|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-262 |
7.63e-137 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 385.60 E-value: 7.63e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA 80
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQNHSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVL 160
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLEL---RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 161 LLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPaATVGEILAVDLPRPRHRvQLADD 240
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARP-GRIVEEIDVDLPRPRDR-ELRTS 238
|
250 260
....*....|....*....|..
gi 556285678 241 SRYHHLRQQILHFLYEKQPKAA 262
Cdd:COG1116 239 PEFAALRAEILDLLREEAERAA 260
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-254 |
2.93e-120 |
|
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: 342.52 E-value: 2.93e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQNHSLLPWLSCFDNVALAVD 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 104 QVfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMH 183
Cdd:TIGR01184 81 RV-LPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 184 IQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVDLPRPRHRVQLADDSRYHHLRQQILHFL 254
Cdd:TIGR01184 160 IWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPFPRPRDRLEVVEDPSYYDLRNEALYFL 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-228 |
1.08e-106 |
|
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: 307.86 E-value: 1.08e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQ 84
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 85 NHSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:cd03293 81 QDALLPWLTVLDNVALGLEL---QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 165 PFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPaATVGEILAVDL 228
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARP-GRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-262 |
1.88e-86 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 257.87 E-value: 1.88e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVV 82
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 83 FQNHSLLPWLSCFDNVALAvdqvFR-RTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLL 161
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFG----LRlRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 162 LDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPaatvGEILAV-DLPRPRHRVQLAD- 239
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGP----GRIVERlELDFSRRFLAGEDa 233
|
250 260
....*....|....*....|....*...
gi 556285678 240 -----DSRYHHLRQQILHFLYEKQPKAA 262
Cdd:COG4525 234 raiksDPAFIALREELLDIIFAQEEAEA 261
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-234 |
1.01e-81 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 249.24 E-value: 1.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER- 79
Cdd:COG3842 2 AMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --AVVFQNHSLLPWLSCFDNVAlavdqvF---RRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:COG3842 78 nvGMVFQDYALFPHLTVAENVA------FglrMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNgpaatvGEILAVDLP----- 229
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND------GRIEQVGTPeeiye 225
|
....*
gi 556285678 230 RPRHR 234
Cdd:COG3842 226 RPATR 230
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
5-254 |
3.04e-75 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 229.24 E-value: 3.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQ 84
Cdd:NF040729 2 LKIQNISKTFINNKKENEVLKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEILVNGNEVTKPGPDRGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 85 NHSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:NF040729 82 NYALFPWMTVKENIEYPMKQ---QKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 165 PFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGpAATVGEILAVDLPRPRHRvqlaDDSRYH 244
Cdd:NF040729 159 PLGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRD-KGKILEDLKIDLPRPRNR----ESEKYL 233
|
250
....*....|
gi 556285678 245 HLRQQILHFL 254
Cdd:NF040729 234 EYKDHLTNIL 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-221 |
1.02e-73 |
|
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: 223.94 E-value: 1.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---AV 81
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 VFQNHSLLPWLSCFDNVALAVDqvfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLL 161
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLK---LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 162 LDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
4.03e-73 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 223.00 E-value: 4.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPER 79
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 A--------VVFQNHSLLPWLSCFDNVALAvdQVFRRtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIAR 151
Cdd:COG1136 81 ArlrrrhigFVFQFFNLLPELTALENVALP--LLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDvDEAVLLSDRVLMMTNG 215
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDG 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-230 |
1.06e-71 |
|
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: 219.42 E-value: 1.06e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERAV-- 81
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRPVnt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 VFQNHSLLPWLSCFDNVALAVDqvfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLL 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLR---LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 162 LDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNgpaatvGEILAVDLPR 230
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK------GKIQQIGTPE 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-215 |
1.06e-69 |
|
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: 213.89 E-value: 1.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 ----AVVFQNHSLLPWLSCFDNVALAvdQVFRRTmSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAM 155
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELP--LLLAGV-PKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 156 KPKVLLLDEPFGALDALTRahlqDTVMHIQQELN----TTIVMITHDvDEAVLLSDRVLMMTNG 215
Cdd:cd03255 158 DPKIILADEPTGNLDSETG----KEVMELLRELNkeagTTIVVVTHD-PELAEYADRIIELRDG 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-230 |
1.01e-68 |
|
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: 212.15 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER- 79
Cdd:COG1127 2 SEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 -------AVVFQNHSLLPWLSCFDNVALAVDQvfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARA 152
Cdd:COG1127 78 yelrrriGMLFQGGALFDSLTVFENVAFPLRE--HTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 153 LAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG---PAATVGEILAVDLP 229
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGkiiAEGTPEELLASDDP 235
|
.
gi 556285678 230 R 230
Cdd:COG1127 236 W 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-233 |
3.05e-67 |
|
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: 216.69 E-value: 3.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFNT-ASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER- 79
Cdd:COG1123 258 EPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSl 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 -------AVVFQN--HSLLPWLSCFDNVALAVDqvFRRTMSKHERREWIEHNLARVQMS-HALHKRPGEISGGMKQRVGI 149
Cdd:COG1123 338 relrrrvQMVFQDpySSLNPRMTVGDIIAEPLR--LHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 150 ARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVdLP 229
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV-FA 494
|
....
gi 556285678 230 RPRH 233
Cdd:COG1123 495 NPQH 498
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-222 |
7.94e-66 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 208.08 E-value: 7.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNRE--IAGPGPERAV- 81
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlfTNLPPRERRVg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 -VFQNHSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVL 160
Cdd:COG1118 79 fVFQHYALFPHMTVAENIAFGLRV---RPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 161 LLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGE 222
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-230 |
2.46e-64 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 201.47 E-value: 2.46e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQNHSLLPWLSCFDNVALAV 102
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 DQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVM 182
Cdd:PRK11248 96 QL---AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 183 HIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVgEILAVDLPR 230
Cdd:PRK11248 173 KLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV-ERLPLNFAR 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-233 |
5.92e-64 |
|
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: 199.65 E-value: 5.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 ---AVVFQNHSLLPWLSCFDNVALAVDQvfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMK 156
Cdd:cd03261 77 rrmGMLFQSGALFDSLTVFENVAFPLRE--HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 157 PKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGP---AATVGEILAVDLPRPRH 233
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKivaEGTPEELRASDDPLVRQ 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-234 |
1.66e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 202.23 E-value: 1.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---AV 81
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrniAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 VFQNHSLLPWLSCFDNVAlavdqvF---RRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPK 158
Cdd:COG3839 80 VFQSYALYPHMTVYENIA------FplkLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 159 VLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNgpaatvGEILAVDLP-----RPRH 233
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND------GRIQQVGTPeelydRPAN 227
|
.
gi 556285678 234 R 234
Cdd:COG3839 228 L 228
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-221 |
9.10e-63 |
|
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: 200.65 E-value: 9.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTasgeFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER- 79
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --AVVFQNHSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:TIGR03265 77 dyGIVFQSYALFPNLTVADNIAYGLKN---RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:TIGR03265 154 GLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-225 |
1.33e-62 |
|
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: 197.48 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 16 TASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---------AVVFQNH 86
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 87 SLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPF 166
Cdd:cd03294 112 ALLPHRTVLENVAFGLEV---QGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 167 GALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG---EILA 225
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGtpeEILT 250
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
5-225 |
8.97e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 196.46 E-value: 8.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNtasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE---RAV 81
Cdd:COG1125 2 IEFENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 --VFQNHSLLPWLSCFDNVALavdqVFR-RTMSKHERREWIEHNLARVQMSHA--LHKRPGEISGGMKQRVGIARALAMK 156
Cdd:COG1125 79 gyVIQQIGLFPHMTVAENIAT----VPRlLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 157 PKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG---EILA 225
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDtpeEILA 226
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-215 |
1.22e-61 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 198.79 E-value: 1.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 17 ASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---------AVVFQNHS 87
Cdd:COG4175 36 KTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElrelrrkkmSMVFQHFA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 88 LLPWLSCFDNVA--LAVdqvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEP 165
Cdd:COG4175 116 LLPHRTVLENVAfgLEI-----QGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556285678 166 FGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG4175 191 FSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDG 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-225 |
2.82e-61 |
|
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: 193.29 E-value: 2.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNtasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:cd03295 1 IEFENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNHSLLPWLSCFDNVALaVDQVFRrtMSKHERREWIEHNLARVQM--SHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIAL-VPKLLK--WPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG---EILA 225
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGtpdEILR 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-221 |
5.22e-60 |
|
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: 189.86 E-value: 5.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP-ERAV-- 81
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqERNVgf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 VFQNHSLLPWLSCFDNVA--LAVDQVFRRTmSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKV 159
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAfgLRVKPRSERP-PEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 160 LLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-215 |
2.27e-59 |
|
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: 186.24 E-value: 2.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --AVVFQNHSLLPWLSCFDNVALAvdqvfrrtmskherrewiehnlarvqmshalhkrpgeISGGMKQRVGIARALAMKP 157
Cdd:cd03229 77 riGMVFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-215 |
6.19e-59 |
|
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: 186.56 E-value: 6.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---- 79
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 ----AVVFQN--HSLLPWLSCFDNVALAVdqVFRRTMSKHERREWIEHNLAR-VQMSHA-LHKRPGEISGGMKQRVGIAR 151
Cdd:cd03257 81 rkeiQMVFQDpmSSLNPRMTIGEQIAEPL--RIHGKLSKKEARKEAVLLLLVgVGLPEEvLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-221 |
2.03e-57 |
|
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: 182.45 E-value: 2.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP-ER--AV 81
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkDRdiAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 VFQNHSLLPWLSCFDNVALAVDqvfrrtmSKHERREWIE---HNLARV-QMSHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLK-------LRKVPKDEIDervREVAELlQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-238 |
1.01e-56 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 182.18 E-value: 1.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIqVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVV 82
Cdd:PRK11247 12 PLL-LNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 83 FQNHSLLPWLSCFDNVALAVdqvfrrtmsKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLL 162
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL---------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 163 DEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGpaaTVGEILAVDLPRPRHR--VQLA 238
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG---KIGLDLTVDLPRPRRRgsARLA 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-230 |
5.35e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.49 E-value: 5.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE-RA--- 80
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRRrig 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQNHSLLPWLSCFDNVALavdqvFRRT--MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPK 158
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRF-----FARLygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 159 VLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNgpaatvGEILAVDLPR 230
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDK------GRIVADGTPD 216
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-221 |
1.26e-55 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 182.84 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFNTASgeflALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE-RA 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 V--VFQNHSLLPWLSCFDNVAlavdqvFRRTMSK---HERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAM 155
Cdd:PRK09452 88 VntVFQSYALFPHMTVFENVA------FGLRMQKtpaAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 156 KPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-215 |
1.63e-55 |
|
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: 177.91 E-value: 1.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNtasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA---- 80
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 -VVFQNhsllPWlscfdnvalavDQVFRRT-------------MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQR 146
Cdd:COG1122 78 gLVFQN----PD-----------DQLFAPTveedvafgpenlgLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 147 VGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-226 |
4.14e-54 |
|
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: 174.83 E-value: 4.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFlALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---AVVFQNHSLLPWLSCF 95
Cdd:cd03299 11 KEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVALAVDqvfRRTMSKHERREWIeHNLARV-QMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTR 174
Cdd:cd03299 90 KNIAYGLK---KRKVDKKEIERKV-LEIAEMlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556285678 175 AHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAV 226
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-215 |
2.42e-53 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 172.16 E-value: 2.42e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntaSGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERA--- 80
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ----VVFQNHSLLPWLSCFDNVALAVdQVfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMK 156
Cdd:COG2884 79 rrigVVFQDFRLLPDRTVYENVALPL-RV--TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 157 PKVLLLDEPFGALDALTRAHlqdtVMHIQQELN---TTIVMITHDVDeavLLSD---RVLMMTNG 215
Cdd:COG2884 156 PELLLADEPTGNLDPETSWE----IMELLEEINrrgTTVLIATHDLE---LVDRmpkRVLELEDG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-234 |
8.62e-53 |
|
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: 171.52 E-value: 8.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---- 79
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 -AVVFQNhsllPWLSCfdNVALAVDQVFR---RTMSKHERREWIEHNLARVQMSHA-LHKRPGEISGGMKQRVGIARALA 154
Cdd:COG1124 81 vQMVFQD----PYASL--HPRHTVDRILAeplRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAAtvgEILAVDLPRPRHR 234
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV---EELTVADLLAGPK 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-215 |
1.52e-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: 1.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 6 QVQAVSQRFNtaSGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----A 80
Cdd:cd03225 1 ELKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQN--HSLLPwLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPK 158
Cdd:cd03225 79 LVFQNpdDQFFG-PTVEEEVAFGLEN---LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 159 VLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-215 |
2.57e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 170.17 E-value: 2.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA--- 80
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINklr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ----VVFQNHSLLPWLSCFDNVALAVDQVfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMK 156
Cdd:COG1126 77 rkvgMVFQQFNLFPHLTVLENVTLAPIKV--KKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 157 PKVLLLDEPFGALD-ALTRAHLQdtVMhiqQEL---NTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG1126 155 PKVMLFDEPTSALDpELVGEVLD--VM---RDLakeGMTMVVVTHEMGFAREVADRVVFMDGG 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-225 |
2.68e-52 |
|
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: 2.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPER--- 79
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 ----AVVFQNHSLLPWLSCFDNVALAVdQVFRrtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAM 155
Cdd:cd03258 81 rrriGMIFQHFNLLSSRTVFENVALPL-EIAG--VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 156 KPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAA---TVGEILA 225
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVeegTVEEVFA 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-229 |
5.15e-52 |
|
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: 169.83 E-value: 5.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA 80
Cdd:COG0411 1 SDPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 V------VFQNHSLLPWLSCFDNVALAVDQVFRRTM------------SKHERREWIEHNLARVQMSHALHKRPGEISGG 142
Cdd:COG0411 77 ArlgiarTFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 143 MKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDeAVL-LSDRVLMMTNgpaatvG 221
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMD-LVMgLADRIVVLDF------G 229
|
....*...
