLrlgrpDASDEELEAA---LEAAGL---------DEFVAA--LPDGLDTPLGEggrgL 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 145 SGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGeRVVVVATHDSRMLPMADRVVEL 215
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RTVILITHRLALLAQADRILVL 544
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-215 |
4.05e-37 |
|
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: 130.97 E-value: 4.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrRNKVGIVFQAFNLVpSLTA 102
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLF-SGTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVmvplrsagmsrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:cd03228 93 RENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|...
gi 15607215 183 LRLIRELADGeRVVVVATHDSRMLPMADRVVEL 215
Cdd:cd03228 136 LEALRALAKG-KTVIVIAHRLSTIRDADRIIVL 167
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
21-213 |
3.38e-36 |
|
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: 130.54 E-value: 3.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaelaNYRRNKVGIVFQAFNLVPSL 100
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PVQERNVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 TAVENVMVPLR----SAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDF 176
Cdd:cd03296 90 TVFDNVAFGLRvkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 15607215 177 IQVEEVLRLIRELADGERVV-VVATHD-SRMLPMADRVV 213
Cdd:cd03296 170 KVRKELRRWLRRLHDELHVTtVFVTHDqEEALEVADRVV 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-215 |
1.29e-35 |
|
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: 128.14 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 5 SIQNLVVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaelanyRR 84
Cdd:cd03226 1 RIENISFSYKKGTEILD---DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 85 NKVGIV-----FQAFNlvpsltavENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIA 159
Cdd:cd03226 71 KSIGYVmqdvdYQLFT--------DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 160 LDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPM-ADRVVEL 215
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKvCDRVLLL 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-229 |
2.18e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.93 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDIT-------TLQGAELANYR--RNKVGIVFQA 93
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVADKNQLRllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 94 FNLVPSLTAVENVM-VPLRSAGMSRRASRRRAEELLARVNLAERMNHR-PGDLSGGQQQRVAVARAIALDPPLILADEPT 171
Cdd:PRK10619 101 FNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 172 AHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLP-MADRVVELTPDFAETNRPPETV 229
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
23-213 |
3.08e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.61 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgAElanyRRNkVGIVFQAFNLVPSLTA 102
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AE----NRH-VNTVFQSYALFPHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDF-----I 177
Cdd:PRK09452 104 FENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYklrkqM 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 178 QVeEVLRLIRELadGERVVVVaTHDS-RMLPMADRVV 213
Cdd:PRK09452 184 QN-ELKALQRKL--GITFVFV-THDQeEALTMSDRIV 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-213 |
3.67e-35 |
|
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: 126.92 E-value: 3.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGgyalRPINGLNLDVAAGSLVmLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgaELANYR 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-----KQPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADgERVVVVATHD-SRMLPMADRVV 213
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIvEDVESLCNQVA 200
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-217 |
3.89e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 3.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLvveyySGGYALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAElanY 82
Cdd:COG4619 1 LELEGL-----SFRVGGKPIlSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---W 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRnKVGIVFQafnlVPSL---TAVENVMVPLRSAGmsRRASRRRAEELLARVNLAERMNHRP-GDLSGGQQQRVAVARAI 158
Cdd:COG4619 73 RR-QVAYVPQ----EPALwggTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRMLP-MADRVVELTP 217
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRaVLWVSHDPEQIErVADRVLTLEA 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-220 |
6.44e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 127.51 E-value: 6.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 9 LVVEYYSGGYALRP-INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlQGAELanyrrnkv 87
Cdd:PRK11248 2 LQISHLYADYGGKPaLEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 88 GIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILA 167
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 168 DEPTAHLDFIQVEE----VLRLIRELA--------DGERVVVVATHDSRMLPMADRVVE-LTPDFA 220
Cdd:PRK11248 153 DEPFGALDAFTREQmqtlLLKLWQETGkqvllithDIEEAVFMATELVLLSPGPGRVVErLPLNFA 218
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-201 |
1.37e-34 |
|
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: 126.64 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGI--LRPK---SGAIKFDEVDITTlQGAE 78
Cdd:TIGR00972 2 IEIENLNL-FYGEKEALKNIN---LDIPKNQVTALIGPSGCGKSTLLRSLNRMndLVPGvriEGKVLFDGQDIYD-KKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LANYRRnKVGIVFQAFNLVPsLTAVENVMVPLRSAGMSR-RASRRRAEELLARVNLAE----RMNHRPGDLSGGQQQRVA 153
Cdd:TIGR00972 77 VVELRR-RVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDkKELDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRLC 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15607215 154 VARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVaTH 201
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIV-TH 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-215 |
2.85e-34 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.57 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 5 SIQNLVVEYYSggyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgaelanYR 83
Cdd:cd03235 1 EVEDLTVSYGG-----HPVlEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE---------KE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTA-VENV--MVPLRSAGMSRRASRR---RAEELLARVNLAERMNHRPGDLSGGQQQRVAVARA 157
Cdd:cd03235 67 RKRIGYVPQRRSIDRDFPIsVRDVvlMGLYGHKGLFRRLSKAdkaKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 158 IALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVVEL 215
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-215 |
8.18e-34 |
|
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: 130.27 E-value: 8.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELan 81
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL-- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 yrRNKVGIVFQA---F------NL---VPSLTAVEnvmvpLRSAgmsrrasrrraeelLARVNLAERMNHRPGDL----- 144
Cdd:COG4987 408 --RRRIAVVPQRphlFdttlreNLrlaRPDATDEE-----LWAA--------------LERVGLGDWLAALPDGLdtwlg 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 145 ------SGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGeRVVVVATHDSRMLPMADRVVEL 215
Cdd:COG4987 467 eggrrlSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG-RTVLLITHRLAGLERMDRILVL 542
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-213 |
9.24e-34 |
|
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: 123.99 E-value: 9.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaelaNYR 83
Cdd:cd03299 1 LKVENLSKDW--KEFKLK---NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL------PPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 164 LILADEPTAHLDfIQVEEVLR-LIRELADGERVVVV-ATHD-SRMLPMADRVV 213
Cdd:cd03299 150 ILLLDEPFSALD-VRTKEKLReELKKIRKEFGVTVLhVTHDfEEAWALADKVA 201
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-217 |
1.12e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 126.38 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYY-SGGYALRPI------NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQG 76
Cdd:COG4608 8 LEVRDLKKHFPvRGGLFGRTVgvvkavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 AELANYRRnKVGIVFQ----AFNlvPSLTAVENVMVPLRSAGMSRRASRRR-AEELLARVNL-AERMNHRPGDLSGGQQQ 150
Cdd:COG4608 88 RELRPLRR-RMQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGLASKAERRErVAELLELVGLrPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 151 RVAVARAIALDPPLILADEPTAHLDF-IQVeEVLRLIRELAD--GERVVVVAtHDSRMLP-MADRV--------VELTP 217
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVsIQA-QVLNLLEDLQDelGLTYLFIS-HDLSVVRhISDRVavmylgkiVEIAP 241
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-215 |
1.37e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 123.35 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 16 GGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQAFN 95
Cdd:PRK10584 19 GEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:PRK10584 99 LIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 176 FIQVEEVLRLIREL-ADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:PRK10584 179 RQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-215 |
1.42e-33 |
|
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: 130.72 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaELAN 81
Cdd:COG2274 472 GDIELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 YRRNkVGIVFQ---------AFNLV-----PSLTAVENVmvpLRSAGmsrrasrrraeeLLARVN-LAERMNHRPGD--- 143
Cdd:COG2274 547 LRRQ-IGVVLQdvflfsgtiRENITlgdpdATDEEIIEA---ARLAG------------LHDFIEaLPMGYDTVVGEggs 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 144 -LSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGeRVVVVATHDSRMLPMADRVVEL 215
Cdd:COG2274 611 nLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG-RTVIIIAHRLSTIRLADRIIVL 682
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-201 |
2.23e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.61 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGI--LRPK---SGAIKFDEVDITTlQGAE 78
Cdd:COG1117 12 IEVRNLNV-YYGDKQALKDIN---LDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYD-PDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LANYRRnKVGIVFQAFNLVPsLTAVENVMVPLRSAGMsrrasrrraeelLARVNLAE-----------------RMNHRP 141
Cdd:COG1117 87 VVELRR-RVGMVFQKPNPFP-KSIYDNVAYGLRLHGI------------KSKSELDEiveeslrkaalwdevkdRLKKSA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 142 GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFI---QVEEvlrLIRELADgERVVVVATH 201
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIstaKIEE---LILELKK-DYTIVIVTH 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-202 |
2.56e-33 |
|
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: 122.23 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGG-YALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaelaNY 82
Cdd:cd03263 1 LQIRNLTKTYKKGTkPAV---DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-----KA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDP 162
Cdd:cd03263 73 ARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGeRVVVVATHD 202
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKG-RSIILTTHS 191
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-213 |
4.30e-33 |
|
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: 123.31 E-value: 4.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGG-YALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevDITTLQGAELANY 82
Cdd:TIGR04520 1 IEVENVSFSYPESEkPAL---KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD--GLDTLDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRnKVGIVFQ---------------AFNLvpsltavENVMVPlrSAGMSRRASRRraeelLARVNLAERMNHRPGDLSGG 147
Cdd:TIGR04520 76 RK-KVGMVFQnpdnqfvgatveddvAFGL-------ENLGVP--REEMRKRVDEA-----LKLVGMEDFRDREPHLLSGG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 148 QQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVA-THDSRMLPMADRVV 213
Cdd:TIGR04520 141 QKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISiTHDMEEAVLADRVI 207
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-213 |
1.42e-32 |
|
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: 120.35 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 27 NLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaelANYRRnKVGIVFQAFNLVPSLTAVENV 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-----APYQR-PVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 107 MVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLI 186
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180
....*....|....*....|....*....
gi 15607215 187 RELADGER--VVVVATHDSRMLPMADRVV 213
Cdd:TIGR01277 172 KQLCSERQrtLLMVTHHLSDARAIASQIA 200
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-215 |
3.01e-32 |
|
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: 125.86 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPingLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVditTLQGAELANYR 83
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRP---VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV---PLADADADSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSlTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRP-GD----LSGGQQQRVAVARAI 158
Cdd:TIGR02857 396 D-QIAWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPiGEggagLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGeRVVVVATHDSRMLPMADRVVEL 215
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG-RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-202 |
3.52e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.59 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 10 VVEYYSGGYalRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRnKVGI 89
Cdd:PRK10908 7 VSKAYLGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 90 VFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|...
gi 15607215 170 PTAHLDFIQVEEVLRLIRELADGERVVVVATHD 202
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHD 196
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-216 |
4.50e-32 |
|
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: 118.94 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLD-VAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDI-TTLQGAELANYRRnKVGIVFQAFNLVPSLTAV 103
Cdd:cd03297 15 LKIDfDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPPQQR-KIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 104 ENVMVPLRsaGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVL 183
Cdd:cd03297 94 ENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 15607215 184 RLIREL-ADGERVVVVATHD-SRMLPMADRVVELT 216
Cdd:cd03297 172 PELKQIkKNLNIPVIFVTHDlSEAEYLADRIVVME 206
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-202 |
5.63e-32 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 117.91 E-value: 5.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIkfdevditTLQGAELANYR------RNKVGIVFQ-AFN 95
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAV--------LIDGEPLDYSRkgllerRQRVGLVFQdPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVN---LAERMNHRpgdLSGGQQQRVAVARAIALDPPLILADEPTA 172
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGasgLRERPTHC---LSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|
gi 15607215 173 HLDFIQVEEVLRLIRELADGERVVVVATHD 202
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-202 |
9.15e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.35 E-value: 9.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 3 DLSIQNLVVeyysgGYALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELAN 81
Cdd:PRK11231 2 TLRTENLTV-----GYGTKRIlNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 YrrnkVGIVFQAfNLVPSLTAVENVMVPLRSA-----GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVAR 156
Cdd:PRK11231 77 R----LALLPQH-HLTPEGITVRELVAYGRSPwlslwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15607215 157 AIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD 202
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD 197
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-213 |
1.63e-31 |
|
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: 118.01 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaelANYR 83
Cdd:TIGR03410 1 LEVSNLNV-YYGQSHILR---GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL-----PPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGI--VFQAFNLVPSLTAVENVMVPLRSAGmsrRASRRRAEELLARVNLAERMNHRP-GDLSGGQQQRVAVARAIAL 160
Cdd:TIGR03410 72 RARAGIayVPQGREIFPRLTVEENLLTGLAALP---RRSRKIPDEIYELFPVLKEMLGRRgGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 161 DPPLILADEPTahlDFIQ---VEEVLRLIRELAD--GERVVVVATHDSRMLPMADRVV 213
Cdd:TIGR03410 149 RPKLLLLDEPT---EGIQpsiIKDIGRVIRRLRAegGMAILLVEQYLDFARELADRYY 203
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
23-228 |
1.68e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.96 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGaelanyRRNKVGIVFQAFNLVPSLTA 102
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRKVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENV-----MVPLRSAgMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDfI 177
Cdd:PRK10851 92 FDNIafgltVLPRRER-PNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD-A 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 178 QV-EEVLRLIRELADGERVV-VVATHDSR-MLPMADRVVEL---------TPDfaETNRPPET 228
Cdd:PRK10851 170 QVrKELRRWLRQLHEELKFTsVFVTHDQEeAMEVADRVVVMsqgnieqagTPD--QVWREPAT 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-220 |
4.16e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.43 E-value: 4.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeyYSGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPK---SGAIKFDEVDITTLQgaelA 80
Cdd:COG4136 2 LSLENLTI--TLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP----A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 NYRRnkVGIVFQAFNLVPSLTAVENVMVPLRsAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIAL 160
Cdd:COG4136 74 EQRR--IGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 161 DPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRMLPMADRVVELTPDFA 220
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpALLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-215 |
2.76e-30 |
|
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: 114.13 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAElanyrrNKVGIVFQAFNLVPSLTAVEN 105
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 106 VMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRL 185
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|..
gi 15607215 186 IREL--ADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:cd03298 171 VLDLhaETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
23-213 |
8.38e-30 |
|
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: 112.70 E-value: 8.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAelanyrRNKVGIVFQAFNLVPSLTA 102
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------LRRIGALIEAPGFYPNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENvmvpLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:cd03268 90 REN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170 180 190
....*....|....*....|....*....|..
gi 15607215 183 LRLIRELADGERVVVVATHD-SRMLPMADRVV 213
Cdd:cd03268 166 RELILSLRDQGITVLISSHLlSEIQKVADRIG 197
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-213 |
9.32e-30 |
|
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: 114.47 E-value: 9.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 11 VEY-YSGG--YALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRnKV 87
Cdd:TIGR04521 6 VSYiYQPGtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK-KV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 88 GIVFQ-----AFnlvpSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHR-PGDLSGGQQQRVAVARAIALD 161
Cdd:TIGR04521 85 GLVFQfpehqLF----EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAME 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 162 PPLILADEPTAHLDFIQVEEVLRLIRELAD--GERVVVVaTHDsrM---LPMADRVV 213
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKekGLTVILV-THS--MedvAEYADRVI 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-213 |
1.82e-29 |
|
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: 112.08 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgaELANYRRNkVGIVFQAFNLVPSLTA 102
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEARRR-LGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:cd03266 96 RENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190
....*....|....*....|....*....|..