gi 556285678 222 EILAVDLP 229
Cdd:COG0411 230 RVIAEGTP 237
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-221 |
5.82e-52 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 169.21 E-value: 5.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---AV 81
Cdd:TIGR00968 1 IEIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDrkiGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 VFQNHSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLL 161
Cdd:TIGR00968 77 VFQHYALFKHLTVRDNIAFGLEI---RKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 162 LDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:TIGR00968 154 LDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-215 |
5.85e-52 |
|
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: 168.48 E-value: 5.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE----R- 79
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelRq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --AVVFQNHSLLPWLSCFDNVALAvdQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:cd03262 77 kvGMVFQQFNLFPHLTVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.54e-51 |
|
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: 175.48 E-value: 1.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPT---EGGLLCDNREIAGP-- 75
Cdd:COG1123 1 MTPLLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELse 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 76 ---GPERAVVFQN--HSLLPwLSCFDNVALAVDqvfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIA 150
Cdd:COG1123 79 alrGRRIGMVFQDpmTQLNP-VTVGDQIAEALE---NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 151 RALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG---PAATVGEILA 225
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGrivEDGPPEEILA 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-215 |
4.89e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 167.16 E-value: 4.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNtasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER--- 79
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 -----AVVFQNHSLLPWLSCFDNV---ALA---VDQVFRRTMSKHERREWIEHnLARVQMSHALHKRPGEISGGMKQRVG 148
Cdd:COG3638 78 lrrriGMIFQQFNLVPRLSVLTNVlagRLGrtsTWRSLLGLFPPEDRERALEA-LERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 149 IARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-166 |
2.61e-50 |
|
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: 162.05 E-value: 2.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVVFQNHSLLPWLSCFDNV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 99 ALAVDqvfRRTMSKHERREWIEHNLARVQMSHALHKR----PGEISGGMKQRVGIARALAMKPKVLLLDEPF 166
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-215 |
3.87e-50 |
|
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: 164.53 E-value: 3.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV--- 81
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 ---VFQNHSLLPWLSCFDNVALAVDQ-------VFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIAR 151
Cdd:cd03219 77 igrTFQIPRLFPELTVLENVMVAAQArtgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDeAVL-LSDRVLMMTNG 215
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMD-VVMsLADRVTVLDQG 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-229 |
5.44e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 163.77 E-value: 5.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 28 SFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP-ER--AVVFQNHSLLPWLSCFDNVALAVDQ 104
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPaERpvSMLFQENNLFPHLTVAQNIGLGLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 105 VFRRTMSKHERrewIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHI 184
Cdd:COG3840 99 GLKLTAEQRAQ---VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDEL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 185 QQELNTTIVMITHDVDEAVLLSDRVLMMTNG---PAATVGEILAVDLP 229
Cdd:COG3840 176 CRERGLTVLMVTHDPEDAARIADRVLLVADGriaADGPTAALLDGEPP 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-235 |
6.73e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 166.79 E-value: 6.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPE-RAV- 81
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERElRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 -----VFQNHSLLPWLSCFDNVALAvdqvFRRT-MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAM 155
Cdd:COG1135 82 rkigmIFQHFNLLSSRTVAENVALP----LEIAgVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 156 KPKVLLLDEPFGALDALTRAH----LQDtvmhIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVdLPRP 231
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSildlLKD----INRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV-FANP 232
|
....
gi 556285678 232 RHRV 235
Cdd:COG1135 233 QSEL 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-233 |
8.33e-49 |
|
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: 163.69 E-value: 8.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTP---TEGGLLCDNREIAGPGPER- 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --------AVVFQN--HSLLPWLSCFDNVALAVdqVFRRTMSKHERREWIEHNLARVQMSHA---LHKRPGEISGGMKQR 146
Cdd:COG0444 81 rkirgreiQMIFQDpmTSLNPVMTVGDQIAEPL--RIHGGLSKAEARERAIELLERVGLPDPerrLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 147 VGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG---PAATVGEI 223
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGrivEEGPVEEL 238
|
250
....*....|
gi 556285678 224 LAvdlpRPRH 233
Cdd:COG0444 239 FE----NPRH 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-215 |
1.04e-48 |
|
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: 160.68 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE-RA- 80
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDaRAr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 -------VVFQNHSLLPWLSCFDNVAL-----AVDQVFRRTmskherREWiehnLARVQMSHALHKRPGEISGGMKQRVG 148
Cdd:COG4181 87 lrarhvgFVFQSFQLLPTLTALENVMLplelaGRRDARARA------RAL----LERVGLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 149 IARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAvLLSDRVLMMTNG 215
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAG 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-222 |
1.35e-47 |
|
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: 160.74 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 39 LIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---AVVFQNHSLLPWLSCFDNVALAVDQvfrRTMSKHER 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKM---RKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 116 REWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMI 195
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170 180
....*....|....*....|....*..
gi 556285678 196 THDVDEAVLLSDRVLMMTNGPAATVGE 222
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-233 |
2.09e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 160.74 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA---GPGPERA- 80
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ----VVFQNHSLLPWLSCFDNVALAVDQVfrrTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMK 156
Cdd:PRK11153 82 rqigMIFQHFNLLSSRTVFDNVALPLELA---GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 157 PKVLLLDEPFGALD-ALTRAHLqDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAA---TVGEILAvdlpRPR 232
Cdd:PRK11153 159 PKVLLCDEATSALDpATTRSIL-ELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVeqgTVSEVFS----HPK 233
|
.
gi 556285678 233 H 233
Cdd:PRK11153 234 H 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
24-215 |
3.95e-47 |
|
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: 157.13 E-value: 3.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERA----VVFQNHSLLPWLSCFDNV 98
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELArriaYVPQEPPAPFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 99 ALAvdqvfR-------RTMSKHERREwIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDA 171
Cdd:COG1120 97 ALG-----RyphlglfGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556285678 172 LTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDG 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-215 |
4.54e-47 |
|
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: 154.48 E-value: 4.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----A 80
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQNHSLLPWLSCFDNVALavdqvfrrtmskherrewiehnlarvqmshalhkrpgeiSGGMKQRVGIARALAMKPKVL 160
Cdd:cd03230 77 YLPEEPSLYENLTVRENLKL---------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 161 LLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-230 |
9.19e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 156.82 E-value: 9.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSqrFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDN------------REI 72
Cdd:TIGR04520 1 IEVENVS--FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeenlweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 73 AGpgperaVVFQNhsllPwlscfDN--VALAV--DQVF---RRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQ 145
Cdd:TIGR04520 79 VG------MVFQN----P-----DNqfVGATVedDVAFgleNLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 146 RVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVlLSDRVLMMTNgpaatvGEILA 225
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNK------GKIVA 216
|
....*
gi 556285678 226 VDLPR 230
Cdd:TIGR04520 217 EGTPR 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-221 |
1.01e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 159.09 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERAV-- 81
Cdd:PRK10851 3 IEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARDRKVgf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 VFQNHSLLPWLSCFDNVALAVDQVFRRTM-SKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVL 160
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLPRRERpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 161 LLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-222 |
1.24e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 159.62 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNtasGEFlALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP-ERAV 81
Cdd:PRK11607 18 PLLEIRNLTKSFD---GQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPyQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 --VFQNHSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKV 159
Cdd:PRK11607 94 nmMFQSYALFPHMTVEQNIAFGLKQ---DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 160 LLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGE 222
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
1.50e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.63 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA 80
Cdd:COG1121 3 MMPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQNHSL---LPwLSCFDNVALAVDQ---VFRRtmSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:COG1121 79 YVPQRAEVdwdFP-ITVRDVVLMGRYGrrgLFRR--PSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNGPAA--TVGEIL 224
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAhgPPEEVL 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-215 |
3.54e-46 |
|
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: 153.60 E-value: 3.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 26 NVSFDIvEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNR-------EIAGPGPERAV--VFQNHSLLPWLSCFD 96
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkKINLPPQQRKIglVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 97 NVALAVdqvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAH 176
Cdd:cd03297 95 NLAFGL-----KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 556285678 177 LQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-212 |
6.13e-46 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 156.43 E-value: 6.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASGEFL-------ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA 73
Cdd:COG4608 4 AEPLLEVRDLKKHFPVRGGLFGrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 74 GPGPERA--------VVFQN--HSLLPWLSCFDNVALAVDqvFRRTMSKHERREWIEHNLARVQM--SHAlHKRPGEISG 141
Cdd:COG4608 84 GLSGRELrplrrrmqMVFQDpyASLNPRMTVGDIIAEPLR--IHGLASKAERRERVAELLELVGLrpEHA-DRYPHEFSG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 142 GMKQRVGIARALAMKPKVLLLDEPFGALDALTRAH----LQDtvmhIQQELNTTIVMITHDVdeAVL--LSDRVLMM 212
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQvlnlLED----LQDELGLTYLFISHDL--SVVrhISDRVAVM 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-221 |
8.72e-45 |
|
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: 149.95 E-value: 8.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 25 QNVSFD--IVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI-AGPGPERAV--VFQNHSLLPWLSCFDNVA 99
Cdd:cd03298 13 QPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtAAPPADRPVsmLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 100 LAVDQVFRRTmskHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQD 179
Cdd:cd03298 93 LGLSPGLKLT---AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556285678 180 TVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-215 |
8.89e-45 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 154.11 E-value: 8.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 10 VSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCD----------NREIAgpgper 79
Cdd:PRK11432 12 ITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvthrsiqQRDIC------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 aVVFQNHSLLPWLSCFDNVALAVDQVFRrtmSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKV 159
Cdd:PRK11432 82 -MVFQSYALFPHMSLGENVGYGLKMLGV---PKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 160 LLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-215 |
5.91e-44 |
|
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: 148.27 E-value: 5.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI-AGPGPERA-- 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsKLSSNERAkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ------VVFQNHSLLPWLSCFDNVALAVdqvFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:TIGR02211 81 rnkklgFIYQFHHLLPDFTALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLsDRVLMMTNG 215
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-215 |
9.26e-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: 147.71 E-value: 9.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 12 QRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGI-----TTPTEGGLLCDNREIAGPGPER------- 79
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVlelrrrv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNHSLLPwLSCFDNVALAVDqvFRRTMSKHERREWIEHNLARVQMSHALHKR--PGEISGGMKQRVGIARALAMKP 157
Cdd:cd03260 84 GMVFQKPNPFP-GSIYDNVAYGLR--LHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQElnTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-215 |
1.26e-43 |
|
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: 147.71 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNtasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA--GPGPERAV- 81
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 -----VFQNHSLLPWLSCFDNV---ALAVD---QVFRRTMSKHERREWIEhNLARVQMSHALHKRPGEISGGMKQRVGIA 150
Cdd:cd03256 78 rqigmIFQQFNLIERLSVLENVlsgRLGRRstwRSLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 151 RALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-215 |
2.22e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.11 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGeflaLQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPE--RAV 81
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEwrRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 --VFQNHSLLPwlscfDNVA---LAVDQVFRRTMSKHERREWiehnLARVQMSHA-LHKRPGEISGGMKQRVGIARALAM 155
Cdd:COG4619 77 ayVPQEPALWG-----GTVRdnlPFPFQLRERKFDRERALEL----LERLGLPPDiLDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 156 KPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-218 |
2.94e-43 |
|
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: 146.14 E-value: 2.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQNHSL---LPwLSCF 95
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRRSIdrdFP-ISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVALAVDQ--VFRRTMSKHERREwIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALT 173
Cdd:cd03235 89 DVVLMGLYGhkGLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556285678 174 RAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNGPAA 218
Cdd:cd03235 168 QEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-215 |
7.53e-43 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 145.77 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---- 79
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNHSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKV 159
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAEL---YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 160 LLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKG 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-215 |
1.53e-42 |
|
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: 144.31 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTAsgeFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAgPGPERA--- 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVN-RLRGRQlpl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ------VVFQNHSLLPWLSCFDNVALAVdQVFRRTMSKHERRewIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:TIGR02673 77 lrrrigVVFQDFRLLPDRTVYENVALPL-EVRGKKEREIQRR--VGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 155 MKPKVLLLDEPFGALDaltrAHLQDTVMHIQQELN---TTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR02673 154 NSPPLLLADEPTGNLD----PDLSERILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-215 |
3.26e-42 |
|
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: 144.36 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASgefLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---- 79
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 ----AVVFQNHSLLPWLSCFDNV---ALAVD---QVFRRTMSKHERREWIEhNLARVQMSHALHKRPGEISGGMKQRVGI 149
Cdd:TIGR02315 78 rrriGMIFQHYNLIERLTVLENVlhgRLGYKptwRSLLGRFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 150 ARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-234 |
3.86e-42 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 144.08 E-value: 3.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP------ 77
Cdd:PRK09493 1 MIEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderlir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 -ERAVVFQNHSLLPWLSCFDNVALAVDQVfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMK 156
Cdd:PRK09493 77 qEAGMVFQQFYLFPHLTALENVMFGPLRV--RGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 157 PKVLLLDEPFGALDALTRaHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG--EILAVDLPRPRHR 234
Cdd:PRK09493 155 PKLMLFDEPTSALDPELR-HEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGdpQVLIKNPPSQRLQ 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-221 |
4.10e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 147.30 E-value: 4.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP-ER--AVVFQNHSLLPWLSCF 95
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPaDRdiAMVFQNYALYPHMSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRA 175
Cdd:PRK11650 95 ENMAYGLKI---RGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556285678 176 HLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:PRK11650 172 QMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-240 |
4.35e-42 |
|
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: 147.17 E-value: 4.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 26 NVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCD-------NREIAGPgPER---AVVFQNHSLLPWLSCF 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdsARGIFLP-PHRrriGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVALAVdqvfRRTmSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRA 175
Cdd:COG4148 96 GNLLYGR----KRA-PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 176 HLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVdLPRPRHRVQLADD 240
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV-LSRPDLLPLAGGE 234
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-215 |
6.27e-42 |
|
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: 144.52 E-value: 6.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASG-EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---- 79
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 ----AVVFQNhsllpwlscfdnvalAVDQVFRRT-------------MSKHERREWIEHNLARVQMSHALHKR-PGEISG 141
Cdd:TIGR04521 81 rkkvGLVFQF---------------PEHQLFEETvykdiafgpknlgLSEEEAEERVKEALELVGLDEEYLERsPFELSG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 142 GMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKG 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-215 |
1.38e-41 |
|
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: 140.21 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSqrFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkni 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNhsllPWLscfdnvalavdqvFRRTmskherrewIEHNLarvqmshalhkrpgeISGGMKQRVGIARALAMKPKV 159
Cdd:cd03228 79 AYVPQD----PFL-------------FSGT---------IRENI---------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 160 LLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRL-STIRDADRIIVLDDG 170
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-225 |
1.80e-41 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 145.94 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 17 ASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERAV--VFQNHSLLPWLS 93
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERGVgmVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVA----LAvdqvfrrTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGAL 169
Cdd:PRK11000 92 VAENMSfglkLA-------GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 170 DALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILA 225
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-221 |
4.72e-41 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 145.56 E-value: 4.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 18 SGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---------AVVFQNHSL 88
Cdd:PRK10070 38 TGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrkkiAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 LPWLSCFDNVALAVDQVfrrTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGA 168
Cdd:PRK10070 118 MPHMTVLDNTAFGMELA---GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556285678 169 LDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
5-215 |
1.78e-40 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 139.00 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV--- 81
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVqlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 -----VFQNHSLLPWLSCFDNVALAVDqvFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMK 156
Cdd:TIGR02982 82 rrigyIFQAHNLLGFLTARQNVQMALE--LQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 157 PKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHD---VDEAvllsDRVLMMTNG 215
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDnriLDVA----DRILQMEDG 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-215 |
2.00e-40 |
|
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: 137.57 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP-ERAvvfQNHSLLPwlscfdnvalav 102
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPkELA---RKIAYVP------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 dQVfrrtmskherrewiehnLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVM 182
Cdd:cd03214 80 -QA-----------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLR 141
|
170 180 190
....*....|....*....|....*....|...
gi 556285678 183 HIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03214 142 RLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-215 |
1.22e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.61 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASGefLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAgpgpERA 80
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS----EET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 V---------VFQNhsllPwlscfDN--VALAV--DQVF---RRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMK 144
Cdd:PRK13635 76 VwdvrrqvgmVFQN----P-----DNqfVGATVqdDVAFgleNIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 145 QRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAvLLSDRVLMMTNG 215
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKG 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
1.39e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.86 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQavsqRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLL---N----LIAGITTptEGGLLCDNREIA 73
Cdd:COG1117 8 LEPKIEVR----NLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGARV--EGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 74 GPG--PE---RAV--VFQNHSLLPwLSCFDNVALAVdqvfrRTM---SKHERREWIEHNLARV----QMSHALHKRPGEI 139
Cdd:COG1117 82 DPDvdVVelrRRVgmVFQKPNPFP-KSIYDNVAYGL-----RLHgikSKSELDEIVEESLRKAalwdEVKDRLKKSALGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 140 SGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELntTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLG 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-229 |
2.96e-39 |
|
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: 135.96 E-value: 2.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGL-------LCDNREIagpgp 77
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtvaghdvVREPREV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 eRA---VVFQNHSLLPWLSCFDNVAlavdqVFRRT--MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARA 152
Cdd:cd03265 72 -RRrigIVFQDLSVDDELTGWENLY-----IHARLygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 153 LAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNgpaatvGEILAVDLP 229
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDH------GRIIAEGTP 216
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-215 |
3.02e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 137.28 E-value: 3.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASG-----EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA-G 74
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 75 PGPERA----VVFQ--NHSLLPWLscfdNVALAVDQVFRRT--MSKHERREWIEHNLARVQMS--HALHKrPGEISGGMK 144
Cdd:COG4167 81 DYKYRCkhirMIFQdpNTSLNPRL----NIGQILEEPLRLNtdLTAEEREERIFATLRLVGLLpeHANFY-PHMLSSGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 145 QRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQG 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
24-214 |
4.02e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 135.30 E-value: 4.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTP---TEGGLLCDNREIAGPGPER---AVVFQNHSLLPWLSCFDN 97
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQrriGILFQDDLLFPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VALAVdqvfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHL 177
Cdd:COG4136 97 LAFAL----PPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 556285678 178 QDTVMHIQQELNTTIVMITHDVDEAvLLSDRVLMMTN 214
Cdd:COG4136 173 REFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDLGN 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-215 |
5.06e-39 |
|
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: 135.23 E-value: 5.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntaSGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPgPERA---- 80
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL-RGRAipyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 -----VVFQNHSLLPWLSCFDNVALAVDqvfrrtMSKHERREW---IEHNLARVQMSHALHKRPGEISGGMKQRVGIARA 152
Cdd:cd03292 77 rrkigVVFQDFRLLPDRNVYENVAFALE------VTGVPPREIrkrVPAALELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 153 LAMKPKVLLLDEPFGALDALTRAHlqdtVMHIQQELN---TTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWE----IMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-215 |
5.93e-39 |
|
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: 133.14 E-value: 5.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnreiagpgperAVVFQNHSLLPWLScfdnv 98
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSG----------------EILIDGKDIAKLPL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 99 alavdqvfrrtmskHERREwiehnlaRVQMSHALhkrpgeiSGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQ 178
Cdd:cd00267 69 --------------EELRR-------RIGYVPQL-------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*..
gi 556285678 179 DTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd00267 121 ELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-215 |
6.48e-39 |
|
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: 134.94 E-value: 6.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNtaSGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAgPGPERA---- 80
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAArqsl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 -VVFQNHSLLPWLSCFDNVALavdqvFRRT--MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:cd03263 78 gYCPQFDALFDELTVREHLRF-----YARLkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-215 |
1.93e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 135.63 E-value: 1.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASgEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAgpgpERA 80
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQ-EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT----EEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 V---------VFQN-HSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIA 150
Cdd:PRK13650 76 VwdirhkigmVFQNpDNQFVGATVEDDVAFGLEN---KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 151 RALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEaVLLSDRVLMMTNG 215
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNG 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
5.20e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.35 E-value: 5.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSqrFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA- 80
Cdd:PRK13632 5 SVMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ----VVFQNhsllPwlscfDN--VALAV--DQVF---RRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGI 149
Cdd:PRK13632 83 kkigIIFQN----P-----DNqfIGATVedDIAFgleNKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 150 ARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAvLLSDRVLMMTNGPAATVG---EIL 224
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGkpkEIL 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-233 |
7.71e-38 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 135.09 E-value: 7.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE----- 78
Cdd:PRK11308 11 LKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 79 -RAV--VFQNhsllPWLSCfdNVALAVDQVFRR------TMSKHERREWIEHNLARVQMSHALHKR-PGEISGGMKQRVG 148
Cdd:PRK11308 91 rQKIqiVFQN----PYGSL--NPRKKVGQILEEpllintSLSAAERREKALAMMAKVGLRPEHYDRyPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 149 IARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVdL 228
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI-F 243
|
....*
gi 556285678 229 PRPRH 233
Cdd:PRK11308 244 NNPRH 248
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-249 |
1.18e-37 |
|
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: 139.97 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGefLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:COG2274 474 IELENVSFRYPGDSP--PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqi 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNHSLlpwlscF-----DNVALAVDQVfrrTMskherrEWIEHNLARVQMSHALHKRP-------GE----ISGGM 143
Cdd:COG2274 552 GVVLQDVFL------FsgtirENITLGDPDA---TD------EEIIEAARLAGLHDFIEALPmgydtvvGEggsnLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 144 KQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDvDEAVLLSDRVLMMTNgpaatvGEI 223
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR-LSTIRLADRIIVLDK------GRI 687
|
250 260
....*....|....*....|....*.
gi 556285678 224 LAvdlpRPRHRVQLADDSRYHHLRQQ 249
Cdd:COG2274 688 VE----DGTHEELLARKGLYAELVQQ 709
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-226 |
1.72e-37 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 134.85 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 10 VSQRFNTASGEFlALqNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNR-------EIAGPGPERAV- 81
Cdd:TIGR02142 1 LSARFSKRLGDF-SL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkGIFLPPEKRRIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 -VFQNHSLLPWLSCFDNVALAVdqvfRRTMSKHERREWiEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVL 160
Cdd:TIGR02142 79 yVFQEARLFPHLSVRGNLRYGM----KRARPSERRISF-ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 161 LLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAV 226
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-233 |
3.08e-37 |
|
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: 137.51 E-value: 3.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFNTASG-------EFLALQNVSFDIVEGETISLIGHSGCGKSTL----LNLIagittPTEGGLLCDNR 70
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 71 EIAGPG-----PERA---VVFQN--HSLLPWLSCFDNVA--LAVDQVfrrTMSKHERREWIEHNLARVQMSHA-LHKRPG 137
Cdd:COG4172 348 DLDGLSrralrPLRRrmqVVFQDpfGSLSPRMTVGQIIAegLRVHGP---GLSAAERRARVAEALEEVGLDPAaRHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 138 EISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVdeAVL--LSDRVLMMTNG 215
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDL--AVVraLAHRVMVMKDG 502
|
250 260
....*....|....*....|....