gi 15607215 183 LRLIRELADGERVVVVATHD-SRMLPMADRVV 213
Cdd:cd03266 176 REFIRQLRALGKCILFSTHImQEVERLCDRVV 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-213 |
2.51e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEY-YSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKfdeVDITTLQGAELANY 82
Cdd:PRK13635 6 IRVEHISFRYpDAATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTIT---VGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRnKVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALD 161
Cdd:PRK13635 80 RR-QVGMVFQnPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 162 PPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVA-THDSRMLPMADRVV 213
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAAQADRVI 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-210 |
2.89e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 112.94 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRnKVGIVFQAFNLVPS 99
Cdd:PRK11831 20 RCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 LTAVENVMVPLRS-AGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQ 178
Cdd:PRK11831 99 MNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180 190
....*....|....*....|....*....|....*
gi 15607215 179 VEEVLRLIREL--ADGERVVVVaTHD-SRMLPMAD 210
Cdd:PRK11831 179 MGVLVKLISELnsALGVTCVVV-SHDvPEVLSIAD 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-245 |
2.98e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDIT--TLQGAELAnyrrnkvgIVFQAFNLVPSL 100
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRDIC--------MVFQSYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 TAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVE 180
Cdd:PRK11432 94 SLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 181 EVLRLIRELAdgERVVVVA---THD-SRMLPMADRVVELTPDFAETNRPPETVHLQAGEvLFEQSTMGD 245
Cdd:PRK11432 174 SMREKIRELQ--QQFNITSlyvTHDqSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS-RFMASFMGD 239
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
21-215 |
5.62e-29 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 111.83 E-value: 5.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaelANYRRNKVGIVFQAFNLVPS 99
Cdd:TIGR03873 14 RLIvDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLS----RRARARRVALVEQDSDTAVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 LTAVENVM---VPLRSA-GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:TIGR03873 90 LTVRDVVAlgrIPHRSLwAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 176 FIQVEEVLRLIRELADGERVVVVATHDSRMLPM-ADRVVEL 215
Cdd:TIGR03873 170 VRAQLETLALVRELAATGVTVVAALHDLNLAASyCDHVVVL 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-216 |
6.11e-29 |
|
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: 111.02 E-value: 6.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlQGAELAnyrrnkvgIVFQAFNLVPSLTA 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRM--------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSA--GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVE 180
Cdd:TIGR01184 72 RENIALAVDRVlpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 15607215 181 EVL-RLIRELADGERVVVVATHD-SRMLPMADRVVELT 216
Cdd:TIGR01184 152 NLQeELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLT 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-215 |
7.29e-29 |
|
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: 109.23 E-value: 7.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysgGYALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgaELANY 82
Cdd:cd03246 1 LEVENVSFRY---PGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRNkVGIVFQAFNLVPSlTAVENVmvplrsagmsrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALDP 162
Cdd:cd03246 75 GDH-VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-213 |
8.88e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.50 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 14 YSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD--EVDITTLQGAElanyrRNKVGIVF 91
Cdd:COG1129 14 FGGVKALD---GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFRSPRDAQ-----AAGIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 92 QAFNLVPSLTAVENVMV---PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILAD 168
Cdd:COG1129 86 QELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15607215 169 EPTAHLDFIQVEEVLRLIRELADGERVVVVATHdsRM---LPMADRVV 213
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRLKAQGVAIIYISH--RLdevFEIADRVT 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-213 |
1.53e-28 |
|
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: 115.17 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKT-TLLSCLG----GILRPkSGAIKFDEVDITTLQGAE 78
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRllpdPAAHP-SGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LANYRRNKVGIVFQ----AFNlvPSLTAVENVMVPLR-SAGMSRRASRRRAEELLARVNLAE---RMNHRPGDLSGGQQQ 150
Cdd:COG4172 86 LRRIRGNRIAMIFQepmtSLN--PLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 151 RVAVARAIALDPPLILADEPTAHLDF-IQvEEVLRLIRELADGERV-VVVATHD----SRmlpMADRVV 213
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVtVQ-AQILDLLKDLQRELGMaLLLITHDlgvvRR---FADRVA 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-215 |
3.07e-28 |
|
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: 112.13 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIkfdEVDITTL----QGAELANYRRnKVGIVFQAFNLVPSLT 101
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI---VLNGRTLfdsrKGIFLPPEKR-RIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 AVENVMVPL-RSAGMSRRASRRRAEELLARVNLAERmnhRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVE 180
Cdd:TIGR02142 92 VRGNLRYGMkRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 181 EVLRLIRELADGERV-VVVATHD-SRMLPMADRVVEL 215
Cdd:TIGR02142 169 EILPYLERLHAEFGIpILYVSHSlQEVLRLADRVVVL 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-213 |
5.52e-28 |
|
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: 108.45 E-value: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 25 GLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyRRNkVGIVFQAFNLVpSLTAVE 104
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRN-IGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 105 NVMVPLRSAgmsrrasrrRAEELLARVNLA-------------ERMNHRPGD-LSGGQQQRVAVARAIALDPPLILADEP 170
Cdd:cd03245 97 NITLGAPLA---------DDERILRAAELAgvtdfvnkhpnglDLQIGERGRgLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15607215 171 TAHLDFIQVEEVLRLIRELAdGERVVVVATHDSRMLPMADRVV 213
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRII 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-191 |
9.17e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 108.19 E-value: 9.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYysGGyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLqgael 79
Cdd:COG1137 1 MMTLEAENLVKSY--GK---RTVvKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 80 ANYRRNKVGI--------VFQafnlvpSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQR 151
Cdd:COG1137 71 PMHKRARLGIgylpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15607215 152 VAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELAD 191
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE 184
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-212 |
9.22e-28 |
|
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: 108.01 E-value: 9.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaelaNYRRNKVGIVF--QAF 94
Cdd:cd03218 10 YGKRKVvNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP-----MHKRARLGIGYlpQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 95 NLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLaERMNHRPGD-LSGGQQQRVAVARAIALDPPLILADEPTAH 173
Cdd:cd03218 85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASsLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15607215 174 LDFIQVEEVLRLIRELADGERVVVVATHDSR-MLPMADRV 212
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITDHNVReTLSITDRA 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
23-213 |
1.15e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.92 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgAELANYRRNKVGIVFQ---------- 92
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS----KENLKEIRKKIGIIFQnpdnqfigat 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 93 -----AFNLvpsltavENVMVPlrsagmsRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILA 167
Cdd:PRK13632 101 veddiAFGL-------ENKKVP-------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15607215 168 DEPTAHLDFIQVEEVLRLIRELAD-GERVVVVATHDSRMLPMADRVV 213
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKtRKKTLISITHDMDEAILADKVI 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-215 |
1.68e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.16 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 17 GYALRP-INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGaikfdevdittlqgaELANYRRNKVGIVFQAFN 95
Cdd:NF040873 1 GYGGRPvLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG---------------TVRRAGGARVAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSL--TAVENVMV----PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:NF040873 66 VPDSLplTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15607215 170 PTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-212 |
1.97e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.24 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELAnyR 83
Cdd:PRK13639 2 LETRDLKYSYPDGTEAL---KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLE--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDP 162
Cdd:PRK13639 77 RKTVGIVFQnPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPM-ADRV 212
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKV 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-215 |
2.04e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGA-ELAN---YRRNKVGIVFQAFNL 96
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREgRLARdirKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 VPSLTAVENVMV------PLRSAGMSRRASRRRAEEL--LARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILAD 168
Cdd:PRK09984 98 VNRLSVLENVLIgalgstPFWRTCFSWFTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 169 EPTAHLDFIQVEEVLRLIREL--ADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-205 |
2.21e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.85 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYSGGY-----ALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQ 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 76 GAELANYRRNkVGIVFQ----AFNlvPSLTAVENVMVPLRS-AGMSRRASRRRAEELLARVNLA-ERMNHRPGDLSGGQQ 149
Cdd:PRK10419 81 RAQRKAFRRD-IQMVFQdsisAVN--PRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 150 QRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIREL-ADGERVVVVATHDSRM 205
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRL 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-212 |
2.78e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.92 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVvEYYSGGYAlrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDIttlqgAELANYR 83
Cdd:PRK11607 20 LEIRNLT-KSFDGQHA---VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:PRK11607 91 R-PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 164 LILADEPTAHLD-----FIQVEEVLRLireladgERV---VVVATHDS-RMLPMADRV 212
Cdd:PRK11607 170 LLLLDEPMGALDkklrdRMQLEVVDIL-------ERVgvtCVMVTHDQeEAMTMAGRI 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-213 |
2.91e-27 |
|
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: 109.42 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 27 NLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEvdiTTLQGAE----LANYRRNkVGIVFQAFNLVPSLTA 102
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG---EVLQDSArgifLPPHRRR-IGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGmsRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:COG4148 95 RGNLLYGRKRAP--RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190
....*....|....*....|....*....|...
gi 15607215 183 LRLIRELADGERV-VVVATHDSR-MLPMADRVV 213
Cdd:COG4148 173 LPYLERLRDELDIpILYVSHSLDeVARLADHVV 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-189 |
3.98e-27 |
|
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: 111.31 E-value: 3.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYY-------SGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLlsclG-GILR--PKSGAIKFDEVDITT 73
Cdd:COG4172 276 LEARDLKVWFPikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTL----GlALLRliPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 74 LQGAELANYRRnKVGIVFQ----AFNlvPSLTAVENVMVPLR--SAGMSRRASRRRAEELLARVNLAERMNHR-PGDLSG 146
Cdd:COG4172 352 LSRRALRPLRR-RMQVVFQdpfgSLS--PRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARHRyPHEFSG 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15607215 147 GQQQRVAVARAIALDPPLILADEPTAHLDF-IQVeEVLRLIREL 189
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDVsVQA-QILDLLRDL 471
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-201 |
1.40e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYSggyaLRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGI--LRPK---SGAIKFDEVDITTLQ 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 76 GAELanyrRNKVGIVFQAFNLVPSLTAVENVMVplrsaGMSRRASRRRAEELLARVNLA-----------ERMNHRPGDL 144
Cdd:PRK14247 77 VIEL----RRRVQMVFQIPNPIPNLSIFENVAL-----GLKLNRLVKSKKELQERVRWAlekaqlwdevkDRLDAPAGKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 145 SGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADgERVVVVATH 201
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-230 |
2.16e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.42 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAElanyrRNkVGIVFQAFNLVPSLTAVEN 105
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-----RG-VGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 106 VMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD-FIQVE---E 181
Cdd:PRK11000 96 MSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaALRVQmriE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 182 VLRLIRELadgERVVVVATHDS-RMLPMADRVVELTPDF-AETNRPPETVH 230
Cdd:PRK11000 176 ISRLHKRL---GRTMIYVTHDQvEAMTLADKIVVLDAGRvAQVGKPLELYH 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
3.31e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:COG4559 2 LEAENLSVRL--GGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 rnkvGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARV---NLAERMNHrpgDLSGGQQQRVAVARAIA- 159
Cdd:COG4559 78 ----AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVglaHLAGRSYQ---TLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607215 160 ------LDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDsrmLPM----ADRVV 213
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHD---LNLaaqyADRIL 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-212 |
3.47e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 3.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 27 NLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQAFNLVPSLTAVENV 106
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 107 MVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD-FIQVEEVLRL 185
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDpLIRTEMQDEL 207
|
170 180
....*....|....*....|....*...
gi 15607215 186 IRELADGERVVVVATHD-SRMLPMADRV 212
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDlDEAMRIGDRI 235
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-211 |
4.00e-26 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 103.89 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSggyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgaELANY 82
Cdd:TIGR04406 2 LVAENLIKSYKK-----RKVvNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIT-----HLPMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRNKVGIVF--QAFNLVPSLTAVENVMVPL-RSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIA 159
Cdd:TIGR04406 72 ERARLGIGYlpQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 160 LDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSR-MLPMADR 211
Cdd:TIGR04406 152 TNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVReTLDICDR 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-216 |
5.32e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 6 IQNLVVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgAELANYRRN 85
Cdd:PRK13647 7 VEDLHFRYKDGTKALK---GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN----AENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 86 KVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPL 164
Cdd:PRK13647 80 KVGLVFQdPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 165 ILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRM-LPMADRVVELT 216
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLK 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
23-215 |
5.88e-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: 102.74 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevdittlqGAELANYRRNKVGIVFQAFNLVPSLTA 102
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD--------GKPLDIAARNRIGYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 15607215 183 LRLIRELADGERVVVVATHdsRM---LPMADRVVEL 215
Cdd:cd03269 168 KDVIRELARAGKTVILSTH--QMelvEELCDRVLLL 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-217 |
6.73e-26 |
|
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: 101.86 E-value: 6.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 15 SGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPK--SGAIKFDEVDIttlqgaELANYRRnKVGIVFQ 92
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPL------DKRSFRK-IIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 93 AFNLVPSLTAVENVMVplrSAGMSRrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALDPPLILADEPTA 172
Cdd:cd03213 90 DDILHPTLTVRETLMF---AAKLRG--------------------------LSGGERKRVSIALELVSNPSLLFLDEPTS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15607215 173 HLDFIQVEEVLRLIRELADGERVVVVATHDSR--MLPMADRVVELTP 217
Cdd:cd03213 141 GLDSSSALQVMSLLRRLADTGRTIICSIHQPSseIFELFDKLLLLSQ 187
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-213 |
1.00e-25 |
|
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: 107.64 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYY-SGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELa 80
Cdd:TIGR03375 462 GEIEFRNVSFAYPgQETPALD---NVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyRRNkVGIVFQAfnlvPSL---TAVENVMVPLRSAGMSRRASRRRAEELLARVN-----LAERMNHRPGDLSGGQQQRV 152
Cdd:TIGR03375 538 --RRN-IGYVPQD----PRLfygTLRDNIALGAPYADDEEILRAAELAGVTEFVRrhpdgLDMQIGERGRSLSGGQRQAV 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607215 153 AVARAIALDPPLILADEPTAHLDFIQVEEVL-RLIRELADgeRVVVVATHDSRMLPMADRVV 213
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKdRLKRWLAG--KTLVLVTHRTSLLDLVDRII 670
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-213 |
1.04e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.22 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 9 LVVEYYSGGYALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIkfdevdittLQGAELANYRRNKV 87
Cdd:PRK11247 13 LLLNAVSKRYGERTVlNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 88 GIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRrraeelLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILA 167
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQA------LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 168 DEPTAHLDFIQVEEVLRLIREL--ADGERVVVVaTHD-SRMLPMADRVV 213
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLwqQHGFTVLLV-THDvSEAVAMADRVL 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-212 |
1.18e-25 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 102.06 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 6 IQNLVVEYysGGYalRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgaELANYRRN 85
Cdd:cd03265 3 VENLVKKY--GDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 86 kVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLI 165
Cdd:cd03265 75 -IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 166 LADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD---SRMLpmADRV 212
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMtILLTTHYmeeAEQL--CDRV 202
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
23-213 |
1.21e-25 |
|
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: 100.85 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAelanyRRNKVGIVFQAfnlvPSLTA 102
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQR----PYLFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VEnvmvpLRSagmsrrasrrraeellarvNLAERmnhrpgdLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:cd03247 89 TT-----LRN-------------------NLGRR-------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190
....*....|....*....|....*....|.
gi 15607215 183 LRLIRELADGERVVVVaTHDSRMLPMADRVV 213
Cdd:cd03247 138 LSLIFEVLKDKTLIWI-THHLTGIEHMDKIL 167
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-213 |
2.84e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYR 83
Cdd:PRK13548 3 LEARNLSVRL--GGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 rnkvGIVFQAFNLVPSLTAVENV-M--VPLRSAgmsRRASRRRAEELLARVN---LAERMNHRpgdLSGGQQQRVAVARA 157
Cdd:PRK13548 79 ----AVLPQHSSLSFPFTVEEVVaMgrAPHGLS---RAEDDALVAAALAQVDlahLAGRDYPQ---LSGGEQQRVQLARV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 158 IA------LDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD----SRmlpMADRVV 213
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLaVIVVLHDlnlaAR---YADRIV 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-219 |
3.36e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLG--GILRPK---SGAIKFDEVDI--TTLQG 76
Cdd:PRK14239 6 LQVSDLSV-YYNKKKAL---NSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 AELanyrRNKVGIVFQAFNLVPsLTAVENVMVPLRSAGMSRRASR-RRAEELLARVNLAERMNHRPGD----LSGGQQQR 151
Cdd:PRK14239 82 VDL----RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLdEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 152 VAVARAIALDPPLILADEPTAHLDFI---QVEEVLRLIREladgERVVVVATHDsrmLPMADRVVELTPDF 219
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPIsagKIEETLLGLKD----DYTMLLVTRS---MQQASRISDRTGFF 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-201 |
3.38e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.49 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 27 NLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD--EVDITTLQGAelanyRRNKVGIVFQAFNLVPSLTAVE 104
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVRIRSPRDA-----IALGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 105 NVMVPLRSAGMSRRASRRRAEELLArvnLAERMN-----HRP-GDLSGGQQQRVAVARAIALDPP-LILaDEPTAHLDFI 177
Cdd:COG3845 100 NIVLGLEPTKGGRLDRKAARARIRE---LSERYGldvdpDAKvEDLSVGEQQRVEILKALYRGARiLIL-DEPTAVLTPQ 175
|
170 180
....*....|....*....|....
gi 15607215 178 QVEEVLRLIRELADGERVVVVATH 201
Cdd:COG3845 176 EADELFEILRRLAAEGKSIIFITH 199
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
3.43e-25 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.04 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD--EVDITTLQGAelan 81
Cdd:cd03216 1 LELRGITK-RFGGVKALDGVS---LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkEVSFASPRDA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 yRRNKVGIVFQafnlvpsltavenvmvplrsagmsrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALD 161
Cdd:cd03216 73 -RRAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 162 PPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHdsRM---LPMADRVV 213
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH--RLdevFEIADRVT 153
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-217 |
3.93e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.33 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 25 GLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANY--RRNkvgivfqAFNlvPSLTA 102
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlgHRN-------AMK--PALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGmsrrASRRRAEELLARVNLAeRMNHRP-GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:PRK13539 91 AENLEFWAAFLG----GEELDIAAALEAVGLA-PLAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 15607215 182 VLRLIRELADGERVVVVATHDSRMLPMAdRVVELTP 217
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATHIPLGLPGA-RELDLGP 200
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-215 |
5.77e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.28 E-value: 5.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEV------DITTLQGAELanyrRNKVGIVFQAFNL 96
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKL----RKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 VPSLTAVENVMVPLRSAGMSRRASRRR-AEELLARVNL----AERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPT 171
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15607215 172 AHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-215 |
9.24e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.42 E-value: 9.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRrNKVGIVFQ-AFNLVPSLT 101
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR-EKVGIVFQnPDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 AVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181
|
170 180 190
....*....|....*....|....*....|....*
gi 15607215 182 VLRLIRELA-DGERVVVVATHDSRMLPMADRVVEL 215
Cdd:PRK13640 182 ILKLIRKLKkKNNLTVISITHDIDEANMADQVLVL 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-213 |
1.45e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 104.09 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELan 81
Cdd:COG1132 338 GEIEFENVSFSYPGDRPVLK---DISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 yrRNKVGIVFQAFNLVpSLTAVENV--------MVPLRSAgmsrrasrrraeelLARVNLAERMNHRPG----------- 142
Cdd:COG1132 413 --RRQIGVVPQDTFLF-SGTIRENIrygrpdatDEEVEEA--------------AKAAQAHEFIEALPDgydtvvgergv 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 143 DLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGeRVVVVATHdsRM--LPMADRVV 213
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTIVIAH--RLstIRNADRIL 545
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-202 |
1.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.93 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 6 IQNLVVEYYSG-GYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAEL----- 79
Cdd:PRK13651 5 VKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEkekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 80 ---------------ANYRRNKVGIVFQ--AFNLVPSlTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHR-P 141
Cdd:PRK13651 85 eklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRsP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 142 GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD 202
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-213 |
1.67e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.06 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGyaLRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELAnyr 83
Cdd:PRK11300 6 LSVSGLMMRF--GG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 rnKVGIV--FQAFNLVPSLTAVENVMVP----LRS---AGM--------SRRASRRRAEELLARVNLAERMNHRPGDLSG 146
Cdd:PRK11300 79 --RMGVVrtFQHVRLFREMTVIENLLVAqhqqLKTglfSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 147 GQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD-SRMLPMADRVV 213
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVtVLLIEHDmKLVMGISDRIY 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-202 |
2.79e-24 |
|
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: 103.21 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 9 LVVEYYSGGY--ALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrRNK 86
Cdd:TIGR02868 335 LELRDLSAGYpgAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV----RRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 87 VGIVFQAFNLVPSlTAVENVMVPLRSAgmsrraSRRRAEELLARVNLAERMNHRPGDL-----------SGGQQQRVAVA 155
Cdd:TIGR02868 411 VSVCAQDAHLFDT-TVRENLRLARPDA------TDEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRElADGERVVVVATHD 202
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-213 |
3.41e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.54 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD--EVDITTLQGAELan 81
Cdd:PRK13636 6 LKVEELNYNYSDGTHAL---KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkPIDYSRKGLMKL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 yrRNKVGIVFQA-FNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLaERMNHRPGD-LSGGQQQRVAVARAIA 159
Cdd:PRK13636 81 --RESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 160 LDPPLILADEPTAHLDFIQVEEVLRLIRELADG-ERVVVVATHDSRMLPM-ADRVV 213
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLyCDNVF 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-201 |
3.52e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.15 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 8 NLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqGAELANYR---- 83
Cdd:PRK14267 9 NLRV-YYGSNHVIK---GVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLF---GRNIYSPDvdpi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 --RNKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLA------ERMNHRPGDLSGGQQQRVAVA 155
Cdd:PRK14267 82 evRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAlwdevkDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADgERVVVVATH 201
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTH 206
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-213 |
7.19e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.92 E-value: 7.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNlVVEYYSGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAEla 80
Cdd:PRK11650 1 MAGLKLQA-VRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNkVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRrraeellARVNLAERM-------NHRPGDLSGGQQQRVA 153
Cdd:PRK11650 76 ---RD-IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIE-------ERVAEAARIlelepllDRKPRELSGGQRQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 154 VARAIALDPPLILADEPTAHLDF---IQVE-EVLRLIRELADGERVVvvaTHDS-RMLPMADRVV 213
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAklrVQMRlEIQRLHRRLKTTSLYV---THDQvEAMTLADRVV 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-201 |
7.97e-24 |
|
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: 97.85 E-value: 7.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGA------IKFDEVDITTLqg 76
Cdd:COG1119 4 LELRNVTVRR--GG---KTIlDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVWEL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 aelanyrRNKVGIVFQAF-NLVPSLTAVENVMVplrSAGM--------SRRASRRRAEELLARVNLAERMNHRPGDLSGG 147
Cdd:COG1119 77 -------RKRIGLVSPALqLRFPRDETVLDVVL---SGFFdsiglyrePTDEQRERARELLELLGLAHLADRPFGTLSQG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 148 QQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELA-DGERVVVVATH 201
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAaEGAPTLVLVTH 201
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-216 |
1.19e-23 |
|
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: 96.92 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyr 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVpSLTAVENVMVPLRSAGMsrrasrrraeellARVNLAERMNH------------------RPGDLS 145
Cdd:cd03251 75 RRQIGLVSQDVFLF-NDTVAENIAYGRPGATR-------------EEVEEAARAANahefimelpegydtvigeRGVKLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 146 GGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVAtHDSRMLPMADRVVELT 216
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA-HRLSTIENADRIVVLE 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-191 |
1.83e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 27 NLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAelanyrRNKVGIVFQAFNLVPSLTAVENV 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 107 MVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLI 186
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
....*
gi 15607215 187 RELAD 191
Cdd:PRK10771 173 SQVCQ 177
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-212 |
2.31e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 96.45 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 25 GLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILrPKSGAIKFDEVDITTLQGAELANYR------RNKVGI--VFQAFNL 96
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRaylsqqQSPPFAmpVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 -VPSLTAVENVmvplrsagmsrrasRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAI-----ALDPP--LILAD 168
Cdd:COG4138 93 hQPAGASSEAV--------------EQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15607215 169 EPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRV 212
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDlNHTLRHADRV 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-212 |
2.40e-23 |
|
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: 100.21 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGGyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELA 80
Cdd:COG4618 329 GRLSVENLTVVPPGSK---RPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 NYrrnkVGIVFQAFNLVPSlTAVENVmvplrsAGMSRRASrrraeellARVNLAERM--------------NHRPGD--- 143
Cdd:COG4618 406 RH----IGYLPQDVELFDG-TIAENI------ARFGDADP--------EKVVAAAKLagvhemilrlpdgyDTRIGEgga 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 144 -LSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRV 212
Cdd:COG4618 467 rLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKL 536
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-191 |
3.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 6 IQNLVVEYYSGG-YALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlQGAELANYRR 84
Cdd:PRK13637 5 IENLTHIYMEGTpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 85 nKVGIVFQ--AFNLVPSlTAVENVMVPLRSAGMSRRASRRRAEELLARVNLA-ERMNHR-PGDLSGGQQQRVAVARAIAL 160
Cdd:PRK13637 84 -KVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKsPFELSGGQKRRVAIAGVVAM 161
|
170 180 190
....*....|....*....|....*....|.
gi 15607215 161 DPPLILADEPTAHLDFIQVEEVLRLIRELAD 191
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHK 192
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
7-213 |
6.95e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.92 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 7 QNLVVEYYSGGYALRP--INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDitTLQGAELANYRr 84
Cdd:PRK13633 8 KNVSYKYESNEESTEKlaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLWDIR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 85 NKVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:PRK13633 85 NKAGMVFQnPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 164 LILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRMLPMADRVV 213
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGItIILITHYMEEAVEADRII 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-203 |
6.99e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 94.98 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELan 81
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLK---DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 yrRNKVGIVFQAFNLVPSlTAVENVMVPLRSAGMSRRASRRRAEELLARVN-----LAERMNHRPGDLSGGQQQRVAVAR 156
Cdd:cd03254 76 --RSMIGVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMklpngYDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15607215 157 AIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDS 203
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLS 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-212 |
8.15e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 95.00 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILrPKSGAIKFDEVDITTLQGAELANYR-----RNKVGI---VFQAFNL- 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFampVFQYLTLh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 VPSLTAVENVMVPLRsagmsrrasrrraeELLARVNLAERMnHRP-GDLSGGQQQRVAVA-------RAIALDPPLILAD 168
Cdd:PRK03695 94 QPDKTRTEAVASALN--------------EVAEALGLDDKL-GRSvNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15607215 169 EPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRV 212
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRV 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-202 |
1.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEY-YSGGYALRPI--NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELA 80
Cdd:PRK13641 1 MSIKFENVDYiYSPGTPMEKKglDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 NYRRNKVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAER-MNHRPGDLSGGQQQRVAVARAI 158
Cdd:PRK13641 81 KKLRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD 202
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN 204
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-213 |
1.93e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 92.50 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLvveyySGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAElanyr 83
Cdd:cd03215 5 LEVRGL-----SVKGAVRDVS---FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVF-----QAFNLVPSLTAVENVMVPLRsagmsrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAI 158
Cdd:cd03215 72 AIRAGIAYvpedrKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELAD-GERVVVVATHDSRMLPMADRVV 213
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELADaGKAVLLISSELDELLGLCDRIL 175
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-201 |
2.43e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGdLSIQNLVVEYYSGG-YALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAEL 79
Cdd:PRK13649 1 MG-INLQNVSYTYQAGTpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 80 ANYRRNKVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHR-PGDLSGGQQQRVAVARA 157
Cdd:PRK13649 80 IKQIRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15607215 158 IALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATH 201
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-213 |
2.58e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.39 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGyALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKfdeVDITTLQGAELANYR 83
Cdd:PRK13642 5 LEVENLVFKYEKES-DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVK---IDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDP 162
Cdd:PRK13642 81 R-KIGMVFQnPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVA-THDSRMLPMADRVV 213
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEAASSDRIL 211
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-213 |
2.71e-22 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 92.99 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 28 LDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevdittlqGAELANYRRNkVGIVFQ----AFNLVPS---- 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVA--------GASPGKGWRH-IGYVPQrhefAWDFPISvaht 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 -LTAVENVMVPLRSAGMSRRASRRRAeelLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQ 178
Cdd:TIGR03771 72 vMSGRTGHIGWLRRPCVADFAAVRDA---LRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 15607215 179 VEEVLRLIRELADGERVVVVATHD-SRMLPMADRVV 213
Cdd:TIGR03771 149 QELLTELFIELAGAGTAILMTTHDlAQAMATCDRVV 184
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-229 |
3.03e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSggyaLRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANyr 83
Cdd:PRK09536 4 IDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 rnKVGIVFQ----AFNLVPSlTAVENVMVPLRSA-GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAI 158
Cdd:PRK09536 78 --RVASVPQdtslSFEFDVR-QVVEMGRTPHRSRfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDsrmLPMA----DRVVELTPDFAETNRPPETV 229
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD---LDLAarycDELVLLADGRVRAAGPPADV 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-201 |
3.21e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.87 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDIttlqgAELANYRRNKVGIVFQAFNLVPSLTA 102
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PSRARHARQRVGVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDfIQVEEV 182
Cdd:PRK13537 98 RENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD-PQARHL 176
|
170 180
....*....|....*....|.
gi 15607215 183 L--RLIRELADGeRVVVVATH 201
Cdd:PRK13537 177 MweRLRSLLARG-KTILLTTH 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-201 |
3.54e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.42 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQ-AFNL 96
Cdd:PRK13643 17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 VPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLA-ERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180
....*....|....*....|....*.
gi 15607215 176 FIQVEEVLRLIRELADGERVVVVATH 201
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-221 |
4.06e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.85 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAElanYRRnKVGIVFQAfnlvPSL-- 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQ-QVSYCAQT----PTLfg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 -TAVENVMVPLRSAGMSRRASRRRAEelLARVNLAERM-NHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQ 178
Cdd:PRK10247 95 dTVYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15607215 179 VEEVLRLIRELADGERVVVV-ATHDSRMLPMADRVVELTPDFAE 221
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLwVTHDKDEINHADKVITLQPHAGE 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-238 |
1.20e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.15 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVeYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGI--LRPK---SGAIKFDEVDITTlQGAE 78
Cdd:PRK14243 11 LRTENLNV-YYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYA-PDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LANYRRnKVGIVFQAFNLVPSlTAVENVMVPLRSAGMSRRASRRRAEELLARV---NLAERMNHRPGDLSGGQQQRVAVA 155
Cdd:PRK14243 86 PVEVRR-RIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAAlwdEVKDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVaTHDsrmLPMADRVVELTPDF-----AETNRPPETVH 230
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV-THN---MQQAARVSDMTAFFnveltEGGGRYGYLVE 239
|
....*...
gi 15607215 231 LQAGEVLF 238
Cdd:PRK14243 240 FDRTEKIF 247
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-217 |
1.20e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 90.63 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 25 GLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAelanYRRNKVGIVFQAfNLVPSLTAVE 104
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQDLLYLGHQP-GIKTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 105 NvmvpLR-SAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVL 183
Cdd:PRK13538 94 N----LRfYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170 180 190
....*....|....*....|....*....|....*
gi 15607215 184 RLIRELADGERVVVVATH-DSRMLPMADRVVELTP 217
Cdd:PRK13538 170 ALLAQHAEQGGMVILTTHqDLPVASDKVRKLRLGQ 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-200 |
2.70e-21 |
|
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: 94.10 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYySGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGI--LRPKSGAI----------------- 64
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNIS---FTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 65 -------------KFDEVDITTLQGAELANYRRnKVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLAR 130
Cdd:TIGR03269 77 kvgepcpvcggtlEPEEVDFWNLSDKLRRRIRK-RIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 131 VNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVAT 200
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLT 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-216 |
4.62e-21 |
|
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: 89.64 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGilRPKSGAIKFDEVditTLQGAELANYR-RNKVGIVFQAFNLVPSLT 101
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGTTSGQI---LFNGQPRKPDQfQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 AVEN----VMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFI 177
Cdd:cd03234 98 VRETltytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 178 QVEEVLRLIRELADGERVVVVATHDSR--MLPMADRVVELT 216
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQPRsdLFRLFDRILLLS 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-202 |
4.70e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFdevdittlQGAELaNYR-------RNKVGIVFQAFN 95
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLW--------QGKPL-DYSkrgllalRQQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVE-NVMVPLRSAGMSRRASRRRAEELLARVNlAERMNHRPGD-LSGGQQQRVAVARAIALDPPLILADEPTAH 173
Cdd:PRK13638 88 QQIFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180
....*....|....*....|....*....
gi 15607215 174 LDFIQVEEVLRLIRELADGERVVVVATHD 202
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-215 |
4.93e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 89.98 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaelANYRRNKVGIVFQ---AFNl 96
Cdd:cd03253 14 RPVlKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT----LDSLRRAIGVVPQdtvLFN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 vpsltavENVMVPLRSAGMSRRASRRRAEELLARV-----NLAERMNHRPGD----LSGGQQQRVAVARAIALDPPLILA 167
Cdd:cd03253 89 -------DTIGYNIRYGRPDATDEEVIEAAKAAQIhdkimRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15607215 168 DEPTAHLDFIQVEEVLRLIRELADGERVVVVAtHDSRMLPMADRVVEL 215
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVNADKIIVL 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-205 |
5.32e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.94 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGA-------ELANYRRNKVG--IVFQA 93
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeERGLYPKMKVGeqLVYLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 94 fnlvpsltavenvmvplRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAH 173
Cdd:COG4152 97 -----------------RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190
....*....|....*....|....*....|..
gi 15607215 174 LDFIQVEEVLRLIRELADGERVVVVATHdsRM 205
Cdd:COG4152 160 LDPVNVELLKDVIRELAAKGTTVIFSSH--QM 189
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-215 |
6.76e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.20 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrRNKVGIVFQ---------- 92
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQnpdnqfvgsi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 93 -----AFNLvpsltavENVMVPLRSagmsrraSRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILA 167
Cdd:PRK13648 101 vkydvAFGL-------ENHAVPYDE-------MHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 168 DEPTAHLDFIQVEEVLRLIRELADGERVVVVA-THDSRMLPMADRVVEL 215
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAMEADHVIVM 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-191 |
2.17e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.63 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyR 83
Cdd:COG3845 258 LEVENLSVRDDRGVPALK---DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER---R 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIV---FQAFNLVPSLTAVENVMV------PLRSAGMSRRASRRRaeelLARvNLAERMNHRPGD-------LSGG 147
Cdd:COG3845 332 RLGVAYIpedRLGRGLVPDMSVAENLILgryrrpPFSRGGFLDRKAIRA----FAE-ELIEEFDVRTPGpdtparsLSGG 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15607215 148 QQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELAD 191
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD 450
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
227-314 |
2.62e-20 |
|
effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels
Pssm-ID: 237999 [Multi-domain] Cd Length: 115 Bit Score: 84.68 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 227 ETVHLQAGEVLFEQSTMGDLIYVVSEGEFEIVHELADGGEELVKVAGPGDYFGEIGVLFHLPRSATVRARSDATAVGYTV 306
Cdd:cd00038 18 EERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPRSATVRALTDSELLVLPR 97
|
....*...
gi 15607215 307 QAFRERLG 314
Cdd:cd00038 98 SDFRRLLQ 105
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-175 |
3.14e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIkfdevditTLQGAEL---ANYRRNKVGIVFQAFNLVPS 99
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI--------TVLGVPVparARLARARIGVVPQFDNLDLE 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 100 LTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:PRK13536 129 FTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-213 |
4.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.51 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAI---KFDEVDITTLQGAela 80
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENIN---LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNKVGIVFQAfnlvPSL-----TAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVA 155
Cdd:PRK13644 76 ---RKLVGIVFQN----PETqfvgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 156 RAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVV 213
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-204 |
4.15e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.64 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYsggyALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELA 80
Cdd:PRK10895 1 MATLTAKNLAKAYK----GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNKVGIVFQAFNLVPSLTAVENVMVPLR-SAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIA 159
Cdd:PRK10895 77 ---RRGIGYLPQEASIFRRLSVYDNLMAVLQiRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15607215 160 LDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSR 204
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR 198
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-211 |
4.70e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.24 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 20 LRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELAnyrRNKVGIVFQAFNLVPS 99
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM---REAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 LTAVEN-VMVPLRSAGMSRRASRRRAEELLARvnLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQ 178
Cdd:PRK11614 95 MTVEENlAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190
....*....|....*....|....*....|....