gi 556285678 216 ------PAATVgeilavdLPRPRH 233
Cdd:COG4172 503 kvveqgPTEQV-------FDAPQH 519
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
19-212 |
8.14e-37 |
|
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: 129.27 E-value: 8.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV---------VFQNHSLL 89
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASkfrreklgyLFQNFALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 90 PWLSCFDNVALAVdqVFRRtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGAL 169
Cdd:TIGR03608 89 ENETVEENLDLGL--KYKK-LSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556285678 170 DALTRahlqDTVMHIQQELN---TTIVMITHDVdEAVLLSDRVLMM 212
Cdd:TIGR03608 166 DPKNR----DEVLDLLLELNdegKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-214 |
5.35e-36 |
|
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: 127.21 E-value: 5.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER--- 79
Cdd:COG4133 1 MMLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 -AVVFQNHSLLPWLSCFDNVALavdqvFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPK 158
Cdd:COG4133 77 lAYLGHADGLKPELTVRENLRF-----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 159 VLLLDEPFGALDALTRAHLQDtvmHIQQELN--TTIVMITHDVDEavLLSDRVLMMTN 214
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAE---LIAAHLArgGAVLLTTHQPLE--LAAARVLDLGD 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-221 |
5.82e-36 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 127.01 E-value: 5.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA-------GPGP 77
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnriGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERAVVFQNHSLLPWLSCFDNValavdqvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQL---------KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHiQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-232 |
9.71e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.83 E-value: 9.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA 80
Cdd:COG1129 1 AEPLLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ------VVFQNHSLLPWLSCFDNVALAVDQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:COG1129 77 qaagiaIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNGpaATVGEILAVDLPRPR 232
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG--RLVGTGPVAELTEDE 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-215 |
3.12e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.28 E-value: 3.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVsqrfNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlcdnrEIAG--------PG 76
Cdd:COG4161 3 IQLKNI----NCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----NIAGhqfdfsqkPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 PERA--------VVFQNHSLLPWLSCFDNVALAVDQVFRrtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVG 148
Cdd:COG4161 74 EKAIrllrqkvgMVFQQYNLWPHLTVMENLIEAPCKVLG--LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 149 IARALAMKPKVLLLDEPFGALDALTRAHlqdtVMHIQQELNT---TIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQ----VVEIIRELSQtgiTQVIVTHEVEFARKVASQVVYMEKG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-215 |
5.45e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.08 E-value: 5.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 28 SFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---AVVFQNHSLLPWLSCFDNVALAVDQ 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvSMLFQENNLFSHLTVAQNIGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 105 VFRRTmskHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHI 184
Cdd:PRK10771 99 GLKLN---AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190
....*....|....*....|....*....|.
gi 556285678 185 QQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK10771 176 CQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-226 |
4.81e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 125.20 E-value: 4.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFNTASGEFL---------ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI 72
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDGKQWfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 73 AGPGPE--RAV------VFQN--HSLLPWLSCFDNVALAVdQVFRRTMSKHERREWIEHNLARVQMSHALHKR-PGEISG 141
Cdd:PRK15079 86 LGMKDDewRAVrsdiqmIFQDplASLNPRMTIGEIIAEPL-RTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 142 GMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
....*
gi 556285678 222 EILAV 226
Cdd:PRK15079 245 TYDEV 249
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-221 |
6.82e-34 |
|
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: 122.09 E-value: 6.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCD----NREIAGPGPER 79
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNHSLLPWLSCFDNValavdQVFRRT--MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:cd03266 81 GFVSDSTGLYDRLTARENL-----EYFAGLygLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHiQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
19-229 |
8.49e-34 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 124.04 E-value: 8.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdNREIAG------PGPER---AVVFQNHSLL 89
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSG-----TARVAGydvvrePRKVRrsiGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 90 PWLSCFDNVALAVDQVfrrTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGAL 169
Cdd:TIGR01188 79 EDLTGRENLEMMGRLY---GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 170 DALTRAHLQDTVMHIqQELNTTIVMITHDVDEAVLLSDRVLMMTNgpaatvGEILAVDLP 229
Cdd:TIGR01188 156 DPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDH------GRIIAEGTP 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-215 |
1.60e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 122.12 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASG-EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERAV- 81
Cdd:COG1101 2 LELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKRAKy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 ---VFQNHSL--LPWLSCFDNVALAVDQVFRRTMS---KHERREWIEHNLARVQMS--HALHKRPGEISGGMKQrvgiAR 151
Cdd:COG1101 82 igrVFQDPMMgtAPSMTIEENLALAYRRGKRRGLRrglTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQRQ----AL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 152 ALAM----KPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG1101 158 SLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-215 |
1.61e-33 |
|
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: 121.00 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 15 NTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV------VFQNHSL 88
Cdd:cd03224 7 NAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAragigyVPEGRRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 LPWLSCFDNVALAVDQVFRRtmSKHERREWIEHNLARV-QMshaLHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFG 167
Cdd:cd03224 87 FPELTVEENLLLGAYARRRA--KRKARLERVYELFPRLkER---RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 168 ALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERG 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-235 |
2.15e-33 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 122.22 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNT-----ASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE 78
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 79 RAVVFQNHSLLPWLSCFD--NVALAVDQVFRR------TMSKHERREWIEHNLARVQM-SHALHKRPGEISGGMKQRVGI 149
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSavNPRMTVRQIIGEplrhltSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 150 ARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGP------------- 216
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQiveecdvaqllsf 241
|
250 260
....*....|....*....|.
gi 556285678 217 AATVGEIL--AVDLPRPRHRV 235
Cdd:TIGR02769 242 KHPAGRNLqsAVLPEHPVRRS 262
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-215 |
3.02e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 120.89 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVsqrfNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlcdnrEIAG--------PG 76
Cdd:PRK11124 3 IQLNGI----NCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----NIAGnhfdfsktPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 PE------RAV--VFQNHSLLPWLSCFDNVALAVDQVfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVG 148
Cdd:PRK11124 74 DKairelrRNVgmVFQQYNLWPHLTVQQNLIEAPCRV--LGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 149 IARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-215 |
5.69e-33 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 122.53 E-value: 5.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKS----TLLNLIA--GITTpteGGLLCDNREIAG 74
Cdd:PRK09473 9 ADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRIG---GSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 75 PgPER----------AVVFQN--HSLLPWLSCFDNVaLAVDQVFRRtMSKHERREWIEHNLARVQMSHAlHKR----PGE 138
Cdd:PRK09473 86 L-PEKelnklraeqiSMIFQDpmTSLNPYMRVGEQL-MEVLMLHKG-MSKAEAFEESVRMLDAVKMPEA-RKRmkmyPHE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 139 ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-221 |
6.76e-33 |
|
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: 125.64 E-value: 6.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSqrFNTASGEFlALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER--- 79
Cdd:COG4988 335 PSIELEDVS--FSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrr 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --AVVFQNhsllPWLscF-----DNVALAvdqvfRRTMSKHERREWIE-HNLARV--QMSHALHKRPGE----ISGGMKQ 145
Cdd:COG4988 412 qiAWVPQN----PYL--FagtirENLRLG-----RPDASDEELEAALEaAGLDEFvaALPDGLDTPLGEggrgLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 146 RVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDvDEAVLLSDRVLMMTNGPAATVG 221
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHR-LALLAQADRILVLDDGRIVEQG 553
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
9.09e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.63 E-value: 9.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSqrFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER--- 79
Cdd:PRK13648 6 SIIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --AVVFQN--HSLLPWLSCFDnVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAM 155
Cdd:PRK13648 84 hiGIVFQNpdNQFVGSIVKYD-VAFGLEN---HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 156 KPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAvLLSDRVLMMTNG 215
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-225 |
1.18e-32 |
|
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: 124.53 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRF-NTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLC----DNREIAGPG 76
Cdd:TIGR03269 277 EPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 PE---RA-----VVFQNHSLLPWLSCFDNVALAVDQVFRRTMSKheRREWIEHNLARVQMSHA---LHKRPGEISGGMKQ 145
Cdd:TIGR03269 357 PDgrgRAkryigILHQEYDLYPHRTVLDNLTEAIGLELPDELAR--MKAVITLKMVGFDEEKAeeiLDKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 146 RVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG---E 222
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGdpeE 514
|
...
gi 556285678 223 ILA 225
Cdd:TIGR03269 515 IVE 517
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-215 |
1.44e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 119.65 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNRE------IAG 74
Cdd:PRK11701 3 DQPLLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 75 PGPER--------AVVFQN--HSLLPWLSCFDNVAlavdqvfRRTMSKHER-----REWIEHNLARVQMSHA-LHKRPGE 138
Cdd:PRK11701 79 SEAERrrllrtewGFVHQHprDGLRMQVSAGGNIG-------ERLMAVGARhygdiRATAGDWLERVEIDAArIDDLPTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 139 ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-215 |
1.48e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 119.15 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP---- 77
Cdd:PRK11629 3 KILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 -----ERAVVFQNHSLLPWLSCFDNVALAVDQVFRRTMSKHER-REWiehnLARVQMSHALHKRPGEISGGMKQRVGIAR 151
Cdd:PRK11629 83 elrnqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRaLEM----LAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTrahlQDTVMHIQQELN----TTIVMITHDVDEAVLLSdRVLMMTNG 215
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARN----ADSIFQLLGELNrlqgTAFLVVTHDLQLAKRMS-RQLEMRDG 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-215 |
1.81e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.81 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRF--NTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDN--------- 69
Cdd:PRK13633 1 MNEMIKCKNVSYKYesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 70 ---REIAGpgperaVVFQNhsllPwlscfDN--VALAV--DQVF---RRTMSKHERREWIEHNLARVQMSHALHKRPGEI 139
Cdd:PRK13633 81 wdiRNKAG------MVFQN----P-----DNqiVATIVeeDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 140 SGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVlLSDRVLMMTNG 215
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMDSG 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-249 |
2.72e-32 |
|
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: 124.11 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSqrFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER--- 79
Cdd:COG4987 332 PSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --AVVFQNHSLlpwlscF-----DNVALAVDQVfrrtmSKHErrewIEHNLARVQMSHALHKRP-------GE----ISG 141
Cdd:COG4987 410 riAVVPQRPHL------FdttlrENLRLARPDA-----TDEE----LWAALERVGLGDWLAALPdgldtwlGEggrrLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 142 GMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDvDEAVLLSDRVLMMTNgpaatvG 221
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHR-LAGLERMDRILVLED------G 545
|
250 260
....*....|....*....|....*...
gi 556285678 222 EILAvdlpRPRHRVQLADDSRYHHLRQQ 249
Cdd:COG4987 546 RIVE----QGTHEELLAQNGRYRQLYQR 569
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-222 |
3.85e-32 |
|
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: 115.60 E-value: 3.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAvvfq 84
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 85 nhsllpwlscfdnvalavdqvfRRtmskherrewiehnlARVQMSHALhkrpgeiSGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:cd03216 73 ----------------------RR---------------AGIAMVYQL-------SVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 165 PFGALDALTRAHLQDtVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGpaATVGE 222
Cdd:cd03216 109 PTAALTPAEVERLFK-VIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-226 |
4.63e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.00 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASG-EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG------- 76
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 PERAVVFQnhslLPWLSCFDNVaLAVDQVF---RRTMSKHERREWIEHNLARVQMSHA--LHKRPGEISGGMKQRVGIAR 151
Cdd:PRK13637 83 KKVGLVFQ----YPEYQLFEET-IEKDIAFgpiNLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAV 226
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-233 |
4.88e-32 |
|
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: 122.87 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKS----TLLNLIAGITTPTEGGLLCDNREIAGPG 76
Cdd:COG4172 3 SMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 PER---------AVVFQN--HSLLPWLSCFDNVAlavdQVFR--RTMSKHERREWIEHNLARVQMSHA---LHKRPGEIS 140
Cdd:COG4172 83 ERElrrirgnriAMIFQEpmTSLNPLHTIGKQIA----EVLRlhRGLSGAAARARALELLERVGIPDPerrLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 141 GGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHD---VDEavlLSDRVLMMTNG-- 215
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVMRQGei 235
|
250
....*....|....*....
gi 556285678 216 -PAATVGEILAvdlpRPRH 233
Cdd:COG4172 236 vEQGPTAELFA----APQH 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-232 |
1.33e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 117.48 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNT-----ASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP 77
Cdd:PRK10419 2 TLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERA--------VVFQNHsllpwLSCFD---NVALAVDQVFRR--TMSKHERREWIEHNLARVQMSHA-LHKRPGEISGGM 143
Cdd:PRK10419 82 AQRkafrrdiqMVFQDS-----ISAVNprkTVREIIREPLRHllSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 144 KQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG---PAATV 220
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGqivETQPV 236
|
250
....*....|..