gi 15607215 179 VEEVLRLIREL-ADGERVVVVATHDSRMLPMADR 211
Cdd:PRK11614 173 IQQIFDTIEQLrEQGMTIFLVEQNANQALKLADR 206
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-214 |
5.48e-20 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 87.67 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVvEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDE-----VDITTLQGAE 78
Cdd:PRK11701 7 LSVRGLT-KLYGPRKGCRDVS---FDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LANYRRNKVGIVFQ--AFNLVPSLTAVENVMVPLRSAGMSR-RASRRRAEELLARVNL-AERMNHRPGDLSGGQQQRVAV 154
Cdd:PRK11701 83 RRRLLRTEWGFVHQhpRDGLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 155 ARAIALDPPLILADEPTAHLDFIQVEEVLRLIREL-ADGERVVVVATHD--------SRMLPMAD-RVVE 214
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDlavarllaHRLLVMKQgRVVE 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-215 |
8.13e-20 |
|
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: 85.87 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEyySGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGaelaNYR 83
Cdd:TIGR01189 1 LAARNLACS--RGERML--FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD----EPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAfNLVPSLTAVENvmvpLRSAGMSRRASRRRAEELLARVNLAERmNHRP-GDLSGGQQQRVAVARAIALDP 162
Cdd:TIGR01189 73 ENILYLGHLP-GLKPELSALEN----LHFWAAIHGGAQRTIEDALAAVGLTGF-EDLPaAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMAdRVVEL 215
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA-RELRL 198
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-202 |
9.63e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 9.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANyrrnKVGIVFQAFNLVPSLTA 102
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK----RLAILRQENHINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMV---PlRSAGMSRRASRRRAEELLARVNLAErMNHRPGD-LSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQ 178
Cdd:COG4604 93 RELVAFgrfP-YSKGRLTAEDREIIDEAIAYLDLED-LADRYLDeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKH 170
|
170 180
....*....|....*....|....*.
gi 15607215 179 VEEVLRLIRELAD--GERVVVVaTHD 202
Cdd:COG4604 171 SVQMMKLLRRLADelGKTVVIV-LHD 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-211 |
1.39e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVditTLQGAELANYR-----RNKVGIVFQAFNLV 97
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDV---LLGGRSIFNYRdvlefRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 98 PsLTAVENVMVPLRSAGMSRRAS-RRRAEELLARVNL----AERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTA 172
Cdd:PRK14271 114 P-MSIMDNVLAGVRAHKLVPRKEfRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 15607215 173 HLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADR 211
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDR 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-201 |
1.71e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.00 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQafnlV 97
Cdd:PRK13634 18 FERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 98 PSLTAVENVMV------PLrSAGMSRRASRRRAEELLARVNLAERMNHR-PGDLSGGQQQRVAVARAIALDPPLILADEP 170
Cdd:PRK13634 94 PEHQLFEETVEkdicfgPM-NFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190
....*....|....*....|....*....|..
gi 15607215 171 TAHLDFIQVEEVLRLIREL-ADGERVVVVATH 201
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTH 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-199 |
1.71e-19 |
|
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: 85.67 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRP----INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLggiLR---PKSGAIKFDEVDITTLQgaelANYRRNKVGIV 90
Cdd:cd03249 10 YPSRPdvpiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDLN----LRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 91 FQAfnlvPSL---TAVENVMVPLRSAGMSRRASRRRAEELLARV-NLAERMNHRPGD----LSGGQQQRVAVARAIALDP 162
Cdd:cd03249 83 SQE----PVLfdgTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDTLVGErgsqLSGGQKQRIAIARALLRNP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVA 199
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIA 195
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-175 |
2.35e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.91 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGG----YALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgaeL 79
Cdd:COG1101 2 LELKNLSKTFNPGTvnekRALD---GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 80 ANYRRNK-VGIVFQ------AfnlvPSLTAVENVMV--------PLRSAgmSRRASRRRAEELLARVN--LAERMNHRPG 142
Cdd:COG1101 74 PEYKRAKyIGRVFQdpmmgtA----PSMTIEENLALayrrgkrrGLRRG--LTKKRRELFRELLATLGlgLENRLDTKVG 147
|
170 180 190
....*....|....*....|....*....|...
gi 15607215 143 DLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-213 |
3.13e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLvveyySGGYALRP---INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAE 78
Cdd:PRK11160 337 VSLTLNNV-----SFTYPDQPqpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LanyrRNKVGIVFQAFNLVpSLTAVENVMVPLRSAGmsrrasRRRAEELLARVNLA------ERMNHRPGD----LSGGQ 148
Cdd:PRK11160 412 L----RQAISVVSQRVHLF-SATLRDNLLLAAPNAS------DEALIEVLQQVGLEklleddKGLNAWLGEggrqLSGGE 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 149 QQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVaTHDSRMLPMADRVV 213
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI-THRLTGLEQFDRIC 544
|
|
| cNMP_binding |
pfam00027 |
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
229-311 |
6.98e-19 |
|
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 459637 [Multi-domain] Cd Length: 89 Bit Score: 79.96 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 229 VHLQAGEVLFEQSTMGDLIYVVSEGEFEIVHELADGGEELVKVAGPGDYFGEIGVLFHLPRSATVRARSDATAVGYTVQA 308
Cdd:pfam00027 2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81
|
...
gi 15607215 309 FRE 311
Cdd:pfam00027 82 FLE 84
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-237 |
7.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.78 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrRNKVGIVFQ-AFNLVPSLT 101
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI----RHKIGMVFQnPDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 AVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 182 VLRLIRELADGERVVVVA-THDSRMLPMADRVVELTPDFAETNRPPETVHLQAGEVL 237
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVISiTHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLL 235
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
9.49e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.47 E-value: 9.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYSGGYALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELa 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKEAL---NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNKVGIVFQ-AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIA 159
Cdd:PRK13652 77 ---RKFVGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 160 LDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVV-ATHDSRMLP-MADRV 212
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfSTHQLDLVPeMADYI 208
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-214 |
2.20e-18 |
|
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: 82.96 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVvEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD-----EVDITTLQGAE 78
Cdd:TIGR02323 4 LQVSGLS-KSYGGGKGCRDVS---FDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrsgaELELYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LANYRRNKVGIVFQ--AFNLVPSLTAVENVMVPLRSAGMSR-RASRRRAEELLARVNL-AERMNHRPGDLSGGQQQRVAV 154
Cdd:TIGR02323 80 RRRLMRTEWGFVHQnpRDGLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 155 ARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELA-DGERVVVVATHD--------SRMLPMAD-RVVE 214
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVrDLGLAVIIVTHDlgvarllaQRLLVMQQgRVVE 229
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-202 |
2.80e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 84.01 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPK---SGAIKFDEVDITTLQGAELA 80
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 NYRRNKVGIVFQ--AFNLVPSLTAVENVM-VPLRSAGMSRRASRRRAEELLARVNLAE---RMNHRPGDLSGGQQQRVAV 154
Cdd:PRK09473 93 KLRAEQISMIFQdpMTSLNPYMRVGEQLMeVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 155 ARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELA-DGERVVVVATHD 202
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHD 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-202 |
2.84e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.01 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGaikfdevDITTLQGAELANYR 83
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-------KISILGQPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAFNLVPSLTA-VENVMVPLRSAGM-----SRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARA 157
Cdd:PRK15056 77 KNLVAYVPQSEEVDWSFPVlVEDVVMMGRYGHMgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15607215 158 IALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD 202
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-212 |
4.74e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEY---------YSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTL 74
Cdd:PRK15079 9 LEVADLKVHFdikdgkqwfWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 75 QGAELANyRRNKVGIVFQ--AFNLVPSLTAVENVMVPLRS--AGMSRRASRRRAEELLARVNLAERM-NHRPGDLSGGQQ 149
Cdd:PRK15079 89 KDDEWRA-VRSDIQMIFQdpLASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 150 QRVAVARAIALDPPLILADEPTAHLDF-IQVeEVLRLIRELAD--GERVVVVAtHD-SRMLPMADRV 212
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVsIQA-QVVNLLQQLQRemGLSLIFIA-HDlAVVKHISDRV 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-219 |
5.97e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKS-----GAIKFDEVDITTLQgAELANYRRnKVGIVFQAFNLV 97
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERR-VNLNRLRR-QVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 98 PsLTAVENVMVPLRSAGMS-RRASRRRAEELLARVNLAERMNHR----PGDLSGGQQQRVAVARAIALDPPLILADEPTA 172
Cdd:PRK14258 101 P-MSVYDNVAYGVKIVGWRpKLEIDDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15607215 173 HLDFIQVEEVLRLIRELA-DGERVVVVATHDsrmLPMADRVVELTPDF 219
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRlRSELTMVIVSHN---LHQVSRLSDFTAFF 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-189 |
9.15e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKT-TLLSCLGGILRPK----SGAIKFDEVDITTLQGAE 78
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LANYRRNKVGIVFQA--FNLVPsLTAVENVMVPLRS--AGMSRRASRRRAEELLARV---NLAERMNHRPGDLSGGQQQR 151
Cdd:PRK15134 86 LRGVRGNKIAMIFQEpmVSLNP-LHTLEKQLYEVLSlhRGMRREAARGEILNCLDRVgirQAAKRLTDYPHQLSGGERQR 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 15607215 152 VAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIREL 189
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL 202
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
227-327 |
9.73e-18 |
|
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.
Pssm-ID: 197516 [Multi-domain] Cd Length: 120 Bit Score: 77.83 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 227 ETVHLQAGEVLFEQSTMGDLIYVVSEGEFEIVHELADGGEELVKVAGPGDYFGEIGVLFH--LPRSATVRARSDATAVGY 304
Cdd:smart00100 18 EPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNsrRAASAAAVALELATLLRI 97
|
90 100
....*....|....*....|...
gi 15607215 305 TVQAFRERLGVGGLRDLIEHRAL 327
Cdd:smart00100 98 DFRDFLQLLPELPQLLLELLLEL 120
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-189 |
1.36e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 81.93 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 20 LRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANyRRNKVGIVFQafNLVPS 99
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKL-LRQKIQIVFQ--NPYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 LT---AVENVMV-PLR-SAGMSRRASRRRAEELLARVNL-AERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAH 173
Cdd:PRK11308 105 LNprkKVGQILEePLLiNTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170
....*....|....*..
gi 15607215 174 LDF-IQVeEVLRLIREL 189
Cdd:PRK11308 185 LDVsVQA-QVLNLMMDL 200
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-201 |
1.43e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKF--DEVDITTLQGAELANyrrnkVGIVFQAFNLVPSL 100
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGPKSSQEAG-----IGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 TAVENVMV----PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDF 176
Cdd:PRK10762 95 TIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180
....*....|....*....|....*
gi 15607215 177 IQVEEVLRLIRELADGERVVVVATH 201
Cdd:PRK10762 175 TETESLFRVIRELKSQGRGIVYISH 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-202 |
1.44e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 81.36 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEY-YSGG--YALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELA 80
Cdd:PRK13646 1 MTIRFDNVSYtYQKGtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 NYRRNKVGIVFQafnlVPSLTAVEN-----VMVPLRSAGMSRRASRRRAEELLARVNLAER-MNHRPGDLSGGQQQRVAV 154
Cdd:PRK13646 81 RPVRKRIGMVFQ----FPESQLFEDtvereIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 155 ARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELA-DGERVVVVATHD 202
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHD 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-215 |
1.66e-17 |
|
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: 80.22 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 16 GGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgAELANYRRnKVGIVFQAfN 95
Cdd:cd03252 14 GPVILDNIS---LRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL---ADPAWLRR-QVGVVLQE-N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVENVmvPLRSAGMSRRASRRRAEELLAR---VNLAERMNHRPGD----LSGGQQQRVAVARAIALDPPLILAD 168
Cdd:cd03252 86 VLFNRSIRDNI--ALADPGMSMERVIEAAKLAGAHdfiSELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15607215 169 EPTAHLDFIQVEEVLRLIRELADGERVVVVAtHDSRMLPMADRVVEL 215
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIA-HRLSTVKNADRIIVM 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-224 |
1.71e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD--EVDITTLQGAELANyrrnkVGIVFQAFNLVP 98
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqEMRFASTTAALAAG-----VAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 99 SLTAVENVMV---PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:PRK11288 93 EMTVAENLYLgqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 176 FIQVEEVLRLIRELADGERVVVVATHdsRM---LPMADRV--------VELTPDFAETNR 224
Cdd:PRK11288 173 AREIEQLFRVIRELRAEGRVILYVSH--RMeeiFALCDAItvfkdgryVATFDDMAQVDR 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-218 |
2.12e-17 |
|
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: 77.49 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYysGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevdittlqgaelanyR 83
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------S 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQafnlvpsltavenvmvplrsagmsrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALDPP 163
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 164 LILADEPTAHLDfiqVEEVLRLIRELADGERVVVVATHDSRMLPM-ADRVVELTPD 218
Cdd:cd03221 91 LLLLDEPTNHLD---LESIEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
10-212 |
2.25e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 10 VVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELAnyrRNKVGI 89
Cdd:PRK09700 11 IGKSFGPVHALKSVN---LTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA---QLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 90 VFQAFNLVPSLTAVENVMV---PLRSA-GMSR---RASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDP 162
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIgrhLTKKVcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIREL-ADGERVVVVATHDSRMLPMADRV 212
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICDRY 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-215 |
3.13e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.05 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAI---------KFDEVDITTLQGA-ELANYR--RNKVGIV 90
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELITNPYSkKIKNFKelRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 91 FQ--AFNLVPSlTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHR-PGDLSGGQQQRVAVARAIALDPPLILA 167
Cdd:PRK13631 122 FQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERsPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 168 DEPTAHLDFIQVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVVEL 215
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVM 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-189 |
5.01e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 19 ALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILrPK---SGAIKFDEvdiTTLQGAELANYRRNKVGIVFQAFN 95
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG---EELQASNIRDTERAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVENVMV---PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTA 172
Cdd:PRK13549 93 LVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170
....*....|....*..
gi 15607215 173 HLDFIQVEEVLRLIREL 189
Cdd:PRK13549 173 SLTESETAVLLDIIRDL 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-215 |
6.83e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 6.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGaikfdevDITTLQGAelanyrrnKVGIVFQAFNL 96
Cdd:COG0488 8 FGGRPLlDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVSIPKGL--------RIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 VPSLTAVENVM---VPLR---------SAGMSRRASRRRAEE--------------------LLARVNLAERMNHRP-GD 143
Cdd:COG0488 73 DDDLTVLDTVLdgdAELRaleaeleelEAKLAEPDEDLERLAelqeefealggweaearaeeILSGLGFPEEDLDRPvSE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 144 LSGGQQQRVAVARAIALDPPLILADEPTAHLDfiqVEEVLRLIRELADGERVVVVATHDSRML-PMADRVVEL 215
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLEEFLKNYPGTVLVVSHDRYFLdRVATRILEL 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-189 |
8.31e-17 |
|
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: 81.02 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 20 LRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGIlRPK---SGAIKFDEvdiTTLQGAELANYRRNKVGIVFQAFNL 96
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSG---SPLKASNIRDTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 VPSLTAVENVM----VPLRSAGMSRRASRRRAEELLARVNLAERMNHRP-GDLSGGQQQRVAVARAIALDPPLILADEPT 171
Cdd:TIGR02633 90 VPELSVAENIFlgneITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170
....*....|....*...
gi 15607215 172 AHLDFIQVEEVLRLIREL 189
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDL 187
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
18-176 |
1.32e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 78.34 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevdittlqGAELAN----YRRNKVGIVFQ- 92
Cdd:COG4167 27 EAVKPVS---FTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILIN--------GHKLEYgdykYRCKHIRMIFQd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 93 ---AFNlvPSLTAVENVMVPLRSA-GMSRRASRRRAEELLARVNL-AERMNHRPGDLSGGQQQRVAVARAIALDPPLILA 167
Cdd:COG4167 96 pntSLN--PRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIA 173
|
....*....
gi 15607215 168 DEPTAHLDF 176
Cdd:COG4167 174 DEALAALDM 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-189 |
1.42e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNkVGIVFQA--FNLVPSL 100
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 TAVENVMVPLRSAGMSRRASRRRAEE-LLARVNLAERMNHR-PGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQ 178
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAARVAwLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170
....*....|.
gi 15607215 179 VEEVLRLIREL 189
Cdd:PRK10261 499 RGQIINLLLDL 509
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-218 |
1.70e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.24 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGgyalRP-INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVD---------- 70
Cdd:COG4178 361 GALALEDLTLRTPDG----RPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGArvlflpqrpy 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 71 --ITTLQGAelanyrrnkvgIVFQAFNLVPSLTAVENVmvpLRSAGMSRrasrrraeeLLARVNLAERMNHRpgdLSGGQ 148
Cdd:COG4178 437 lpLGTLREA-----------LLYPATAEAFSDAELREA---LEAVGLGH---------LAERLDEEADWDQV---LSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 149 QQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVAtHDSRMLPMADRVVELTPD 218
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVG-HRSTLAAFHDRVLELTGD 559
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-213 |
2.53e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 33 GSLVMLLGPSGCGKTTLLSCLGGILRPKSG----AIKFDEVdITTLQGAELANY----RRNKVGIVF--QAFNLVPSLT- 101
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeEPSWDEV-LKRFRGTELQNYfkklYNGEIKVVHkpQYVDLIPKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 -AVENVMVPLRSAGMSRRasrrraeeLLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVE 180
Cdd:PRK13409 178 gKVRELLKKVDERGKLDE--------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRL 249
|
170 180 190
....*....|....*....|....*....|....
gi 15607215 181 EVLRLIRELADGERVVVVaTHDSRMLPM-ADRVV 213
Cdd:PRK13409 250 NVARLIRELAEGKYVLVV-EHDLAVLDYlADNVH 282
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-273 |
2.78e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.03 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEyySGGyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGI--LRPKSGAIKFDEVDITtlqgaELA 80
Cdd:COG0396 1 LEIKNLHVS--VEG---KEIlKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDIL-----ELS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 NYRRNKVGIvFQAFNLVPSLTAVeNVMVPLRSA-------GMSRRASRRRAEELLARVNLAERMNHRP--GDLSGGQQQR 151
Cdd:COG0396 71 PDERARAGI-FLAFQYPVEIPGV-SVSNFLRTAlnarrgeELSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 152 VAVARAIALDPPLILADEPTAHLD--FIQVeeVLRLIRELADGERVVVVATHDSRMLPmadrvvELTPDFaetnrppetV 229
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDidALRI--VAEGVNKLRSPDRGILIITHYQRILD------YIKPDF---------V 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15607215 230 H-LQAGEvlfeqstmgdliyVVSEGEFEIVHEL-ADGGEELVKVAG 273
Cdd:COG0396 212 HvLVDGR-------------IVKSGGKELALELeEEGYDWLKEEAA 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-201 |
2.96e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 33 GSLVMLLGPSGCGKTTLLSCLGGILRP---KSGAIKFDEVDITTLQGAELANYrrnkvgiVFQAFNLVPSLTAVE--NVM 107
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAY-------VQQDDLFIPTLTVREhlMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 108 VPLR-SAGMSRRASRRRAEELLARVNLAERMNHRPGD------LSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVE 180
Cdd:TIGR00955 124 AHLRmPRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180
....*....|....*....|.
gi 15607215 181 EVLRLIRELADGERVVVVATH 201
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIH 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-216 |
3.74e-16 |
|
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: 75.61 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEyySGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEvditTLQGAELANYR 83
Cdd:cd03231 1 LEADELTCE--RDGRAL--FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQAfNLVPSLTAVENVMVplrsagMSRRASRRRAEELLARVNLAErMNHRP-GDLSGGQQQRVAVARAIALDP 162
Cdd:cd03231 73 RGLLYLGHAP-GIKTTLSVLENLRF------WHADHSDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATH-DSRMLPMADRVVELT 216
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAGARELDLG 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-213 |
3.79e-16 |
|
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: 79.06 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 33 GSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIK----FDEVdITTLQGAELANYRRN------KVGIVFQAFNLVPS--- 99
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepsWDEV-LKRFRGTELQDYFKKlangeiKVAHKPQYVDLIPKvfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 ------LTAVENVMVplrsagmsrrasrrrAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAH 173
Cdd:COG1245 178 gtvrelLEKVDERGK---------------LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 174 LDFIQVEEVLRLIRELADGERVVVVATHDSRMLPM-ADRVV 213
Cdd:COG1245 243 LDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYlADYVH 283
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-213 |
5.07e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLvveyySGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD--EVDITTLQGAeLAN 81
Cdd:COG1129 257 LEVEGL-----SVGGVVRDVS---FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRIRSPRDA-IRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 yrrnkvGIVF-----QAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARvNLAERMNHRPGD-------LSGGQQ 149
Cdd:COG1129 328 ------GIAYvpedrKGEGLVLDLSIRENITLASLDRLSRGGLLDRRRERALAE-EYIKRLRIKTPSpeqpvgnLSGGNQ 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 150 QRVAVARAIALDPPLILADEPTAHLDfiqV---EEVLRLIRELADGERVVVVATHDsrmLP----MADRVV 213
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSE---LPellgLSDRIL 465
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-212 |
5.55e-16 |
|
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: 78.54 E-value: 5.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevdittlqGAELANYRRNK----VGIVFQAFNLVP 98
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD--------GADLKQWDRETfgkhIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 99 SlTAVENVMvplrSAGMSRRASRRRAEELLARV-----NLAERMNHRPGD----LSGGQQQRVAVARAIALDPPLILADE 169
Cdd:TIGR01842 406 G-TVAENIA----RFGENADPEKIIEAAKLAGVhelilRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15607215 170 PTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRV 212
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKI 523
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-213 |
9.71e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.69 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaeLANYRRNkVGIVFQA---FNlvps 99
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRN-IAVVFQDaglFN---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 LTAVENVMVPLRSAG---MSRRASRRRAEELLAR--VNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHL 174
Cdd:PRK13657 423 RSIEDNIRVGRPDATdeeMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190
....*....|....*....|....*....|....*....
gi 15607215 175 DFIQVEEVLRLIRELADGERVVVVAtHDSRMLPMADRVV 213
Cdd:PRK13657 503 DVETEAKVKAALDELMKGRTTFIIA-HRLSTVRNADRIL 540
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-215 |
1.17e-15 |
|
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: 74.67 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 13 YYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGIVFQ 92
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 93 AFNLVpSLTAVENVMV--PL---RSAGMSRRASRRRAEELLARVNLAErMNHRPGDLSGGQQQRVAVARAIALDPPLILA 167
Cdd:cd03290 87 KPWLL-NATVEENITFgsPFnkqRYKAVTDACSLQPDIDLLPFGDQTE-IGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15607215 168 DEPTAHLDFIQVEEVLR--LIRELADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:cd03290 165 DDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAM 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-265 |
1.20e-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: 74.10 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEyySGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPK--SGAIKFDEVDITtlqgaELAN 81
Cdd:cd03217 1 LEIKDLHVS--VGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDIT-----DLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 YRRNKVGIvFQAFNLVPSLTAVENVMVpLRSagmsrrasrrraeellarVNLAermnhrpgdLSGGQQQRVAVARAIALD 161
Cdd:cd03217 72 EERARLGI-FLAFQYPPEIPGVKNADF-LRY------------------VNEG---------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 162 PPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLpmadrvveltpDFAEtnrpPETVH-LQAGEvlfeq 240
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLL-----------DYIK----PDRVHvLYDGR----- 182
|
250 260
....*....|....*....|....*
gi 15607215 241 stmgdliyVVSEGEFEIVHELADGG 265
Cdd:cd03217 183 --------IVKSGDKELALEIEKKG 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-215 |
1.51e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 74.04 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEvDI----------- 71
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIayvsqepwiqn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 72 TTLQ-----GAELANYRRNKVgivFQAFNLVPSLTAVE---NVMVplrsagmsrrasrrraeellarvnlAER-MNhrpg 142
Cdd:cd03250 80 GTIRenilfGKPFDEERYEKV---IKACALEPDLEILPdgdLTEI-------------------------GEKgIN---- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 143 dLSGGQQQRVAVARAIALDPPLILADEPTAHLDfIQVEEVL--RLIRELADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:cd03250 128 -LSGGQKQRISLARAVYSDADIYLLDDPLSAVD-AHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVL 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-201 |
2.08e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGIL--RPKSGAIKFDEVDITtlqgaelanyrrNKVGIVFQAFNLVPSL 100
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG------------REASLIDAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 TAVEnvmvplrsagmsrrasrrraeeLLARVNLAERMNHR--PGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQ 178
Cdd:COG2401 114 DAVE----------------------LLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....
gi 15607215 179 VEEVLRLIRELAD-GERVVVVATH 201
Cdd:COG2401 172 AKRVARNLQKLARrAGITLVVATH 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-188 |
3.22e-15 |
|
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: 73.30 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGG-YALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELa 80
Cdd:cd03244 1 GDIEFKNVSLRYRPNLpPVLK---NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNKVGIVFQ---------AFNLVP----SLTAVENVmvplrsagmsrrasrrraeelLARVNLAERMNHRPG----- 142
Cdd:cd03244 77 ---RSRISIIPQdpvlfsgtiRSNLDPfgeySDEELWQA---------------------LERVGLKEFVESLPGgldtv 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15607215 143 ------DLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRE 188
Cdd:cd03244 133 veeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE 184
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-215 |
3.26e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.30 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKF-DEVDITTLQGAELANYRRnKVGIVFQAFNLVPSLTave 104
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLnGRVLFDAEKGICLPPEKR-RIGYVFQDARLFPHYK--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 105 nVMVPLRSaGMSRRASRR--RAEELLARVNLAERMnhrPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:PRK11144 93 -VRGNLRY-GMAKSMVAQfdKIVALLGIEPLLDRY---PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 183 LRLIRELAdgERV---VVVATHD-SRMLPMADRVVEL 215
Cdd:PRK11144 168 LPYLERLA--REInipILYVSHSlDEILRLADRVVVL 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-208 |
3.26e-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: 74.33 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 33 GSLVMLLGPSGCGKTTLLSCLGGILRPKSGaiKFDEVD-----ITTLQGAELANY----RRNKVGIVF--QAFNLVPSlt 101
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPdwdeiLDEFRGSELQNYftklLEGDVKVIVkpQYVDLIPK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 AVENVMVPLrsagMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:cd03236 102 AVKGKVGEL----LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|....*..
gi 15607215 182 VLRLIRELADGERVVVVATHDSRMLPM 208
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEHDLAVLDY 204
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-201 |
3.29e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 3 DLSIQNLVVEYYSGGYALRPingLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILrPKSGAIKFDEVDITTLqgaELANY 82
Cdd:PRK11174 349 TIEAEDLEILSPDGKTLAGP---LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELREL---DPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRNkVGIVFQafNlvPSL---TAVENVMVPLRSAGmsrrasRRRAEELLARVNLAE-------RMNHRPGD----LSGGQ 148
Cdd:PRK11174 422 RKH-LSWVGQ--N--PQLphgTLRDNVLLGNPDAS------DEQLQQALENAWVSEflpllpqGLDTPIGDqaagLSVGQ 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15607215 149 QQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVaTH 201
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMV-TH 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-213 |
5.20e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 24 NGLNLDVAAGSL-----VMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDeVDITtlqgaelanYRRNKVGIVFQafnlvp 98
Cdd:PRK13409 351 GDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS---------YKPQYIKPDYD------ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 99 sltavENVMVPLRSAGmSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDfiq 178
Cdd:PRK13409 415 -----GTVEDLLRSIT-DDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--- 485
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15607215 179 VEE---VLRLIRELADG-ERVVVVATHDSRMLPM-ADRVV 213
Cdd:PRK13409 486 VEQrlaVAKAIRRIAEErEATALVVDHDIYMIDYiSDRLM 525
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-201 |
5.57e-15 |
|
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: 76.21 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 6 IQNLVVEYYSGGyalRP-INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAElanyrR 84
Cdd:TIGR01257 931 VKNLVKIFEPSG---RPaVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-----R 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 85 NKVGIVFQAFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPL 164
Cdd:TIGR01257 1003 QSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 165 ILADEPTAHLDFIQVEEVLRLIRELADGeRVVVVATH 201
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSG-RTIIMSTH 1118
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-213 |
7.46e-15 |
|
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: 72.83 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 24 NGLNLDVAAGSL-----VMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgaelanYRRNKVGIVFQA----- 93
Cdd:cd03237 11 GEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKADYEGtvrdl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 94 -FNLVPSLTAVE----NVMVPLRsagmsrrasrrraeellarvnLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILAD 168
Cdd:cd03237 82 lSSITKDFYTHPyfktEIAKPLQ---------------------IEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15607215 169 EPTAHLDFIQVEEVLRLIRELAD-GERVVVVATHDSRMLPM-ADRVV 213
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFAEnNEKTAFVVEHDIIMIDYlADRLI 187
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-202 |
1.79e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKT-TLLSCLGGILRP---KSGAIKFDEVDITTLQG 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 AElanyRRNKVG----IVFQ--AFNLVPSLTAVENVMVPLRS-AGMSRRASRRRAEELLARVNL---AERMNHRPGDLSG 146
Cdd:PRK11022 81 KE----RRNLVGaevaMIFQdpMTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 147 GQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHD 202
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMaLVLITHD 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-213 |
1.98e-14 |
|
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: 71.59 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGaikfdEVDITTLQGAELANYRRNKVGIVF-QAFNLVPSLT 101
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG-----EVRVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 AVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190
....*....|....*....|....*....|....
gi 15607215 182 VLRLIREL-ADGERVVVVATHDSR-MLPMADRVV 213
Cdd:cd03267 192 IRNFLKEYnRERGTTVLLTSHYMKdIEALARRVL 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-189 |
2.53e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGK-TTLLSCLGgiLRPKSGAIKFDEVDITTLQGAELANYRRnKVGIVFQAFN--LVPS 99
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKsTTGLALLR--LINSQGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNssLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 LTAVENVMVPLR--SAGMSRRASRRRAEELLARVNLAERMNHR-PGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDF 176
Cdd:PRK15134 379 LNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDK 458
|
170
....*....|...
gi 15607215 177 IQVEEVLRLIREL 189
Cdd:PRK15134 459 TVQAQILALLKSL 471
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-202 |
2.54e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.30 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYAL-RPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKF----DEVDITTLqGAE 78
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKP-GPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 79 LANYRRNKVGIVFQAFNLVPSLTAVENVM------VPLRSAGMSRRASrrraeelLARVNLAER-----MNHRPGDLSGG 147
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTeaigleLPDELARMKAVIT-------LKMVGFDEEkaeeiLDKYPDELSEG 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 148 QQQRVAVARAIALDPPLILADEPTAHLDFI---QVEEVLRLIRElaDGERVVVVATHD 202
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPItkvDVTHSILKARE--EMEQTFIIVSHD 487
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-213 |
2.59e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.96 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGG-YALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDI-TTLQGAEL 79
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 80 ANYRRNKVGIVFQ--AFNLVPSLTAVENVMVPLrSAGMSRRASRRRAEELLARVNLAERMNHR-PGDLSGGQQQRVAVAR 156
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPV-NLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 157 AIALDPPLILADEPTAHLDFIQVEEVLRLIRELAD--GERVVVVATHDSRMLPMADRVV 213
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVI 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
17-217 |
3.15e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.18 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 17 GYALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDevdiTTLQGAELANYRRnkvgivfqafN 95
Cdd:COG0488 324 SYGDKTLlDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETVKIGYFDQHQE----------E 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVENVM--------VPLRSagmsrrasrrraeeLLARVNLAERMNHRP-GDLSGGQQQRVAVARaIALDPP--L 164
Cdd:COG0488 390 LDPDKTVLDELRdgapggteQEVRG--------------YLGRFLFSGDDAFKPvGVLSGGEKARLALAK-LLLSPPnvL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 165 ILaDEPTAHLDfIQVEEVLrlirE--LADGERVVVVATHDSRMLP-MADRVVELTP 217
Cdd:COG0488 455 LL-DEPTNHLD-IETLEAL----EeaLDDFPGTVLLVSHDRYFLDrVATRILEFED 504
|
|
| Crp |
COG0664 |
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
218-313 |
3.92e-14 |
|
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];
Pssm-ID: 440428 [Multi-domain] Cd Length: 207 Bit Score: 70.02 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 218 DFAETNRPPETVHLQAGEVLFEQSTMGDLIYVVSEGEFEIVHELADGGEELVKVAGPGDYFGEIGVLFHLPRSATVRARS 297
Cdd:COG0664 8 ELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSPATAEALE 87
|
90
....*....|....*.
gi 15607215 298 DATAVGYTVQAFRERL 313
Cdd:COG0664 88 DSELLRIPREDLEELL 103
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-201 |
4.00e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.22 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRP----INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaelANYRRNKVGIVFQA 93
Cdd:TIGR00958 488 YPNRPdvpvLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD----HHYLHRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 94 FNLVpSLTAVENVMVPLRSAGMSRRASRRRAEELLARV-NLAERMNHRPGD----LSGGQQQRVAVARAIALDPPLILAD 168
Cdd:TIGR00958 564 PVLF-SGSVRENIAYGLTDTPDEEIMAAAKAANAHDFImEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190
....*....|....*....|....*....|...
gi 15607215 169 EPTAHLDfIQVEEVLRLIRELADgeRVVVVATH 201
Cdd:TIGR00958 643 EATSALD-AECEQLLQESRSRAS--RTVLLIAH 672
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-215 |
5.24e-14 |
|
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: 69.75 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGgyaLRP-INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELa 80
Cdd:cd03369 5 GEIEVENLSVRYAPD---LPPvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNKVGIVFQAfnlvPSLtavenVMVPLRSAgmSRRASRRRAEELLARVNLAERMNhrpgDLSGGQQQRVAVARAIAL 160
Cdd:cd03369 81 ---RSSLTIIPQD----PTL-----FSGTIRSN--LDPFDEYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 161 DPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVAtHDSRMLPMADRVVEL 215
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIA-HRLRTIIDYDKILVM 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-215 |
5.92e-14 |
|
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: 69.87 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKfdevdittlqgaelanyRRNKVGIVFqAFN-- 95
Cdd:cd03220 36 WALK---DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----------------VRGRVSSLL-GLGgg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:cd03220 95 FNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 176 FIQVEEVLRLIRELADGERVVVVATHDSRML-PMADRVVEL 215
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVL 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-213 |
2.53e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.58 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 24 NGLNLDVAAGSL-----VMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDeVDITtlqgaelanYRRNKVGIVFQafnlvp 98
Cdd:COG1245 352 GGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKIS---------YKPQYISPDYD------ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 99 sltavENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDfiq 178
Cdd:COG1245 416 -----GTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--- 487
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15607215 179 VEE---VLRLIRELADG-ERVVVVATHDSRMLPM-ADRVV 213
Cdd:COG1245 488 VEQrlaVAKAIRRFAENrGKTAMVVDHDIYLIDYiSDRLM 527
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-215 |
2.72e-13 |
|
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: 70.21 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 15 SGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqGAELANYRRNkVGIVFQAF 94
Cdd:COG4615 343 DEGFTLGPID---LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQL-FSAVFSDF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 95 NLVPSLtavenvmvplrsAGMSRRASRRRAEELLARVNLAERMNHRPG-----DLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:COG4615 416 HLFDRL------------LGLDGEADPARARELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15607215 170 PTAHLD--FIQV--EEVLRLIRelADGeRVVVVATHDSRMLPMADRVVEL 215
Cdd:COG4615 484 WAADQDpeFRRVfyTELLPELK--ARG-KTVIAISHDDRYFDLADRVLKM 530
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-210 |
2.83e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTlqgaELANYRRnKVGIVFQAFNLVPSLTA 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQK-QLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAGmsrraSRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEV 182
Cdd:PRK13540 92 RENCLYDIHFSP-----GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|....*...