gi 556285678 221 GEILAVDLPRPR 232
Cdd:PRK10419 237 GDKLTFSSPAGR 248
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-215 |
4.66e-31 |
|
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: 114.21 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGeTISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE-RAVVf 83
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 84 qnhSLLPW-LSCFDNV----ALAVDQVFRRTMSKHERREwIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPK 158
Cdd:cd03264 75 ---GYLPQeFGVYPNFtvreFLDYIAWLKGIPSKEVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 159 VLLLDEPFGALDALTRAHLQdtvmHIQQEL--NTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFR----NLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-222 |
5.91e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.75 E-value: 5.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA 80
Cdd:COG3845 2 MPPALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 V------VFQNHSLLPWLSCFDNVALAVDQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:COG3845 78 IalgigmVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 155 MKPKVLLLDEP------------FGALDALTRAhlqdtvmhiqqelNTTIVMITHDVDEAVLLSDRVLMMTNGpaATVGE 222
Cdd:COG3845 158 RGARILILDEPtavltpqeadelFEILRRLAAE-------------GKSIIFITHKLREVMAIADRVTVLRRG--KVVGT 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-215 |
6.20e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.21 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE-----RAVVFQNHSL-LPWlSCFDN 97
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrRAVLPQHSSLaFPF-TVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VALAVDQVFRrtmSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA-------MKPKVLLLDEPFGALD 170
Cdd:COG4559 96 VALGRAPHGS---SAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 171 AltrAHlQDTVMHIQQEL---NTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG4559 173 L---AH-QHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-240 |
8.76e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.56 E-value: 8.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAgpgperavvFQNHSLLpwlSCFDNVALAV 102
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK---------YDKKSLL---EVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 ----DQVFRRT-------------MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEP 165
Cdd:PRK13639 85 qnpdDQLFAPTveedvafgplnlgLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 166 FGALDALTRAHlqdtVMHIQQELN---TTIVMITHDVDEAVLLSDRVLMMTNGP---AATVGEILA---------VDLPR 230
Cdd:PRK13639 165 TSGLDPMGASQ----IMKLLYDLNkegITIIISTHDVDLVPVYADKVYVMSDGKiikEGTPKEVFSdietirkanLRLPR 240
|
250
....*....|
gi 556285678 231 PRHRVQLADD 240
Cdd:PRK13639 241 VAHLIEILNK 250
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-230 |
9.64e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 115.67 E-value: 9.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEG--------GL------LCDNREIAGpgperaVVFQN-HS 87
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNpnskitvdGItltaktVWDIREKVG------IVFQNpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 88 LLPWLSCFDNVALAVD--QVFRRTMSKherrewIEHN-LARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:PRK13640 96 QFVGATVGDDVAFGLEnrAVPRPEMIK------IVRDvLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 165 PFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVlLSDRVLMMTNgpaatvGEILAVDLPR 230
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDD------GKLLAQGSPV 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-215 |
2.42e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.05 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 13 RFNTASGEFL----ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLL--------CDNREIAGPGPERA 80
Cdd:PRK10908 3 RFEHVSKAYLggrqALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghditrLKNREVPFLRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQNHSLLPWLSCFDNVALAvdqVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVL 160
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAIP---LIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 161 LLDEPFGALDaltrAHLQDTVMHIQQELN---TTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK10908 160 LADEPTGNLD----DALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-215 |
1.00e-29 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 110.77 E-value: 1.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVV-- 82
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIga 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 83 -FQNHSLLPWLSCFDNValavdQVFRRTMSKHERRewIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLL 161
Cdd:cd03268 77 lIEAPGFYPNLTARENL-----RLLARLLGIRKKR--IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556285678 162 LDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-215 |
1.46e-29 |
|
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: 110.42 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 22 LALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV--VFQN--HSLLpwlscFDN 97
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIgyVMQDvdYQLF-----TDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VAlavDQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHL 177
Cdd:cd03226 89 VR---EELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 556285678 178 QDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03226 166 GELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-240 |
1.52e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.51 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIaGPGP------- 77
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDrrrigyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 --ERavvfqnhSLLPWLSCFDN-VALAVdqvfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:COG4152 77 peER-------GLYPKMKVGEQlVYLAR----LKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAV--DLPRPR 232
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIrrQFGRNT 224
|
....*...
gi 556285678 233 HRVQLADD 240
Cdd:COG4152 225 LRLEADGD 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-219 |
1.89e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 111.24 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPER 79
Cdd:PRK11300 2 SQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 A---VV--FQNHSLLPWLSCFDNVALAVDQ--------------VFRRtmSKHERREWIEHNLARVQMSHALHKRPGEIS 140
Cdd:PRK11300 78 ArmgVVrtFQHVRLFREMTVIENLLVAQHQqlktglfsgllktpAFRR--AESEALDRAATWLERVGLLEHANRQAGNLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 141 GGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG-PAAT 219
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGtPLAN 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-215 |
2.04e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.03 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVVFQNHSLLPwLSCFDN 97
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrrqiGVVPQDTFLFS-GTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VALAvdqvfRRTMSkherREWIEHNLARVQMSHALHKRP-------GE----ISGGMKQRVGIARALAMKPKVLLLDEPF 166
Cdd:COG1132 434 IRYG-----RPDAT----DEEVEEAAKAAQAHEFIEALPdgydtvvGErgvnLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556285678 167 GALDALTRAHLQDTVMHIQQelNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:COG1132 505 SALDTETEALIQEALERLMK--GRTTIVIAHRL-STIRNADRILVLDDG 550
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-215 |
3.24e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.83 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA----GPGPER--------------A 80
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdKDGQLKvadknqlrllrtrlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQNHSLLPWLSCFDNVALAVDQVFrrTMSKHERREWIEHNLARVQMSH-ALHKRPGEISGGMKQRVGIARALAMKPKV 159
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 160 LLLDEPFGALDaltrAHLQDTVMHIQQEL---NTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK10619 174 LLFDEPTSALD----PELVGEVLRIMQQLaeeGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-215 |
3.32e-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: 108.46 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSqrFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNHSLLPWlSCFDNValavdqvfrrtmskherrewiehnlarvqmshalhkrpgeISGGMKQRVGIARALAMKPKV 159
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 160 LLLDEPFGALDALTRAHLQDTVMHIqQELNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVLEDG 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-215 |
3.98e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.87 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASgeflALQNVSFDIVEGETISLIGHSGCGKSTLLN----LIAGITTPTEGGLLCDN------- 69
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRtvqregr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 70 --REIAGPGPERAVVFQNHSLLPWLSCFDNV---ALAVDQVFRRTMS--KHERREWIEHNLARVQMSHALHKRPGEISGG 142
Cdd:PRK09984 77 laRDIRKSRANTGYIFQQFNLVNRLSVLENVligALGSTPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 143 MKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-202 |
7.25e-29 |
|
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: 108.28 E-value: 7.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA----GPGPER---AVVFQNhsllpwlscf 95
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrkGLLERRqrvGLVFQD---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 dnvalAVDQVFRRT-------------MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLL 162
Cdd:TIGR01166 77 -----PDDQLFAADvdqdvafgplnlgLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556285678 163 DEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEA 202
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAE-GMTVVISTHDVDLA 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-215 |
9.93e-29 |
|
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: 109.40 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLcdnrEIAGPGPERAVV 82
Cdd:COG1119 2 PLLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFGERRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 83 FQ------------NHSLLPWLSCFDNV---ALAVDQVFRRTMSKHERR--EWiehnLARVQMSHALHKRPGEISGGMKQ 145
Cdd:COG1119 74 WElrkriglvspalQLRFPRDETVLDVVlsgFFDSIGLYREPTDEQRERarEL----LELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 146 RVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-215 |
1.17e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.48 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPE--- 78
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAElar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 79 -RAVVFQNHSLlpwlscfdNVALAVDQVFR-----RTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARA 152
Cdd:PRK13548 77 rRAVLPQHSSL--------SFPFTVEEVVAmgrapHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 153 LA------MKPKVLLLDEPFGALDAltrAHlQDTVMHIQQEL----NTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDL---AH-QHHVLRLARQLaherGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-215 |
1.25e-28 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 108.61 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKST----LLNLIAGITTPTEGGLLCDNREIAGP---GPERAVVFQNhsllPwLSCF 95
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLsirGRHIATIMQN----P-RTAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 dNVALAVDQVFRRTMSKHER-----REWIEHNLARVQMSHA---LHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFG 167
Cdd:TIGR02770 76 -NPLFTMGNHAIETLRSLGKlskqaRALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 168 ALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDG 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-241 |
1.27e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 114.05 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER- 79
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --------AVVFQNHSLLPWLSCFDNVAlaVDQVFRRTmSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIAR 151
Cdd:PRK10535 81 aqlrrehfGFIFQRYHLLSHLTAAQNVE--VPAVYAGL-ERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 152 ALAMKPKVLLLDEPFGALDaltrAHLQDTVMHIQQELNT---TIVMITHDVDEAVlLSDRVLMMTNgpaatvGEILAVDL 228
Cdd:PRK10535 158 ALMNGGQVILADEPTGALD----SHSGEEVMAILHQLRDrghTVIIVTHDPQVAA-QAERVIEIRD------GEIVRNPP 226
|
250
....*....|...