gi 15607215 183 LRLIRELADGERVVVVATHDSRMLPMAD 210
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-215 |
6.57e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqGAELANYR 83
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RnKVGIVFQAFNLVPSLTAVENVMVPlrsagmsrrasRRRAEELLARVNLAERMNHRPG-----DLSGGQQQRVAVARAI 158
Cdd:PRK10522 397 K-LFSAVFTDFHLFDQLLGPEGKPAN-----------PALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607215 159 ALDPPLILADEPTAHLD--FIQV--EEVLRLIRELAdgeRVVVVATHDSRMLPMADRVVEL 215
Cdd:PRK10522 465 AEERDILLLDEWAADQDphFRREfyQVLLPLLQEMG---KTIFAISHDDHYFIHADRLLEM 522
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-191 |
8.31e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.99 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 27 NLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD--EVDITTLQGAelanyRRNKVGIVFQAFNLVPSLTAVE 104
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkEIDFKSSKEA-----LENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 105 NVMV---PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:PRK10982 93 NMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170
....*....|
gi 15607215 182 VLRLIRELAD 191
Cdd:PRK10982 173 LFTIIRKLKE 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-215 |
1.09e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 22 PING-LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANYRRNKVGivfqafnLVPSL 100
Cdd:PRK13543 25 PVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPG-------LKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 TAVENVMVplrSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARaIALDP-PLILADEPTAHLDFIQV 179
Cdd:PRK13543 98 STLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPaPLWLLDEPYANLDLEGI 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 180 EEVLRLIRELADGERVVVVATHDSR-MLPMADRVVEL 215
Cdd:PRK13543 174 TLVNRMISAHLRGGGAALVTTHGAYaAPPVRTRMLTL 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-215 |
1.61e-12 |
|
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: 65.96 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRP----INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQgaelANYRRNKVGIVFQA 93
Cdd:cd03248 21 YPTRPdtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE----HKYLHSKVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 94 FNLVpSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAER-----MNHRPGDLSGGQQQRVAVARAIALDPPLILAD 168
Cdd:cd03248 97 PVLF-ARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASgydteVGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15607215 169 EPTAHLDFIQVEEVLRLIRELADGERVVVVAtHDSRMLPMADRVVEL 215
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLVIA-HRLSTVERADQILVL 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
38-213 |
4.46e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.20 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 38 LLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAelanYRRNKVGIVFQ--AFNLVPSLTAVENVMVPLR-SAG 114
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS----YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRlNTD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 115 MSRRASRRRAEELLARVNL-AERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELAD-- 191
Cdd:PRK15112 120 LEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkq 199
|
170 180
....*....|....*....|..
gi 15607215 192 GERVVVVATHDSRMLPMADRVV 213
Cdd:PRK15112 200 GISYIYVTQHLGMMKHISDQVL 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-218 |
5.41e-12 |
|
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: 63.33 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIkfdevdittlqgaelanyrrnkvgivfqafnlvpSLTAVEN 105
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------------------------GMPEGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 106 VM-VPLRSagmsrrasrrraeeLLARVNLAERMNHrPGD--LSGGQQQRVAVARAIALDPPLILADEPTAHLDfiqvEEV 182
Cdd:cd03223 66 LLfLPQRP--------------YLPLGTLREQLIY-PWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EES 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 183 LRLIRELADGERVVVVA-THDSRMLPMADRVVELTPD 218
Cdd:cd03223 127 EDRLYQLLKELGITVISvGHRPSLWKFHDRVLDLDGE 163
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-216 |
6.23e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSgaikfdevdittLQGAELANYRR------NKVGIVFQAFNL 96
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN------------FTGTILANNRKptkqilKRTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 VPSLTAVENVMVP--LR-SAGMSRRASRRRAEELLARVNLAERMNHRPGD-----LSGGQQQRVAVARAIALDPPLILAD 168
Cdd:PLN03211 152 YPHLTVRETLVFCslLRlPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15607215 169 EPTAHLDFIQVEEVLRLIRELADGERVVVVATH--DSRMLPMADRVVELT 216
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHqpSSRVYQMFDSVLVLS 281
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-201 |
1.26e-11 |
|
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: 62.65 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGilRPKSGAIKFDevdiTTLQGAEL-ANY 82
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITGE----ILINGRPLdKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 83 RRnKVGIVFQAFNLVPSLTavenVMVPLR-SAgmsrrasrrraeelLARvnlaermnhrpgDLSGGQQQRVAVARAIALD 161
Cdd:cd03232 78 QR-STGYVEQQDVHSPNLT----VREALRfSA--------------LLR------------GLSVEQRKRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15607215 162 PPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATH 201
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-218 |
2.19e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 7 QNLVVEYYSGGYALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFdevdittlqgAELANyrrn 85
Cdd:PRK15064 318 NALEVENLTKGFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENAN---- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 86 kVGIVFQ--AFNLVPSLTAVEnVMVPLRSAGMSRRASRRRAEELLARvnlAERMNHRPGDLSGGQQQRVAVARAIALDPP 163
Cdd:PRK15064 384 -IGYYAQdhAYDFENDLTLFD-WMSQWRQEGDDEQAVRGTLGRLLFS---QDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 164 LILADEPTAHLDFIQVEEvLRLIRELADGERVVVvaTHDSRMLP-MADRVVELTPD 218
Cdd:PRK15064 459 VLVMDEPTNHMDMESIES-LNMALEKYEGTLIFV--SHDREFVSsLATRIIEITPD 511
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-200 |
2.54e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.89 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPK---SGAIKFDevditTLQGAELANYRRNKVGIVFQAFNLVPS 99
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYN-----GIPYKEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 LTaVENVMvplrsagmsrrasrrraeellarvNLAERMNhrpGD-----LSGGQQQRVAVARAIALDPPLILADEPTAHL 174
Cdd:cd03233 98 LT-VRETL------------------------DFALRCK---GNefvrgISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180
....*....|....*....|....*.
gi 15607215 175 DFIQVEEVLRLIRELADGERVVVVAT 200
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVS 175
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-218 |
3.43e-11 |
|
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: 61.85 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 35 LVMLLGPSGCGKTTLLSC----LGGILRPKSGAIKFDEVDITTlqGAELAnyrrnKVGIVFQAFN-----LVPSLTAVEN 105
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkyaLTGELPPNSKGGAHDPKLIRE--GEVRA-----QVKLAFENANgkkytITRSLAILEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 106 VmVPLRSAGMSRrasrrraeellarvnLAERMnhrPGDLSGGQQQ------RVAVARAIALDPPLILADEPTAHLDFIQV 179
Cdd:cd03240 97 V-IFCHQGESNW---------------PLLDM---RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 180 EEVLRLIRELADGERV--VVVATHDSRMLPMADRVVELTPD 218
Cdd:cd03240 158 EESLAEIIEERKSQKNfqLIVITHDEELVDAADHIYRVEKD 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-189 |
4.20e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELAnyRRnkVGIVFQAFNLVPSLTAVEN 105
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 106 VMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGD----LSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
....*...
gi 15607215 182 VLRLIREL 189
Cdd:PRK10253 182 LLELLSEL 189
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-213 |
5.51e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDE----------VDITT 73
Cdd:PRK10261 13 LAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 74 LQGAELANYRRNKVGIVFQA--FNLVPSLTAVENVMVPLR-SAGMSRRASRRRAEELLARVNLAER---MNHRPGDLSGG 147
Cdd:PRK10261 93 QSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 148 QQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIREL-ADGERVVVVATHDSRMLP-MADRVV 213
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAeIADRVL 240
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-199 |
5.90e-11 |
|
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: 63.30 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrRNKVGIVFQ---AFNL 96
Cdd:COG5265 371 RPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQdtvLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 97 vpslTAVENVMVPLRSAGMsrrasrrraeellARVNLAERMNH--------------RPGD----LSGGQQQRVAVARAI 158
Cdd:COG5265 447 ----TIAYNIAYGRPDASE-------------EEVEAAARAAQihdfieslpdgydtRVGErglkLSGGEKQRVAIARTL 509
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 159 ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVA 199
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIA 550
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
13-239 |
6.24e-11 |
|
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: 60.41 E-value: 6.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 13 YYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLlsCLGGIlrPKSGAIKFDEvdittlqgaELANYRRNKvgIVFq 92
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGL--YASGKARLIS---------FLPKFSRNK--LIF- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 93 afnlVPSLTAVENVMvplrsagmsrrasrrraeelLARVNLAERMNhrpgDLSGGQQQRVAVARAIALDPP--LILADEP 170
Cdd:cd03238 65 ----IDQLQFLIDVG--------------------LGYLTLGQKLS----TLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 171 TAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVELTPdfaETNRppetvhlQAGEVLFE 239
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGP---GSGK-------SGGKVVFS 175
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
21-175 |
6.60e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 6.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEvdittlqgaelanyrRNKVGIVFQAFNLVPSL 100
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------------KLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 101 TAVENVMVPLRSAgmsrrASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:PRK09544 83 PLTVNRFLRLRPG-----TKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-217 |
1.10e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.87 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEyysggyALRP-INGLNLDVAAGSLVMLLGPSGCGKTtlLSCLG--GILRP----KSGAIKFDEVDIttlqg 76
Cdd:PRK10418 5 IELRNIALQ------AAQPlVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAalGILPAgvrqTAGRVLLDGKPV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 aELANYRRNKVGIVFQ----AFNlvPSLTAVENVMVPLRSAGmsRRASRRRAEELLARVNLAER---MNHRPGDLSGGQQ 149
Cdd:PRK10418 72 -APCALRGRKIATIMQnprsAFN--PLHTMHTHARETCLALG--KPADDATLTAALEAVGLENAarvLKLYPFEMSGGML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 150 QRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADgERV--VVVATHD--------SRMLPMAD-RVVELTP 217
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQ-KRAlgMLLVTHDmgvvarlaDDVAVMSHgRIVEQGD 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-215 |
2.32e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEvDITTLqgaeLAnyrrnkVGIVFQafnlv 97
Cdd:COG1134 40 WALK---DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL----LE------LGAGFH----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 98 PSLTAVENVMVPLRSAGMSrrasrrraeellaRVNLAERMN------------HRP-GDLSGGQQQRVAVARAIALDPPL 164
Cdd:COG1134 101 PELTGRENIYLNGRLLGLS-------------RKEIDEKFDeivefaelgdfiDQPvKTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 165 ILADEPTAhldfiqV------EEVLRLIRELADGERVVVVATHDSRML-PMADRVVEL 215
Cdd:COG1134 168 LLVDEVLA------VgdaafqKKCLARIRELRESGRTVIFVSHSMGAVrRLCDRAIWL 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-202 |
2.56e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 38 LLGPSGCGKTTLLSCLGGILRPKSGAIKFDEvdittlqGAelanyrrnKVGIVFQAFNLVPSLTAVENVMVPLRSAgmsr 117
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQP-------GI--------KVGYLPQEPQLDPTKTVRENVEEGVAEI---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 118 rasrrraEELLARVN---------------LAERM---------------NHR-----------PGD-----LSGGQQQR 151
Cdd:TIGR03719 97 -------KDALDRFNeisakyaepdadfdkLAAEQaelqeiidaadawdlDSQleiamdalrcpPWDadvtkLSGGERRR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 152 VAVARAIALDPPLILADEPTAHLDfiqVEEVLRLIRELADGERVVVVATHD 202
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-213 |
4.33e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAikfdEVDIttlqgaelanyrRNKVGIVFQA---FNLvpslTA 102
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA----SVVI------------RGTVAYVPQVswiFNA----TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMV-----PLRSAGMSRRASRRRAEELLARVNLAErMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFI 177
Cdd:PLN03130 696 RDNILFgspfdPERYERAIDVTALQHDLDLLPGGDLTE-IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190
....*....|....*....|....*....|....*...
gi 15607215 178 QVEEVLR--LIRELADGERVVVvaTHDSRMLPMADRVV 213
Cdd:PLN03130 775 VGRQVFDkcIKDELRGKTRVLV--TNQLHFLSQVDRII 810
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-189 |
5.21e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 27 NLDVAAGSLVMLLGPSGCGKTTLLSCLGGILrPK---SGAIKFDevdittlqgAELANYRR----NKVGIVF--QAFNLV 97
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFD---------GEVCRFKDirdsEALGIVIihQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 98 PSLTAVENVMV---PLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHL 174
Cdd:NF040905 91 PYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170
....*....|....*
gi 15607215 175 DFIQVEEVLRLIREL 189
Cdd:NF040905 171 NEEDSAALLDLLLEL 185
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-188 |
5.88e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGGYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELan 81
Cdd:PRK10790 339 GRIDIDNVSFAYRDDNLVLQNIN---LSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 yrRNKVGIVfQAFNLVPSLTAVENVMvplrsagMSRRASRRRAEELLARVNLAE-----------RMNHRPGDLSGGQQQ 150
Cdd:PRK10790 414 --RQGVAMV-QQDPVVLADTFLANVT-------LGRDISEEQVWQALETVQLAElarslpdglytPLGEQGNNLSVGQKQ 483
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 151 RVAVARAIALDPPLILADEPTAHLDF---IQVEEVLRLIRE 188
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVRE 524
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-227 |
6.11e-10 |
|
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: 57.58 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 29 DVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgaelanYRRNKVgivfqafnlvpsltavenvmv 108
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV---------YKPQYI--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 109 plrsagmsrrasrrraeellarvnlaermnhrpgDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRE 188
Cdd:cd03222 71 ----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15607215 189 LAD-GERVVVVATHDSRMLP-MADR--VVELTPDFAETNRPPE 227
Cdd:cd03222 117 LSEeGKKTALVVEHDLAVLDyLSDRihVFEGEPGVYGIASQPK 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-216 |
7.41e-10 |
|
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: 60.34 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILR---------------PKSGAIKFDEVDITTLQGAEL-ANYRRNk 86
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDkveghvhmkgsvayvPQQAWIQNDSLRENILFGKALnEKYYQQ- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 87 vgiVFQAFNLVPSLTavenvMVPlrsAGmsrrasrrraeellARVNLAERmnhrpG-DLSGGQQQRVAVARAIALDPPLI 165
Cdd:TIGR00957 733 ---VLEACALLPDLE-----ILP---SG--------------DRTEIGEK-----GvNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 166 LADEP----TAHLDFIQVEEVLRLIRELADGERVVVvaTHDSRMLPMADRVVELT 216
Cdd:TIGR00957 783 LFDDPlsavDAHVGKHIFEHVIGPEGVLKNKTRILV--THGISYLPQVDVIIVMS 835
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-212 |
8.35e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.05 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGI----LRPKSGAIKFDEVDITTLQG 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 AELANYRRNKVGIVFQAFN--LVPSLTAVENVM--VP---------------LRSAgmsrrasrrraEELLARVNLAER- 136
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQscLDPSERVGRQLMqnIPgwtykgrwwqrfgwrKRRA-----------IELLHRVGIKDHk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 137 --MNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIREL-ADGERVVVVATHDSRMLP-MADRV 212
Cdd:PRK15093 150 daMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSqWADKI 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-205 |
8.63e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.65 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELANyrrnKVGIVFQAFNLVPSLTAVEN 105
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 106 VMV---PLRSA-GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEE 181
Cdd:PRK10575 106 VAIgryPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180
....*....|....*....|....*
gi 15607215 182 VLRLIRELADGERVVVVAT-HDSRM 205
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVlHDINM 210
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-222 |
2.09e-09 |
|
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: 55.83 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 144 LSGGQQQRVAVARAIAL----DPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVELTPDF 219
Cdd:cd03227 78 LSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKVI 157
|
...