gi 556285678 229 PRPRHRVQLADDS 241
Cdd:PRK10535 227 AQEKVNVAGGTEP 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-215 |
2.35e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASG-EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---- 79
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 -----AVVFQnhsllpwlscfdnvaLAVDQVFRRT-------------MSKHERREWIEHNLARVQMSHA-LHKRPGEIS 140
Cdd:PRK13634 83 lrkkvGIVFQ---------------FPEHQLFEETvekdicfgpmnfgVSEEDAKQKAREMIELVGLPEElLARSPFELS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 141 GGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
23-223 |
2.55e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.17 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI----AGPGPER---AVVFQ--NHSLLPwLS 93
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLResvGMVFQdpDNQLFS-AS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAVdqvFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALT 173
Cdd:PRK13636 100 VYQDVSFGA---VNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556285678 174 RAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEI 223
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
23-212 |
3.06e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 106.55 E-value: 3.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLcdnreiAGPGPERAVVFQnHSLLPW---LSCFDNVA 99
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------RAGGARVAYVPQ-RSEVPDslpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 100 LAV--DQVFRRTMSKHERREwIEHNLARVQMsHALHKRP-GEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAH 176
Cdd:NF040873 80 MGRwaRRGLWRRLTRDDRAA-VDDALERVGL-ADLAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 556285678 177 LQDTVMHIQQElNTTIVMITHDvDEAVLLSDRVLMM 212
Cdd:NF040873 158 IIALLAEEHAR-GATVVVVTHD-LELVRRADPCVLL 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-225 |
3.24e-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: 107.63 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERA---VVF--QNHSLLPWLSCFDN 97
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRArlgIGYlpQEASIFRKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHL 177
Cdd:cd03218 96 ILAVLEI---RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556285678 178 QDTVMHIQQElntTI-VMIT-HDVDEAVLLSDRVLMMTNgpaatvGEILA 225
Cdd:cd03218 173 QKIIKILKDR---GIgVLITdHNVRETLSITDRAYIIYE------GKVLA 213
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-233 |
6.06e-28 |
|
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: 107.22 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG------P 75
Cdd:TIGR02323 1 KPLLQVSGLSKSY----GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAElelyqlS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 76 GPER--------AVVFQNHSllpwlscfDNVALAVD---QVFRRTMSKHER-----REWIEHNLARVQMSHA-LHKRPGE 138
Cdd:TIGR02323 77 EAERrrlmrtewGFVHQNPR--------DGLRMRVSagaNIGERLMAIGARhygniRATAQDWLEEVEIDPTrIDDLPRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 139 ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAA 218
Cdd:TIGR02323 149 FSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
250
....*....|....*
gi 556285678 219 TVGEILAVdLPRPRH 233
Cdd:TIGR02323 229 ESGLTDQV-LDDPQH 242
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-215 |
7.33e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.40 E-value: 7.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE----- 78
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEarakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 79 RA----VVFQNHSLLPWLSCFDNVALAVdqvFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:PRK10584 86 RAkhvgFVFQSFMLIPTLNALENVELPA---LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVlLSDRVLMMTNG 215
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNG 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-215 |
7.40e-28 |
|
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: 106.60 E-value: 7.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV- 81
Cdd:COG0410 2 PMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 -----VFQNHSLLPWLSCFDNVALAvdqvfRRTMSKHERREWiehNLARV--------QMshaLHKRPGEISGGMKQRVG 148
Cdd:COG0410 78 lgigyVPEGRRIFPSLTVEENLLLG-----AYARRDRAEVRA---DLERVyelfprlkER---RRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 149 IARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERG 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-215 |
7.90e-28 |
|
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: 106.36 E-value: 7.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRF---NTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNRE----IA 73
Cdd:COG4778 1 MTTLLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 74 GpGPERAV----------VFQNHSLLPWLSCFDNVALAVdqvFRRTMSKHERREWIEHNLARVQMSHAL-HKRPGEISGG 142
Cdd:COG4778 81 Q-ASPREIlalrrrtigyVSQFLRVIPRVSALDVVAEPL---LERGVDREEARARARELLARLNLPERLwDLPPATFSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 143 MKQRVGIARALAMKPKVLLLDEPFGALDALTRAhlqdTVMHIQQEL---NTTIVMITHDVD--EAVllSDRVLMMTNG 215
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRA----VVVELIEEAkarGTAIIGIFHDEEvrEAV--ADRVVDVTPF 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-215 |
1.22e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.13 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAgPGPERAV------VFQNHSllpwlscfd 96
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKWVrskvglVFQDPD--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 97 nvalavDQVFRRT-------------MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLD 163
Cdd:PRK13647 90 ------DQVFSSTvwddvafgpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 164 EPFGALDALTrahlQDTVMHIQQELN---TTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13647 164 EPMAYLDPRG----QETLMEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-215 |
2.04e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.01 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASgeflALQNVSFDIVEGETISLIGHSGCGKSTLL-------NLIAGITTptEGGLLCDNREIA 73
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmnDLNPEVTI--TGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 74 GPG-------PERAVVFQNHSLLPwLSCFDNVALAVDqvFRRTMSKHERREWIEHNL--ARV--QMSHALHKRPGEISGG 142
Cdd:PRK14239 76 SPRtdtvdlrKEIGMVFQQPNPFP-MSIYENVVYGLR--LKGIKDKQVLDEAVEKSLkgASIwdEVKDRLHDSALGLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 143 MKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELntTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-215 |
2.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.75 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCD---------NREIAGPGPERAVVFQnhslLPWLS 93
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstskNKDIKQIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAvDQVF---RRTMSKHERREWIEHNLARVQMSHAL-HKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGAL 169
Cdd:PRK13649 98 LFEETVLK-DVAFgpqNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556285678 170 DALTRAHLqdtvMHIQQELN---TTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13649 177 DPKGRKEL----MTLFKKLHqsgMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-212 |
2.23e-27 |
|
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: 110.07 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNtasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:TIGR02857 322 LEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqi 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNhsllPWL---SCFDNVALAvdqvfRRTMSKHERREWIE----HNLARVqMSHALHKRPGE----ISGGMKQRVG 148
Cdd:TIGR02857 399 AWVPQH----PFLfagTIAENIRLA-----RPDASDAEIREALEraglDEFVAA-LPQGLDTPIGEggagLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 149 IARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDvDEAVLLSDRVLMM 212
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-201 |
7.10e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.03 E-value: 7.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFNTASgeflALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-- 79
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAK----ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 ---AVVFQNHSLLPwLSCFDNvaLAVDQVFRRtmsKHERREWIEHNLARVQM-SHALHKRPGEISGGMKQRVGIARALAM 155
Cdd:PRK10247 81 qqvSYCAQTPTLFG-DTVYDN--LIFPWQIRN---QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556285678 156 KPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDE 201
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-225 |
1.18e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.57 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI----------AGPG--PERAVVFQNhsllpw 91
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarLGIGylPQEASIFRK------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 92 LSCFDNVaLAVDQVfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDA 171
Cdd:COG1137 93 LTVEDNI-LAVLEL--RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 172 LTRAHLQDTVMHIQQElntTI-VMIT-HDVDEAVLLSDRVLMMTNgpaatvGEILA 225
Cdd:COG1137 170 IAVADIQKIIRHLKER---GIgVLITdHNVRETLGICDRAYIISE------GKVLA 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-235 |
1.68e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.45 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGIT-----TPTEGGLLCDNREI-AGPGPE--RAV--VFQNHSL 88
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIElrRRVqmVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 LPWLSCFDNVALAVdQVFRRTMSKHERREWIEHNLARVQMSHALHKR----PGEISGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:PRK14247 94 IPNLSIFENVALGL-KLNRLVKSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 165 PFGALDALTRAHLQDTVMHIQQELntTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVdLPRPRHRV 235
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV-FTNPRHEL 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-215 |
1.89e-26 |
|
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: 102.67 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 20 EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPerAVVFQNHSLLP---WL---S 93
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP--ADLRRNIGYVPqdvTLfygT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAvdqvfrrtMSKHERREWIE-------HNLARVQmSHALHKRPGE----ISGGMKQRVGIARALAMKPKVLLL 162
Cdd:cd03245 94 LRDNITLG--------APLADDERILRaaelagvTDFVNKH-PNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 163 DEPFGALDALTRAHLqdtVMHIQQEL-NTTIVMITHdvdEAVLLS--DRVLMMTNG 215
Cdd:cd03245 165 DEPTSAMDMNSEERL---KERLRQLLgDKTLIIITH---RPSLLDlvDRIIVMDSG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-215 |
4.21e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.52 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASgeflALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA---- 80
Cdd:PRK11264 4 IEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ---------VVFQNHSLLPWLSCFDNVALAvdQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIAR 151
Cdd:PRK11264 80 irqlrqhvgFVFQNFNLFPHRTVLENIIEG--PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-198 |
5.24e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 5.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 7 VQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGPER-AVVFQN 85
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVSIPKGLRiGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 86 HSLLPWLSCFDNVAlavdQVFRRTMSKHERREWIEHN----------LARVQM-----------------------SHAL 132
Cdd:COG0488 70 PPLDDDLTVLDTVL----DGDAELRALEAELEELEAKlaepdedlerLAELQEefealggweaearaeeilsglgfPEED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 133 HKRP-GEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVmhiqQELNTTIVMITHD 198
Cdd:COG0488 146 LDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-207 |
7.76e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 102.04 E-value: 7.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNTASgeflALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGIT-----TPTEGGLLCDNREIAgpgp 77
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERAV-----------VFQNHSLLPwLSCFDNVALAVDQVFRRtmSKHERREWIEHNLARVQM----SHALHKRPGEISGG 142
Cdd:PRK14258 78 ERRVnlnrlrrqvsmVHPKPNLFP-MSVYDNVAYGVKIVGWR--PKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 143 MKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSD 207
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-248 |
9.10e-26 |
|
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: 101.41 E-value: 9.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 13 RFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE--RA---VVFQNHS 87
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlRRqvgVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 88 LLPwLSCFDNVALAvdqvfRRTMSKHERREwiehnLARVQMSHA-LHKRP-------GE----ISGGMKQRVGIARALAM 155
Cdd:cd03252 87 LFN-RSIRDNIALA-----DPGMSMERVIE-----AAKLAGAHDfISELPegydtivGEqgagLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 156 KPKVLLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDVdEAVLLSDRVLMMTNGPAATVGeilavdlprpRHRV 235
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQG----------SHDE 222
|
250
....*....|...
gi 556285678 236 QLADDSRYHHLRQ 248
Cdd:cd03252 223 LLAENGLYAYLYQ 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-215 |
1.16e-25 |
|
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: 100.87 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlcdnrEIAG--PGPER-------AVVFQNHSLLPW-L 92
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGlvPWKRRkkflrriGVVFGQKTQLWWdL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 93 SCFDNVALAVDqVFRrtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDAL 172
Cdd:cd03267 111 PVIDSFYLLAA-IYD--LPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556285678 173 TRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-215 |
1.84e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 101.32 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASgEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG---- 76
Cdd:PRK13642 1 MNKILEVENLVFKYEKES-DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 -PERAVVFQN-HSLLPWLSCFDNVALAVDQvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:PRK13642 80 rRKIGMVFQNpDNQFVGATVEDDVAFGMEN---QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVlLSDRVLMMTNG 215
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAG 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-215 |
2.02e-25 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 99.78 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA-------GPGP 77
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrkdlhkiGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERAVVFQNhsllpwLSCFDNVALavdqvfrRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:TIGR03740 77 ESPPLYEN------LTARENLKV-------HTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHP 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEG 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-233 |
2.08e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLL---------NLIAGIttptEGGLLCDNREIAGPG-------PERAVVFQNHS 87
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllelNEEARV----EGEVRLFGRNIYSPDvdpievrREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 88 LLPWLSCFDNVALAVdQVFRRTMSKHERREWIEHNLARV----QMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLD 163
Cdd:PRK14267 96 PFPHLTIYDNVAIGV-KLNGLVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 164 EPFGALDALTRAHLQDTVMHIQQELntTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVdLPRPRH 233
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV-FENPEH 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-215 |
2.08e-25 |
|
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: 99.91 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 13 RFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGPERAVVFQNHSLLPWL 92
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG-------TVTVRGRVSSLLGLGGGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 93 SCFDNValavdqVFRRT---MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGAL 169
Cdd:cd03220 100 TGRENI------YLNGRllgLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556285678 170 DALTRAHLQDtVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03220 174 DAAFQEKCQR-RLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-215 |
3.34e-25 |
|
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: 99.27 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 10 VSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAG---ITTPTEGGLLCDNREI-AGPGPER-AVVFQ 84
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRkPDQFQKCvAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 85 NHSLLPWLSCFDNVALAVDQVFRRTMSKHERR-EWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLD 163
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILRLPRKSSDAIRKkRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556285678 164 EPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSG 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-215 |
1.03e-24 |
|
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: 96.73 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA----VVF-----QNHSLLPWLS 93
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAVdqvfrrtmskherrewiehnlarvqmshalhkrpgEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALT 173
Cdd:cd03215 95 VAENIALSS-----------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556285678 174 RAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-207 |
2.15e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAV--SQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLL-------NLIAGITTptEGGLLCDNRE 71
Cdd:PRK14243 1 TSTLNGTETVlrTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 72 IAGPGPERA-------VVFQNHSLLPwLSCFDNVALAVdqvfRRTMSKHERREWIEHNLARV----QMSHALHKRPGEIS 140
Cdd:PRK14243 79 LYAPDVDPVevrrrigMVFQKPNPFP-KSIYDNIAYGA----RINGYKGDMDELVERSLRQAalwdEVKDKLKQSGLSLS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 141 GGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELntTIVMITHDVDEAVLLSD 207
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
15-215 |
2.44e-24 |
|
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: 97.21 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 15 NTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER------AVVFQNHSL 88
Cdd:TIGR03410 7 NVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHEraragiAYVPQGREI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 LPWLSCFDNVALAVDQVFRRtmskheRREWIEHNLARV----QMshaLHKRPGEISGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:TIGR03410 87 FPRLTVEENLLTGLAALPRR------SRKIPDEIYELFpvlkEM---LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 556285678 165 PFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-226 |
3.50e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 99.18 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 41 GHSGCGKSTLLNLIAGITTPTEGGLLCDNR-------EIAGPGPERAV--VFQNHSLLPWLSCFDNValavdqvfRRTMS 111
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekGICLPPEKRRIgyVFQDARLFPHYKVRGNL--------RYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 112 KHERREW--------IEHNLARVqmshalhkrPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMH 183
Cdd:PRK11144 103 KSMVAQFdkivallgIEPLLDRY---------PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556285678 184 IQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAV 226
Cdd:PRK11144 174 LAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-251 |
5.66e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 100.70 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFNTASG-------EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI-- 72
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdt 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 73 AGPGPERAV------VFQN--HSLLPWLSCFDNV--ALAVDQVFRRTMSKhERREWIehnLARVQM--SHALhKRPGEIS 140
Cdd:PRK10261 391 LSPGKLQALrrdiqfIFQDpyASLDPRQTVGDSImePLRVHGLLPGKAAA-ARVAWL---LERVGLlpEHAW-RYPHEFS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 141 GGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATV 220
Cdd:PRK10261 466 GGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEI 545
|
250 260 270
....*....|....*....|....*....|....*....