gi 15607215 220 AET 222
Cdd:cd03227 158 TGV 160
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-175 |
2.63e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.11 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNlVVEYYSG--GYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDittLQGAEL 79
Cdd:PRK11176 340 GDIEFRN-VTFTYPGkeVPALRNIN---FKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 80 ANYRrNKVGIVFQAFNLVPSlTAVENVmvplrsAGMSRRASRRRAEELLARVNLA----ERMNHrpG----------DLS 145
Cdd:PRK11176 413 ASLR-NQVALVSQNVHLFND-TIANNI------AYARTEQYSREQIEEAARMAYAmdfiNKMDN--GldtvigengvLLS 482
|
170 180 190
....*....|....*....|....*....|
gi 15607215 146 GGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-265 |
2.73e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSGGYalrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGI--LRPKSGAIKFDEVDITtlqgaELAN 81
Cdd:PRK09580 2 LSIKDLHVSVEDKAI----LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLL-----ELSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 YRRNKVGIvFQAFNLVPSLTAVENVMVpLRSAgmSRRASRRRAEELLARVNLAERMNHR------PGDL---------SG 146
Cdd:PRK09580 73 EDRAGEGI-FMAFQYPVEIPGVSNQFF-LQTA--LNAVRSYRGQEPLDRFDFQDLMEEKiallkmPEDLltrsvnvgfSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 147 GQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMadrvveLTPDFaetnrpp 226
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDY------IKPDY------- 215
|
250 260 270
....*....|....*....|....*....|....*....
gi 15607215 227 etVHlqageVLFEQStmgdliyVVSEGEFEIVHELADGG 265
Cdd:PRK09580 216 --VH-----VLYQGR-------IVKSGDFTLVKQLEEQG 240
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-212 |
3.68e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAElanyrRNKVGIVF-----QAFNLVPSL 100
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 TAVENVmVPLRSAGMSRRASRRRAEELLARVN--LAERMNHRP---GDLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:PRK15439 357 PLAWNV-CALTHNRRGFWIKPARENAVLERYRraLNIKFNHAEqaaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190
....*....|....*....|....*....|....*...
gi 15607215 176 FIQVEEVLRLIRELADGERVVVVATHDSRMLP-MADRV 212
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEqMADRV 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-212 |
3.85e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 14 YSGGYALRpinGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAelanyRRNKVGI--VF 91
Cdd:PRK15439 21 YSGVEVLK---GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-----KAHQLGIylVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 92 QAFNLVPSLTAVENVMVPL-RSAGmsrraSRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEP 170
Cdd:PRK15439 93 QEPLLFPNLSVKENILFGLpKRQA-----SMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15607215 171 TAHLDFIQVEEVLRLIRELADGERVVVVATHDsrmLP----MADRV 212
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHK---LPeirqLADRI 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-215 |
4.05e-09 |
|
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: 54.69 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 33 GSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrrnkvgivfqafnlvpsltavenvmvplrs 112
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQ--------------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 113 agmsrrasrrraeellarvNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADG 192
Cdd:smart00382 49 -------------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 15607215 193 ERV------VVVATHDSR------MLPMADRVVEL 215
Cdd:smart00382 110 LLKseknltVILTTNDEKdlgpalLRRRFDRRIVL 144
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-216 |
5.95e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAikfdEVDIttlqgaelanyrRNKVGIVFQA---FNLvps 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS----SVVI------------RGSVAYVPQVswiFNA--- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 100 lTAVENVMV-----PLRSAGMSRRASRRRAEELLARVNLAErMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHL 174
Cdd:PLN03232 694 -TVRENILFgsdfeSERYWRAIDVTALQHDLDLLPGRDLTE-IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15607215 175 DFIQVEEVLR--LIRELADGERVVVvaTHDSRMLPMADRVVELT 216
Cdd:PLN03232 772 DAHVAHQVFDscMKDELKGKTRVLV--TNQLHFLPLMDRIILVS 813
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
39-201 |
8.08e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 39 LGPSGCGKTTLLSCLGGILRPKSG-AIKF----DEVDITTlqgaelanyrRNKVGIVFQAFNLVPSLTAVENVMVPLRSA 113
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGeAWLFgqpvDAGDIAT----------RRRVGYMSQAFSLYGELTVRQNLELHARLF 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 114 GMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPP-LILaDEPTAHLDFIQVEEVLRLIRELADG 192
Cdd:NF033858 368 HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPElLIL-DEPTSGVDPVARDMFWRLLIELSRE 446
|
170
....*....|
gi 15607215 193 ERVVV-VATH 201
Cdd:NF033858 447 DGVTIfISTH 456
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-202 |
1.14e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 38 LLGPSGCGKTTLLSCLGGILRPKSGAIKFDEvdittlqGAelanyrrnKVGIVFQAFNLVPSLTAVENVMVPLRSAgmsr 117
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAP-------GI--------KVGYLPQEPQLDPEKTVRENVEEGVAEV---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 118 rasrrraEELLARVN---------------LAERM---------------NHR-----------PGD-----LSGGQQQR 151
Cdd:PRK11819 99 -------KAALDRFNeiyaayaepdadfdaLAAEQgelqeiidaadawdlDSQleiamdalrcpPWDakvtkLSGGERRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15607215 152 VAVARAIALDPPLILADEPTAHLDfiqVEEVLRLIRELADGERVVVVATHD 202
Cdd:PRK11819 172 VALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-208 |
1.46e-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: 56.07 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLggiLRPKS--GAIKFDEV--DITTLQga 77
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL---LRLLSteGEIQIDGVswNSVTLQ-- 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 78 elaNYRRnkvgivfqAFNLVPsltavENVMVPLRSAGMSRRASRRRAEELLAR----VNLAERMNHRPGD---------- 143
Cdd:TIGR01271 1289 ---TWRK--------AFGVIP-----QKVFIFSGTFRKNLDPYEQWSDEEIWKvaeeVGLKSVIEQFPDKldfvlvdggy 1352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 144 -LSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVeEVLRLIRELADGERVVVVATHdsRMLPM 208
Cdd:TIGR01271 1353 vLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTL-QIIRKTLKQSFSNCTVILSEH--RVEAL 1415
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-212 |
1.95e-08 |
|
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: 55.33 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQnlvVEYYSGGYALRP-INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDE-VDITTL-QGA 77
Cdd:TIGR03719 318 LGDKVIE---AENLTKAFGDKLlIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtVKLAYVdQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 78 ELANYRRNkvgiVFQAFNLVPSLTAVENVMVPLRSagmsrrasrrraeeLLARVNL-AERMNHRPGDLSGGQQQRVAVAR 156
Cdd:TIGR03719 395 DALDPNKT----VWEEISGGLDIIKLGKREIPSRA--------------YVGRFNFkGSDQQKKVGQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 157 AIALDPPLILADEPTAHLDFiqveEVLRLIRE-LADGERVVVVATHDSRMLpmaDRV 212
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDV----ETLRALEEaLLNFAGCAVVISHDRWFL---DRI 506
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-206 |
2.46e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 14 YSGGYAL-RPIN-GLNLDvaagSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIkfdevdittlqgaelanYRRNKVGIVF 91
Cdd:PLN03073 518 YPGGPLLfKNLNfGIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 92 QAFNLVPSLTAVENVMVPLRSA--GMSRRASRRRAEELLARVNLAERMNHrpgDLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:PLN03073 577 FSQHHVDGLDLSSNPLLYMMRCfpGVPEQKLRAHLGSFGVTGNLALQPMY---TLSGGQKSRVAFAKITFKKPHILLLDE 653
|
170 180 190
....*....|....*....|....*....|....*..
gi 15607215 170 PTAHLDFIQVEEvlrLIRELADGERVVVVATHDSRML 206
Cdd:PLN03073 654 PSNHLDLDAVEA---LIQGLVLFQGGVLMVSHDEHLI 687
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
137-213 |
3.33e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 3.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 137 MNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELAD-GERVVVVATHDSRMLPMADRVV 213
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADdGKVILMVSSELPEIITVCDRIA 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
142-229 |
4.63e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.45 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 142 GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELA-DGERVVVVATHDSRMLPMADRVV-----EL 215
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGLSDRVLvigegKL 481
|
90
....*....|....
gi 15607215 216 TPDFAETNRPPETV 229
Cdd:TIGR02633 482 KGDFVNHALTQEQV 495
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
143-215 |
6.55e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 6.55e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607215 143 DLSGGQQQRVAVARAIALDPPLILADEPTAHLDfiqVEEVLRLIRELADGERVVVVATHD-SRMLPMADRVVEL 215
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD---IETIEWLEGFLKTFQGSIIFISHDrSFIRNMATRIVDL 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-215 |
7.59e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.91 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGIL----RPKSGAIKFDevdiTTLQGAELANYRRNKV----GIVFQAF 94
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGARVTGD----VTLNGEPLAAIDAPRLarlrAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 95 NLVPSLTAVENVMVP----LRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIA---------LD 161
Cdd:PRK13547 93 QPAFAFSAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 162 PPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVA-THDSRMLPM-ADRVVEL 215
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAiVHDPNLAARhADRIAML 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-210 |
8.24e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.55 E-value: 8.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSGGYALrpINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKsGAIKFDEVDITTLQgaeLAN 81
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP---LQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 82 YRRnkvgivfqAFNLVPsltavENVMV---PLRSAGMSRRASRRRAEELLA-RVNLAERMNHRPGD-----------LSG 146
Cdd:cd03289 75 WRK--------AFGVIP-----QKVFIfsgTFRKNLDPYGKWSDEEIWKVAeEVGLKSVIEQFPGQldfvlvdggcvLSH 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607215 147 GQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRElADGERVVVVATHdsRMLPMAD 210
Cdd:cd03289 142 GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEH--RIEAMLE 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-215 |
1.04e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.55 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD---------------EVDITTLQGAELANYRRNKVgiv 90
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSgrisfssqfswimpgTIKENIIFGVSYDEYRYKSV--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 91 FQAFNLVPSLTAV-ENVMVPLRSAGMSrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:cd03291 133 VKACQLEEDITKFpEKDNTVLGEGGIT---------------------------LSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15607215 170 PTAHLDFIQVEEVLR--LIRELADGERVVVvaTHDSRMLPMADRVVEL 215
Cdd:cd03291 186 PFGYLDVFTEKEIFEscVCKLMANKTRILV--TSKMEHLKKADKILIL 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-206 |
1.19e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 9 LVVEYYSGGYALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGaikfdevDITTLQGAELANYRRNKV 87
Cdd:PRK10636 313 LKMEKVSAGYGDRIIlDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIGLAKGIKLGYFAQHQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 88 GIvfqafnlvpsLTAVENvmvPLRS-AGMSRRASRRRAEELLARVNL-AERMNHRPGDLSGGQQQRVAVARAIALDPPLI 165
Cdd:PRK10636 386 EF----------LRADES---PLQHlARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15607215 166 LADEPTAHLDFIQVEEvlrLIRELADGERVVVVATHDSRML 206
Cdd:PRK10636 453 LLDEPTNHLDLDMRQA---LTEALIDFEGALVVVSHDRHLL 490
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
23-270 |
1.23e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGilRPK----SGAIKFDEVDITTLQGAElanyrRNKVGIvFQAFNLVP 98
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEE-----RAHLGI-FLAFQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 99 SLTAVENvMVPLRSA--------GMSRRASRRRAEEL---LARVNLAERMNHRPGD--LSGGQQQRVAVARAIALDPPLI 165
Cdd:CHL00131 95 EIPGVSN-ADFLRLAynskrkfqGLPELDPLEFLEIInekLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 166 LADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLpmaDRVVeltPDFaetnrppetVH-LQAGEvlfeqstmg 244
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLL---DYIK---PDY---------VHvMQNGK--------- 229
|
250 260
....*....|....*....|....*.
gi 15607215 245 dliyVVSEGEFEIVHELADGGEELVK 270
Cdd:CHL00131 230 ----IIKTGDAELAKELEKKGYDWLK 251
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-213 |
2.19e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITtlqgAELANYRRNkVGIVF-QAFNLVPSLT 101
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF----KRRKEFARR-IGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 AVENvmvpLRsagmsrrasrrraeeLLARV-------------NLAERMN-----HRP-GDLSGGQQQRVAVARAIALDP 162
Cdd:COG4586 113 AIDS----FR---------------LLKAIyripdaeykkrldELVELLDlgellDTPvRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDsrmlpMAD------RVV 213
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTtILLTSHD-----MDDiealcdRVI 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-212 |
2.81e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.44 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 1 MGDLSIQNLVVEYYSGGYALRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPK----SGAIKFDEVDITTLQG 76
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 AElanyRRNKVG----IVFQ--AFNLVPSLTAVENVM--VPLRSAG----MSRRASRRRAEELLARVNLAER---MNHRP 141
Cdd:COG4170 81 RE----RRKIIGreiaMIFQepSSCLDPSAKIGDQLIeaIPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDHkdiMNSYP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 142 GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERV-VVVATHDSRML-PMADRV 212
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTsILLISHDLESIsQWADTI 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
137-213 |
3.02e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 3.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 137 MNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIREL-ADGERVVVVATHDSRMLPMADRVV 213
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkAEGLSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
142-229 |
3.03e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 142 GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELAD-GERVVVVATHDSRMLPMADRVV-----EL 215
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGLSDRVLvmhegKL 483
|
90
....*....|....
gi 15607215 216 TPDFAETNRPPETV 229
Cdd:PRK13549 484 KGDLINHNLTQEQV 497
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-201 |
6.47e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 33 GSLVMLLGPSGCGKTTLLSCLGGilRPKSGAIKFDeVDITTLQG-----AELANYRRN----------KVGIVFQAFNLV 97
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGD-IRISGFPKkqetfARISGYCEQndihspqvtvRESLIYSAFLRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 98 PSLTAVENVMVplrsagmsrraSRRRAEELLARVNLAERMNHRPG--DLSGGQQQRVAVARAIALDPPLILADEPTAHLD 175
Cdd:PLN03140 983 PKEVSKEEKMM-----------FVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180
....*....|....*....|....*.
gi 15607215 176 FIQVEEVLRLIRELADGERVVVVATH 201
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
144-218 |
8.55e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 8.55e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 144 LSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELAD-GERVVVVATHDSRMLPMADRVVEL-TPD 218
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKRSDKIVVFnNPD 1435
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-191 |
1.26e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 20 LRPINGLnldVAAGSLVMLLGPSGCGKTTLL----SCLGGILRPKSGAIKFDEVDittlqGAELANYRRNKVGIVFQAFN 95
Cdd:TIGR00956 77 LKPMDGL---IKPGELTVVLGRPGSGCSTLLktiaSNTDGFHIGVEGVITYDGIT-----PEEIKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 96 LVPSLTAVENV-------MVPLRSAGMSRRASRRRAEELLARV-NLAERMNHRPGD-----LSGGQQQRVAVARAIALDP 162
Cdd:TIGR00956 149 HFPHLTVGETLdfaarckTPQNRPDGVSREEYAKHIADVYMATyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170 180
....*....|....*....|....*....
gi 15607215 163 PLILADEPTAHLDFIQVEEVLRLIRELAD 191
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSAN 257
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-209 |
1.37e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 4 LSIQNLVVEYYSggyalRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELAnYR 83
Cdd:PRK13541 2 LSLHQLQFNIEQ-----KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT-YI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 84 RNKVGIVFQafnlvpsLTAVENVMVplrsagmsRRASRRRAEELLARVN---LAERMNHRPGDLSGGQQQRVAVARAIAL 160
Cdd:PRK13541 76 GHNLGLKLE-------MTVFENLKF--------WSEIYNSAETLYAAIHyfkLHDLLDEKCYSLSSGMQKIVAIARLIAC 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 161 DPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMA 209
Cdd:PRK13541 141 QSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKSA 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
142-213 |
1.46e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607215 142 GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDsrmLP----MADRVV 213
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSD---LPevlgVADRIV 467
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-238 |
1.58e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 144 LSGGQQQRVAVARAIA--LDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVELTPDFAe 221
Cdd:PRK00635 477 LSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGAG- 555
|
90
....*....|....*..
gi 15607215 222 tnrppetvhLQAGEVLF 238
Cdd:PRK00635 556 ---------IFGGEVLF 563
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-171 |
1.69e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 24 NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAikfdevdITTLqGAELANYR-RNKVG--IvfqAF------ 94
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGR-------VEVL-GGDMADARhRRAVCprI---AYmpqglg 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 95 -NLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNhRP-GDLSGGQQQRVAVARAIALDPPLILADEPT 171
Cdd:NF033858 87 kNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFAD-RPaGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-215 |
1.80e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.33 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELanyrRNKVGIVFQAFNLVpSLTA 102
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQTPFLF-SDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 103 VENVMVPLRSAgmsrRASRRRAEELLARV-----NLAERMNHRPGD----LSGGQQQRVAVARAIALDPPLILADEPTAH 173
Cdd:PRK10789 406 ANNIALGRPDA----TQQEIEHVARLASVhddilRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15607215 174 LDFIQVEEVLRLIRELADGeRVVVVATHDSRMLPMADRVVEL 215
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEG-RTVIISAHRLSALTEASEILVM 522
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-215 |
2.80e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 26 LNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFD---------------EVDITTLQGAELANYRRNKVgiv 90
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSgrisfspqtswimpgTIKDNIIFGLSYDEYRYTSV--- 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 91 FQAFNLVPSLTAV-ENVMVPLRSAGMSrrasrrraeellarvnlaermnhrpgdLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:TIGR01271 522 IKACQLEEDIALFpEKDKTVLGEGGIT---------------------------LSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15607215 170 PTAHLDFIQVEEVLR--LIRELADGERVVVvaTHDSRMLPMADRVVEL 215
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEscLCKLMSNKTRILV--TSKLEHLKKADKILLL 620
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
127-217 |
4.33e-06 |
|
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: 46.87 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 127 LLARVNLAER-------------MNHRPGDLSGGQQQRVAVARAI--ALDPPLILADEPTAHLDFIQVEEVLRLIRELAD 191
Cdd:cd03270 108 LFARVGIRERlgflvdvglgyltLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRD 187
|
90 100
....*....|....*....|....*.
gi 15607215 192 GERVVVVATHDSRMLPMADRVVELTP 217
Cdd:cd03270 188 LGNTVLVVEHDEDTIRAADHVIDIGP 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-202 |
4.56e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 38 LLGPSGCGKTTLLSCLGGILRPKSGAIKFDevdiTTLQGAELANYRRnkvgivfqafNLVPSLTAVEN-------VMV-- 108
Cdd:PRK11147 350 LIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFDQHRA----------ELDPEKTVMDNlaegkqeVMVng 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 109 ---------------PLRsagmsrrasrrraeellARVNLAErmnhrpgdLSGGQQQRVAVARaIALDPP-LILADEPTA 172
Cdd:PRK11147 416 rprhvlgylqdflfhPKR-----------------AMTPVKA--------LSGGERNRLLLAR-LFLKPSnLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|.
gi 15607215 173 HLDFiqveEVLRLIREL-ADGERVVVVATHD 202
Cdd:PRK11147 470 DLDV----ETLELLEELlDSYQGTVLLVSHD 496
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
143-222 |
4.91e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 143 DLSGGQQQRVAVARAIALDPPLILADEPTAHLDfIQVEEvlRLIRELADGE---RVVVVATHDSRMLPMADRVVEL---- 215
Cdd:PTZ00243 782 NLSGGQKARVSLARAVYANRDVYLLDDPLSALD-AHVGE--RVVEECFLGAlagKTRVLATHQVHVVPRADYVVALgdgr 858
|
90
....*....|...
gi 15607215 216 ------TPDFAET 222
Cdd:PTZ00243 859 vefsgsSADFMRT 871
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-201 |
5.07e-06 |
|
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: 48.47 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 8 NLVVEYYSGGYAlRPINGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGaikfdevDITTLQGAELANyrrnkV 87
Cdd:TIGR01257 1941 NELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-------DATVAGKSILTN-----I 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 88 GIVFQAFNLVPS-------LTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIAL 160
Cdd:TIGR01257 2008 SDVHQNMGYCPQfdaiddlLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15607215 161 DPPLILADEPTAHLDfIQVEEVL-----RLIREladgERVVVVATH 201
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMD-PQARRMLwntivSIIRE----GRAVVLTSH 2128
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
141-224 |
5.51e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 141 PGDLSGGQQQ------RVAVARAIALD-------PPLILaDEPTAHLDFIQVEEVLRLIRELAD-GERVVVVATHDSRML 206
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEGiegdaplPPLIL-DEPTVFLDSGHVSQLVDLVESMRRlGVEQIVVVSHDDELV 857
|
90
....*....|....*...
gi 15607215 207 PMADRVVELTPDfAETNR 224
Cdd:PRK02224 858 GAADDLVRVEKD-PTTNR 874
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
144-217 |
5.57e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 5.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 144 LSGGQQQRVAVARAIAL---DP-PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVaTHDSRMLPMADRVVELTP 217
Cdd:pfam02463 1078 LSGGEKTLVALALIFAIqkyKPaPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVI-SLREEMLEKADKLVGVTM 1154
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-206 |
6.23e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 127 LLARVNLAERMNHRPGD-LSGGQQQRVAVARAIALDPPLILADEPTAHLDfiqVEEVLRLIRELADGERVVVVATHDSRM 205
Cdd:PLN03073 327 ILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREF 403
|
.
gi 15607215 206 L 206
Cdd:PLN03073 404 L 404
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-218 |
8.17e-06 |
|
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: 46.45 E-value: 8.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 144 LSGGQQQRVAVARAI---ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVELTPD 218
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPE 247
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
144-201 |
8.21e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 8.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 144 LSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGE-RVVVVATH 201
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnRITIIIAH 638
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-224 |
9.72e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.92 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 21 RPINGLNLDVAAGsLVMLLGPSGCGKTTLLSCLGGILRPKSGaIKFDEVD---------------------ITTLQGAEL 79
Cdd:COG3593 12 RSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSS-RKFDEEDfylgddpdlpeieieltfgslLSRLLRLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 80 ANYRRNKVGIVFQAFN--LVPSLTAVENV-------MVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQ 150
Cdd:COG3593 90 KEEDKEELEEALEELNeeLKEALKALNELlseylkeLLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLDRLGSGFQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 151 RV--AVARAIAL-----DPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMAD----RVVELTPDF 219
Cdd:COG3593 170 LIllALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPleniRRLRRDSGG 249
|
....*
gi 15607215 220 AETNR 224
Cdd:COG3593 250 TTSTK 254
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-232 |
1.09e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.06 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSggyALRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELa 80
Cdd:cd03288 18 GEIKIHDLCVRYEN---NLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNKVGIVFQ---------AFNLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERmnhrpgDLSGGQQQR 151
Cdd:cd03288 94 ---RSRLSIILQdpilfsgsiRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGE------NFSVGQRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 152 VAVARAIALDPPLILADEPTAHLDfIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVELTPDFAETNRPPETVHL 231
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
.
gi 15607215 232 Q 232
Cdd:cd03288 244 Q 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-213 |
1.37e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 142 GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGER-VVVVATHDSRMLPMADRVV 213
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMPELLGITDRIL 462
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-201 |
1.42e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 30 VAAGSLVMLLGPSGCGKTTLLSCLGGilRPKSGAIkfdEVDITTLQGAELANYRRNKVGIVFQAFNLVPSLTAVENvmvp 109
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVI---TGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRES---- 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 110 LR-SAGMsrrasrrraeELLARVNLAERMNH-------------------RPGD-LSGGQQQRVAVARAIALDPPLIL-A 167
Cdd:TIGR00956 857 LRfSAYL----------RQPKSVSKSEKMEYveevikllemesyadavvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|....
gi 15607215 168 DEPTAHLDFIQVEEVLRLIRELADGERVVVVATH 201
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
144-213 |
1.81e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 44.61 E-value: 1.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607215 144 LSGGQQQRVAVARAIAL---DP-PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVV 213
Cdd:cd03239 95 LSGGEKSLSALALIFALqeiKPsPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLI 168
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-218 |
2.15e-05 |
|
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: 46.16 E-value: 2.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607215 144 LSGGQQQRVAVARAI---ALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVELTPD 218
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPE 907
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-215 |
2.53e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 33 GSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDE-------------VDITTLQ------------GAEL--ANYRRN 85
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpaLPQPALEyvidgdreyrqlEAQLhdANERND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 86 KVGIVfqafNLVPSLTAVENVMVPLRSAGmsrrasrrraeeLLARVNLAERMNHRP-GDLSGGQQQRVAVARAIALDPPL 164
Cdd:PRK10636 107 GHAIA----TIHGKLDAIDAWTIRSRAAS------------LLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15607215 165 ILADEPTAHLDfiqVEEVLRLIRELADGERVVVVATHDSRML-PMADRVVEL 215
Cdd:PRK10636 171 LLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLdPIVDKIIHI 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
8-202 |
2.71e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 8 NLVVEYYSggyalRPI-NGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGG----------IL---RPKSGAIKFDevdItt 73
Cdd:PRK10938 265 NGVVSYND-----RPIlHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndlTLfgrRRGSGETIWD---I-- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 74 lqgaelanyrRNKVGIVFQAFNL---VPslTAVENVMVP--LRSAGM---SRRASRRRAEELLARVNLAERMNHRP-GDL 144
Cdd:PRK10938 335 ----------KKHIGYVSSSLHLdyrVS--TSVRNVILSgfFDSIGIyqaVSDRQQKLAQQWLDILGIDKRTADAPfHSL 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 145 SGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIREL-ADGE-RVVVVATHD 202
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEGEtQLLFVSHHA 462
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
36-73 |
2.80e-05 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 43.25 E-value: 2.80e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15607215 36 VMLLGPSGCGKTTLLSCLGGILRP--KSGAIKFDEVDITT 73
Cdd:COG4917 4 IMLIGRSGAGKTTLTQALNGEELEyrKTQAVEYYDNIIDT 43
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-176 |
4.87e-05 |
|
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: 45.32 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYYSG-GYALRPINglnLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAELa 80
Cdd:TIGR00957 1283 GRVEFRNYCLRYREDlDLVLRHIN---VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL- 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 81 nyrRNKVGIVFQ---------AFNLVP-SLTAVENVMVPLRSAGMSRRASRrraeellarvnLAERMNHRPGD----LSG 146
Cdd:TIGR00957 1359 ---RFKITIIPQdpvlfsgslRMNLDPfSQYSDEEVWWALELAHLKTFVSA-----------LPDKLDHECAEggenLSV 1424
|
170 180 190
....*....|....*....|....*....|
gi 15607215 147 GQQQRVAVARAIALDPPLILADEPTAHLDF 176
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
144-211 |
1.63e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. 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: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.07 E-value: 1.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607215 144 LSGGQQQRVAVARAIAL---DP-PLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVaTHDSRMLPMADR 211
Cdd:cd03278 114 LSGGEKALTALALLFAIfrvRPsPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVI-THRKGTMEAADR 184
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-217 |
2.08e-04 |
|
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: 43.08 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 142 GDLSGGQQQRVAVARAI--ALDPPLILADEPTAHL---DFIQVEEVLRLIRELadGERVVVVAtHDSRMLPMADRVVELT 216
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLhqrDNRRLINTLKRLRDL--GNTLIVVE-HDEDTIRAADYVIDIG 563
|
.
gi 15607215 217 P 217
Cdd:TIGR00630 564 P 564
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-188 |
2.22e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 2 GDLSIQNLVVEYysggyalRP-----INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQG 76
Cdd:PLN03130 1236 GSIKFEDVVLRY-------RPelppvLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 77 AELanyrRNKVGIVFQA---------FNLVPsltAVENVMVPLRSAgmsrrasrrraeelLARVNLAE--RMNHRPGD-- 143
Cdd:PLN03130 1309 MDL----RKVLGIIPQApvlfsgtvrFNLDP---FNEHNDADLWES--------------LERAHLKDviRRNSLGLDae 1367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 144 -------LSGGQQQRVAVARAIALDPPLILADEPTAHLD-----FIQveevlRLIRE 188
Cdd:PLN03130 1368 vseagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtdaLIQ-----KTIRE 1419
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
142-212 |
2.89e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 2.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15607215 142 GDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIRELAD-GERVVVVATHDSRMLPMADRV 212
Cdd:NF040905 403 GNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVISSELPELLGMCDRI 474
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-171 |
3.39e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.43 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGiLRPksgaikfdevdittLQGAELANYRRNKVGIVFQAfnlvPSL-- 100
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWP--------------VYGGRLTKPAKGKLFYVPQR----PYMtl 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 101 -TAVENVMVPLRSAGMSRRASR-RRAEELLARVNLAERMNHRPG---------DLSGGQQQRVAVARAIALDPPLILADE 169
Cdd:TIGR00954 529 gTLRDQIIYPDSSEDMKRRGLSdKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
..
gi 15607215 170 PT 171
Cdd:TIGR00954 609 CT 610
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-218 |
3.77e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 140 RP-GDLSGGQQQRVAVAR---AIALDPPLILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRMLPMADRVVEL 215
Cdd:PRK00635 805 RPlSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
...
gi 15607215 216 TPD 218
Cdd:PRK00635 885 GPE 887
|
|
| EutP |
TIGR02528 |
ethanolamine utilization protein, EutP; This protein is found within operons which code for ... |
36-73 |
7.28e-04 |
|
ethanolamine utilization protein, EutP; This protein is found within operons which code for polyhedral organelles containing the enzyme ethanolamine ammonia lyase. The function of this gene is unknown, although the presence of an N-terminal GxxGxGK motif implies a GTP-binding site. [Energy metabolism, Amino acids and amines]
Pssm-ID: 131580 [Multi-domain] Cd Length: 142 Bit Score: 39.35 E-value: 7.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15607215 36 VMLLGPSGCGKTTLLSCLGG--ILRPKSGAIKFDEVDITT 73
Cdd:TIGR02528 3 IMFIGSVGCGKTTLTQALQGeeILYKKTQAVEYNDGAIDT 42
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
141-206 |
7.99e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 7.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 141 PGDLSGGQQQRVAVARAIALDPP---LILADEPTAHLDFIQVEEVLRLIRELADGERVVVVATHDSRML 206
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLL 302
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-216 |
8.51e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 8.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607215 144 LSGGQQQRVAVARAIALD----PPLILADEPTAHLDFIQVEEVLRLIRELAdGERVVVVATHDSRMLPMADRVVELT 216
Cdd:TIGR02169 1075 MSGGEKSLTALSFIFAIQrykpSPFYAFDEVDMFLDGVNVERVAKLIREKA-GEAQFIVVSLRSPMIEYADRAIGVT 1150
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
144-212 |
9.26e-04 |
|
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: 40.32 E-value: 9.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607215 144 LSGGQQQRVAVARAIAL---DP-PLILADEPTAHLDFIQVEEVLRLIRELADGERvVVVATHDSRMLPMADRV 212
Cdd:cd03272 159 LSGGQKSLVALALIFAIqkcDPaPFYLFDEIDAALDAQYRTAVANMIKELSDGAQ-FITTTFRPELLEVADKF 230
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-201 |
1.54e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.10 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 20 LRPINGLNLDVAAGSLVMLLGPSGCG--KTTLLSCLGGilrPKSGAIKFDEVDITTLQGA---ELANYRRNKVGivfqaf 94
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRAlrrTIG*HRPVR*G------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 95 nLVPSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHL 174
Cdd:NF000106 97 -RRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180
....*....|....*....|....*...
gi 15607215 175 DFIQVEEVLRLIRELA-DGERVVVVATH 201
Cdd:NF000106 176 DPRTRNEVWDEVRSMVrDGATVLLTTQY 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-204 |
1.67e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 18 YALrpiNGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKfdevdittlqgaelanyRRNKVGIVFQAFNLV 97
Cdd:PRK13546 38 FAL---DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 98 PSLTAVENVMVPLRSAGMSRRASRRRAEELLARVNLAERMNHRPGDLSGGQQQRVAVARAIALDPPLILADEPTAHLDFI 177
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*..
gi 15607215 178 QVEEVLRLIRELADGERVVVVATHDSR 204
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLG 204
|
|
| PduV-EutP |
pfam10662 |
Ethanolamine utilization - propanediol utilization; Members of this family function in ... |
36-73 |
1.77e-03 |
|
Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.
Pssm-ID: 402341 [Multi-domain] Cd Length: 137 Bit Score: 38.03 E-value: 1.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15607215 36 VMLLGPSGCGKTTLLSCLGG--ILRPKSGAIKFDEVDITT 73
Cdd:pfam10662 4 IMLIGPTGCGKTTLCQALSGeeLKYKKTQAIEFYDNAIDT 43
|
|
| PRK11753 |
PRK11753 |
cAMP-activated global transcriptional regulator CRP; |
246-298 |
1.92e-03 |
|
cAMP-activated global transcriptional regulator CRP;
Pssm-ID: 236969 [Multi-domain] Cd Length: 211 Bit Score: 38.81 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15607215 246 LIYVVSeGEFEIVHELADGGEELVKVAGPGDYFGEIGvLFH--LPRSATVRARSD 298
Cdd:PRK11753 41 LYYIVK-GSVAVLIKDEEGKEMILSYLNQGDFIGELG-LFEegQERSAWVRAKTA 93
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-212 |
2.24e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 23 INGLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEvditTLqgaelanyrrnKVGIVFQAF-NLVPSLT 101
Cdd:PRK11819 340 IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE----TV-----------KLAYVDQSRdALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 102 AVENVmvplrSAGmsrrasrrraeelLARVNLAER-MNHRP----------------GDLSGGQQQRVAVARAIALDPPL 164
Cdd:PRK11819 405 VWEEI-----SGG-------------LDIIKVGNReIPSRAyvgrfnfkggdqqkkvGVLSGGERNRLHLAKTLKQGGNV 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15607215 165 ILADEPTAHLDFiqveEVLRLIRE-LADGERVVVVATHDSRMLpmaDRV 212
Cdd:PRK11819 467 LLLDEPTNDLDV----ETLRALEEaLLEFPGCAVVISHDRWFL---DRI 508
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
240-297 |
3.38e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 39.08 E-value: 3.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15607215 240 QSTMGDLIYVVSEGEFEIVheLADGGEELVKVA-GPGDYFGEIGVLFHLPRSATVRARS 297
Cdd:PLN03192 411 QNEAPDDVYIVVSGEVEII--DSEGEKERVVGTlGCGDIFGEVGALCCRPQSFTFRTKT 467
|
|
| PRK09862 |
PRK09862 |
ATP-dependent protease; |
25-78 |
6.53e-03 |
|
ATP-dependent protease;
Pssm-ID: 182120 [Multi-domain] Cd Length: 506 Bit Score: 38.04 E-value: 6.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15607215 25 GLNLDVAAGSLVMLLGPSGCGKTTLLSCLGGILRPKSGAIKFDEVDITTLQGAE 78
Cdd:PRK09862 202 GLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNEEALESAAILSLVNAE 255
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
144-215 |
6.74e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607215 144 LSGGQQQ------RVAVARAIALDPPLILADEPTAHLDFIQVEEVLRLIR-ELADGERV--VVVATHDSRMLPMADRVVE 214
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDIpqVIMISHHRELLSVADVAYE 881
|
.
gi 15607215 215 L 215
Cdd:PRK01156 882 V 882
|
|
| |