gi 556285678 221 GEILAVdLPRPRH--------RVQLADDSRYHhlRQQIL 251
Cdd:PRK10261 546 GPRRAV-FENPQHpytrklmaAVPVADPSRQR--PQRVL 581
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
5.82e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.49 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER- 79
Cdd:PRK11614 2 EKVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 -----AVVFQNHSLLPWLSCFDNvaLAVDQVFRRTMSKHERREWIEHNLARVQMSHalHKRPGEISGGMKQRVGIARALA 154
Cdd:PRK11614 78 mreavAIVPEGRRVFSRMTVEEN--LAMGGFFAERDQFQERIKWVYELFPRLHERR--IQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-215 |
6.70e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.30 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRF------------------NTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTE 62
Cdd:COG1134 1 MSSMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 63 GGLLCDNReIAGPgPERAVVFQNHsllpwLSCFDNValavdqVFRRTMSKHERREwIEHNLARV----QMSHALH---KR 135
Cdd:COG1134 81 GRVEVNGR-VSAL-LELGAGFHPE-----LTGRENI------YLNGRLLGLSRKE-IDEKFDEIvefaELGDFIDqpvKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 136 pgeISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG1134 147 ---YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-215 |
6.77e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.57 E-value: 6.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGL-LCDNreiagPGPER 79
Cdd:PRK13537 4 SVAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGE-----PVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 A--------VVFQNHSLLPWLSCFDNValavdQVFRR--TMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGI 149
Cdd:PRK13537 75 ArharqrvgVVPQFDNLDPDFTVRENL-----LVFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 150 ARALAMKPKVLLLDEPFGALDALTRaHLqdtvmhIQQELNT------TIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQAR-HL------MWERLRSllargkTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-233 |
8.21e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.93 E-value: 8.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 6 QVQAVSQ---RFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKS----TLLNLI--AGITTPTEGGLLCD-NREIAG- 74
Cdd:PRK10261 11 DVLAVENlniAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRrSRQVIEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 75 -----------PGPERAVVFQN--HSLLPWLSCFDNVA--LAVDQVFRRTMSKHERREWIEhnLARVQMSHALHKR-PGE 138
Cdd:PRK10261 91 seqsaaqmrhvRGADMAMIFQEpmTSLNPVFTVGEQIAesIRLHQGASREEAMVEAKRMLD--QVRIPEAQTILSRyPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 139 ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAA 218
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250
....*....|....*
gi 556285678 219 TVGEILAVdLPRPRH 233
Cdd:PRK10261 249 ETGSVEQI-FHAPQH 262
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-215 |
2.14e-23 |
|
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: 94.07 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGE-FLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGPErAVVF 83
Cdd:cd03250 1 ISVEDASFTWDSGEQEtSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG-------SVSVPGSI-AYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 84 QNhsllPWL---SCFDNValavdqVFRRTMSKherrEWIEhnlaRV-----------QMSHALHKRPGE----ISGGMKQ 145
Cdd:cd03250 73 QE----PWIqngTIRENI------LFGKPFDE----ERYE----KVikacalepdleILPDGDLTEIGEkginLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 146 RVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVmhIQQEL--NTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLlnNKTRILVTHQL-QLLPHADQIVVLDNG 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-207 |
3.36e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.22 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRfntaSGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---- 79
Cdd:PRK11831 7 LVDMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlytv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 ----AVVFQNHSLLPWLSCFDNVALAvdqvfrrtMSKHER------REWIEHNLARVQMSHALHKRPGEISGGMKQRVGI 149
Cdd:PRK11831 83 rkrmSMLFQSGALFTDMNVFDNVAYP--------LREHTQlpapllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 150 ARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSD 207
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-249 |
4.06e-23 |
|
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: 94.22 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 20 EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA-----------GPGPERAVVFQNhsl 88
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevtldslrraiGVVPQDTVLFND--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 lpwlSCFDNVALAvdqvfRRTMSKHERREwiehnLARVQMSHALHKR-P-------GE----ISGGMKQRVGIARALAMK 156
Cdd:cd03253 90 ----TIGYNIRYG-----RPDATDEEVIE-----AAKAAQIHDKIMRfPdgydtivGErglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 157 PKVLLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDVDEaVLLSDRVLMMTNGPAATVGeilavdlprpRHRVQ 236
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRIVERG----------THEEL 222
|
250
....*....|...
gi 556285678 237 LADDSRYHHLRQQ 249
Cdd:cd03253 223 LAKGGLYAEMWKA 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-221 |
4.92e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGL---------LCDNREIAGPGPERAVVFQnhslLPWLS 93
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvssTSKQKEIKPVRKKVGVVFQ----FPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAvDQVF---RRTMSKHERREWIEHNLARVQMSHAL-HKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGAL 169
Cdd:PRK13643 97 LFEETVLK-DVAFgpqNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556285678 170 DALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:PRK13643 176 DPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-233 |
5.68e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.47 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASGEFL-----ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA-G 74
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 75 PGPERA----VVFQNHSLLpwLSCFDNVALAVDQVFR--RTMSKHERREWIEHNLARVQM--SHALHkRPGEISGGMKQR 146
Cdd:PRK15112 81 DYSYRSqrirMIFQDPSTS--LNPRQRISQILDFPLRlnTDLEPEQREKQIIETLRQVGLlpDHASY-YPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 147 VGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAV 226
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
....*..
gi 556285678 227 dLPRPRH 233
Cdd:PRK15112 238 -LASPLH 243
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-221 |
6.91e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.96 E-value: 6.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNR-----------EIAGPGPERAVVFQNHSLLPWL 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifqiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 93 SCFDNVALAVDQvfRRTMSKHERREWIEHNLARVQMSHALHKR----PGEISGGMKQRVGIARALAMKPKVLLLDEPFGA 168
Cdd:PRK14246 106 SIYDNIAYPLKS--HGIKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556285678 169 LDALTRAHLQDTVMHIQQELntTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-242 |
7.71e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.42 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERA-----VVFQNHSLLPWLSCFDN 97
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlPLHARArrgigYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VaLAVDQVfRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHL 177
Cdd:PRK10895 99 L-MAVLQI-RDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 178 QDTVMHIqQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVDLPRPRHRVQLADDSR 242
Cdd:PRK10895 177 KRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFR 240
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-247 |
7.97e-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: 93.45 E-value: 7.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG-----PERAVVFQNhSLLPWLSCFDN 97
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrRQIGLVSQD-VFLFNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VALAVDQVFR-------RTMSKHErreWIEhnlarvQMSHALHKRPGE----ISGGMKQRVGIARALAMKPKVLLLDEPF 166
Cdd:cd03251 96 IAYGRPGATReeveeaaRAANAHE---FIM------ELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 167 GALDALTRAHLQDTVMHIQQElNTTIVmITHDvdeavlLS-----DRVLMMTNgpaatvGEILAvdlpRPRHRVQLADDS 241
Cdd:cd03251 167 SALDTESERLVQAALERLMKN-RTTFV-IAHR------LStienaDRIVVLED------GKIVE----RGTHEELLAQGG 228
|
....*.
gi 556285678 242 RYHHLR 247
Cdd:cd03251 229 VYAKLH 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-198 |
8.07e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 8.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNTASGEF-------LALQNVSFDIVEGETISLIGHSGCGKST----LLNLIAgittpTEGGLLCDNRE 71
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 72 IAGPGPER--------AVVFQ--NHSLLPWLSCFDNVALAVdQVFRRTMSKHERREWIEHNLARVQMSHAL-HKRPGEIS 140
Cdd:PRK15134 349 LHNLNRRQllpvrhriQVVFQdpNSSLNPRLNVLQIIEEGL-RVHQPTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFS 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 141 GGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHD 198
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
19-197 |
9.42e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.24 E-value: 9.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQNHS--LLPWLSCFD 96
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRnaMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 97 NVALavdqvFRRTMSKHERRewIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAH 176
Cdd:PRK13539 93 NLEF-----WAAFLGGEELD--IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|.
gi 556285678 177 LQDtVMHIQQELNTTIVMITH 197
Cdd:PRK13539 166 FAE-LIRAHLAQGGIVIAATH 185
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-215 |
1.12e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 92.67 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVVFQNhsllPWL---SC 94
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGVVLQD----TFLfsgTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 95 FDNVALAvdqvfrRTMSKHErrEWIEhNLARVQMSHALHKRP-----------GEISGGMKQRVGIARALAMKPKVLLLD 163
Cdd:cd03254 94 MENIRLG------RPNATDE--EVIE-AAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556285678 164 EPFGALDALTRAHLQDTVMHIQQelNTTIVMITHDVDeAVLLSDRVLMMTNG 215
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-215 |
1.60e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE---RAVVFQNHSLL----------- 89
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlaRRLALLPQHHLtpegitvrelv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 90 -----PWLSCFDnvalavdqvfRRTMSKHERREWiehNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:PRK11231 98 aygrsPWLSLWG----------RLSAEDNARVNQ---AMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556285678 165 PFGALDALTRAHLqdtvMHIQQELNT---TIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK11231 165 PTTYLDINHQVEL----MRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-215 |
1.78e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA----VVF-----QNHSLLPWLS 93
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAiragIAYvpedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAVDQVFRRT--MSKHERREWIEHNLARVQM-SHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPfgald 170
Cdd:COG1129 347 IRENITLASLDRLSRGglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP----- 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556285678 171 alTR-----AHLQdtVMHIQQEL---NTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG1129 422 --TRgidvgAKAE--IYRLIRELaaeGKAVIVISSELPELLGLSDRILVMREG 470
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-260 |
1.85e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.15 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNT-ASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGL----------LCDNREI 72
Cdd:PRK13631 21 ILRVKNLYCVFDEkQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 73 AGPGPER-----------AVVFQnhsllpwlscFDNVALAVDQVFRRTM--------SKHERREWIEHNLARVQMSHA-L 132
Cdd:PRK13631 101 TNPYSKKiknfkelrrrvSMVFQ----------FPEYQLFKDTIEKDIMfgpvalgvKKSEAKKLAKFYLNKMGLDDSyL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 133 HKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMM 212
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVM 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 213 TNGPAATVG---------EILA---VDLPrprHRVQLADDsryhhLRQQILHF--LYEKQPK 260
Cdd:PRK13631 250 DKGKILKTGtpyeiftdqHIINstsIQVP---RVIQVIND-----LIKKDPKYkkLYQKQPR 303
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-215 |
2.95e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.97 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlcdnrEIAGPG--------------PERAVVFQnhslL 89
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI-----TIAGYHitpetgnknlkklrKKVSLVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 90 PWLSCFDNVALAvDQVF---RRTMSKHERREWIEHNLARVQMSHAL-HKRPGEISGGMKQRVGIARALAMKPKVLLLDEP 165
Cdd:PRK13641 94 PEAQLFENTVLK-DVEFgpkNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556285678 166 FGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-215 |
3.52e-22 |
|
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: 90.06 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 20 EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----AVVFQNhsllPWLscF 95
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALssliSVLNQR----PYL--F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNValavdqvfrrtmskherrewIEHNLARvqmshalhkrpgEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRA 175
Cdd:cd03247 88 DTT--------------------LRNNLGR------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556285678 176 HLQDTVMhiQQELNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03247 136 QLLSLIF--EVLKDKTLIWITHHL-TGIEHMDKILFLENG 172
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-225 |
3.73e-22 |
|
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: 95.20 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERavvFQNH-SLLPwlscfDNVALav 102
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE---LGRHiGYLP-----QDVEL-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 dqvFRRTmskherrewIEHNLAR----------------------VQMSHALHKRPGE----ISGGMKQRVGIARALAMK 156
Cdd:COG4618 418 ---FDGT---------IAENIARfgdadpekvvaaaklagvhemiLRLPDGYDTRIGEggarLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 157 PKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVdeAVL-LSDRVLMMTNGPAATVG---EILA 225
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP--SLLaAVDKLLVLRDGRVQAFGprdEVLA 555
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-215 |
5.27e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.46 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASG-EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGG---LLCDNREIAGPGPERA 80
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQNHSLLPWLSCFDNVA-----------LAVDQVFRRT-------------MSKHERREWIEHNLARVQMSHA-LHKR 135
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKeirrrvgvvfqFAEYQLFEQTiekdiifgpvsmgVSKEEAKKRAAKYIELVGLDESyLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 136 PGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-215 |
1.23e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 20 EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER---------AVVFQnhslLP 90
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrkriGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 91 WLSCFD------------NVALAVDQVFRRTMskherREWIEHNLARVQMShalhKRPGEISGGMKQRVGIARALAMKPK 158
Cdd:PRK13646 95 ESQLFEdtvereiifgpkNFKMNLDEVKNYAH-----RLLMDLGFSRDVMS----QSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 159 VLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-221 |
2.90e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 20 EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDN----------REIAGPGPERAVVFQnhslL 89
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlkkiKEVKRLRKEIGLVFQ----F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 90 PWLSCFDNvALAVDQVF---RRTMSKHERREWIEHNLARVQMSHALHKR-PGEISGGMKQRVGIARALAMKPKVLLLDEP 165
Cdd:PRK13645 99 PEYQLFQE-TIEKDIAFgpvNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 166 FGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-215 |
5.27e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.95 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVVFQNHSLLPwLSCFDN 97
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlrrniAVVFQDAGLFN-RSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VAL----AVDQVFRRTMSKHERREWIEHNLARVQMshALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALT 173
Cdd:PRK13657 429 IRVgrpdATDEEMRAAAERAQAHDFIERKPDGYDT--VVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 174 RAHLQ---DTVMHiqqelNTTIVMITH---DVDEAvllsDRVLMMTNG 215
Cdd:PRK13657 507 EAKVKaalDELMK-----GRTTFIIAHrlsTVRNA----DRILVFDNG 545
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-223 |
5.56e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.77 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA 80
Cdd:PRK09700 2 ATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ------VVFQNHSLLPWLSCFDNV---------ALAVDQVFRRTMskherREWIEHNLARVQMSHALHKRPGEISGGMKQ 145
Cdd:PRK09700 78 aqlgigIIYQELSVIDELTVLENLyigrhltkkVCGVNIIDWREM-----RVRAAMMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 146 RVGIARALAMKPKVLLLDEPfgaLDALTRAHLQDTVMHIQQELN--TTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEI 223
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEP---TSSLTNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-198 |
5.63e-21 |
|
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: 91.65 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFNTASgefLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLL-----------CDNR 70
Cdd:TIGR02868 332 KPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvssldqDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 71 EIAGPGPERAVVFQNhsllpwlSCFDNVALAVDQVFRRTMSKHERR----EWIEhnlarvQMSHALHKRPGE----ISGG 142
Cdd:TIGR02868 409 RRVSVCAQDAHLFDT-------TVRENLRLARPDATDEELWAALERvglaDWLR------ALPDGLDTVLGEggarLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 143 MKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELntTIVMITHD 198
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-223 |
7.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 16 TASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVVFQNHSllp 90
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfvGLVFQNPD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 91 wlscfdnvalavDQVFRRTMSKHER---------REWIEHN----LARVQMSHALHKRPGEISGGMKQRVGIARALAMKP 157
Cdd:PRK13652 89 ------------DQIFSPTVEQDIAfgpinlgldEETVAHRvssaLHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG---PAATVGEI 223
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGrivAYGTVEEI 225
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-215 |
9.75e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 89.38 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREiagPGPER-------AVVFQNHSLLPW-LSC 94
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PFKRRkefarriGVVFGQRSQLWWdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 95 FDNVAL--AV----DQVFRRTMskherREWIEhnlaRVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGA 168
Cdd:COG4586 114 IDSFRLlkAIyripDAEYKKRL-----DELVE----LLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556285678 169 LDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG4586 185 LDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-224 |
1.50e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTAsgefLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERA--- 80
Cdd:COG4604 2 IEIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAkrl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 -VVFQNHSLLPWLSCFDNVAlavdqvFRR------TMSKhERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARAL 153
Cdd:COG4604 78 aILRQENHINSRLTVRELVA------FGRfpyskgRLTA-EDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 154 AMKPKVLLLDEPFGALDAltrAHLQDTVMHIQQ---ELNTTIVMITHDVDEAVLLSDRVLMMTNGPAA---TVGEIL 224
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDM---KHSVQMMKLLRRladELGKTVVIVLHDINFASCYADHIVAMKDGRVVaqgTPEEII 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
24-249 |
1.58e-20 |
|
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: 87.21 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIagpgperavvfqnHSL-LPWLScfDNVALaV 102
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-------------RDLnLRWLR--SQIGL-V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 DQ---VFRRTM------SKHER-REWIEH-----NLARVQMS--HALHKRPGE----ISGGMKQRVGIARALAMKPKVLL 161
Cdd:cd03249 83 SQepvLFDGTIaeniryGKPDAtDEEVEEaakkaNIHDFIMSlpDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 162 LDEPFGALDALTRAHLQ---DTVMhiqqeLNTTIVMITHDVdEAVLLSDRVLMMTNGPAATVGeilavdlprpRHRVQLA 238
Cdd:cd03249 163 LDEATSALDAESEKLVQealDRAM-----KGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQG----------THDELMA 226
|
250
....*....|.
gi 556285678 239 DDSRYHHLRQQ 249
Cdd:cd03249 227 QKGVYAKLVKA 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-215 |
1.59e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.07 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAG--ITTPTEGGLLCDNReiagpgPERAVVFQNhsllpwLSCF---DNV 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGR------PLDKRSFRK------IIGYvpqDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 99 ALAVDQVfRRTMSkherrewiehnlarvqmsHALHKRpgEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQ 178
Cdd:cd03213 93 LHPTLTV-RETLM------------------FAAKLR--GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 556285678 179 DTVMHIQQElNTTIVMITHDV-DEAVLLSDRVLMMTNG 215
Cdd:cd03213 152 SLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQG 188
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-239 |
1.66e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 90.55 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEflALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG-----PE 78
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlaslrRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 79 RAVVFQNHSLLPwLSCFDNVALAVdqvfRRTMSKHERREWIEH-NLARV--QMSHALHKRPGE----ISGGMKQRVGIAR 151
Cdd:TIGR02203 408 VALVSQDVVLFN-DTIANNIAYGR----TEQADRAEIERALAAaYAQDFvdKLPLGLDTPIGEngvlLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVmITHDVdEAVLLSDRVLMMTNG---PAATVGEILAVD- 227
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQG-RTTLV-IAHRL-STIEKADRIVVMDDGrivERGTHNELLARNg 559
|
250
....*....|..
gi 556285678 228 LPRPRHRVQLAD 239
Cdd:TIGR02203 560 LYAQLHNMQFRE 571
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-215 |
2.42e-20 |
|
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: 86.39 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNtaSGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER----- 79
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlrsri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNhsllPWLscfdnvalavdqvFRRTM-------SKHERREwIEHNLARVQMSHALHKRPGEI-----------SG 141
Cdd:cd03244 81 SIIPQD----PVL-------------FSGTIrsnldpfGEYSDEE-LWQALERVGLKEFVESLPGGLdtvveeggenlSV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 142 GMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTvmhIQQEL-NTTIVMITHDVDeAVLLSDRVLMMTNG 215
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLD-TIIDSDRILVLDKG 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-250 |
2.56e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.88 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSqrFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGpGPERA- 80
Cdd:PRK11160 336 QVSLTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD-YSEAAl 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 -----VVFQ-----NHSLLpwlscfDNVALAvdqvfrrtmSKHERREWIEHNLARVQMSHALHKRPG----------EIS 140
Cdd:PRK11160 413 rqaisVVSQrvhlfSATLR------DNLLLA---------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 141 GGMKQRVGIARALAMKPKVLLLDEPFGALDALT-RAHLQDTVMHIQqelNTTIVMITHdvdEAVLLS--DRVLMMTNGPA 217
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQ---NKTVLMITH---RLTGLEqfDRICVMDNGQI 551
|
250 260 270
....*....|....*....|....*....|...
gi 556285678 218 ATVGEilavdlprprHRVQLADDSRYHHLRQQI 250
Cdd:PRK11160 552 IEQGT----------HQELLAQQGRYYQLKQRL 574
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-215 |
2.67e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKS-TLLNLIAGITTPT------------EGGLLCDN 69
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypsgdirfhgESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 70 REIAG-PGPERAVVFQNH--SLLPwlscFDNVALAVDQVF--RRTMSKHERREWIEHNLARVQMSHA---LHKRPGEISG 141
Cdd:PRK15134 84 QTLRGvRGNKIAMIFQEPmvSLNP----LHTLEKQLYEVLslHRGMRREAARGEILNCLDRVGIRQAakrLTDYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 142 GMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-233 |
4.68e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.49 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKS-TLLNLIAGITTPteGGLLCDNREIAGP------- 75
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQdlqrise 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 76 -------GPERAVVFQN--HSLLPwlsCFD-----NVALAVDQvfrrTMSKHERREWIEHNLARVQM---SHALHKRPGE 138
Cdd:PRK11022 81 kerrnlvGAEVAMIFQDpmTSLNP---CYTvgfqiMEAIKVHQ----GGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 139 ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAA 218
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
250
....*....|....*.
gi 556285678 219 TVGEilAVDLPR-PRH 233
Cdd:PRK11022 234 ETGK--AHDIFRaPRH 247
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-215 |
5.95e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.75 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITtPTEGGLLCDNREIAGPGPER-----AVVFQNhSLLPWLSCFDNV 98
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrkhlSWVGQN-PQLPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 99 AL----AVDQVFRRTMSKHERREWIEhnlarvQMSHALHKRPGE----ISGGMKQRVGIARALAMKPKVLLLDEPFGALD 170
Cdd:PRK11174 444 LLgnpdASDEQLQQALENAWVSEFLP------LLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 556285678 171 ALTRAHLQDTVMHIQQelNTTIVMITHDVDEavLLS-DRVLMMTNG 215
Cdd:PRK11174 518 AHSEQLVMQALNAASR--RQTTLMVTHQLED--LAQwDQIWVMQDG 559
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-210 |
6.62e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.94 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERa 80
Cdd:PRK09544 1 MTSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 vvfqnhsllpwLSCFDNVALAVDQVFRrtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVL 160
Cdd:PRK09544 76 -----------LYLDTTLPLTVNRFLR--LRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556285678 161 LLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVL 210
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-248 |
1.36e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 87.85 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 22 LALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVVFQNHSLLPwLSCFD 96
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlrqgvAMVQQDPVVLA-DTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 97 NVALAvdqvfrRTMSkhERREWieHNLARVQ-------MSHALHKRPGE----ISGGMKQRVGIARALAMKPKVLLLDEP 165
Cdd:PRK10790 434 NVTLG------RDIS--EEQVW--QALETVQlaelarsLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 166 FGALDALTRAHLQDTVMHIQQelNTTIVMITHDVdEAVLLSDRVLMMTNGPAATVGeilavdlprpRHRVQLADDSRYHH 245
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVRE--HTTLVVIAHRL-STIVEADTILVLHRGQAVEQG----------THQQLLAAQGRYWQ 570
|
...
gi 556285678 246 LRQ 248
Cdd:PRK10790 571 MYQ 573
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-215 |
2.96e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 86.99 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 26 NVSFdiVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAgpgPERAVVFQNHSLLPWLSC-FDNVALAVDQ 104
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE---TNLDAVRQSLGMCPQHNIlFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 105 VFrrtMSKHERREWIEhnlARVQMSHAL------HKRPGE---ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRA 175
Cdd:TIGR01257 1025 LF---YAQLKGRSWEE---AQLEMEAMLedtglhHKRNEEaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 556285678 176 HLQDTVMHIQQelNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR01257 1099 SIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-222 |
3.07e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLL------CDNREIAGPGPERAVVFQNHSllpwlSCFD 96
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgidtGDFSKLQGIRKLVGIVFQNPE-----TQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 97 NVALAVDQVF---RRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALT 173
Cdd:PRK13644 92 GRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556285678 174 RAHLQDTVMHIQQElNTTIVMITHDVDEaVLLSDRVLMMTNGPAATVGE 222
Cdd:PRK13644 172 GIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGE 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-215 |
3.14e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCdnreIAGPGPERA---- 80
Cdd:PRK13536 42 IDLAGVSKSY----GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARArlar 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ----VVFQNHSLLPWLSCFDNVaLAVDQVFRrtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMK 156
Cdd:PRK13536 114 arigVVPQFDNLDLEFTVRENL-LVFGRYFG--MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 157 PKVLLLDEPFGALDALTRaHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13536 191 PQLLILDEPTTGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-246 |
6.62e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.84 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 20 EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI-----AGPGPERAVVFQNHSLlpwlsc 94
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdytlASLRNQVALVSQNVHL------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 95 F-----DNVALAVDQVFrrtmskheRREWIEHnLARV--------QMSHALHKRPGE----ISGGMKQRVGIARALAMKP 157
Cdd:PRK11176 429 FndtiaNNIAYARTEQY--------SREQIEE-AARMayamdfinKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQelNTTIVMITH------DVDEAVLLSDrvlmmtngpaatvGEILAvdlpRP 231
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHrlstieKADEILVVED-------------GEIVE----RG 560
|
250
....*....|....*
gi 556285678 232 RHRVQLADDSRYHHL 246
Cdd:PRK11176 561 THAELLAQNGVYAQL 575
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-178 |
1.17e-18 |
|
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: 81.25 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIA--GPGPERAVVFQNHS--LLPWLSC 94
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeqRDEPHENILYLGHLpgLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 95 FDNValavdQVFRRTMSKHERRewIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALD---- 170
Cdd:TIGR01189 91 LENL-----HFWAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagv 163
|
170
....*....|..
gi 556285678 171 ----ALTRAHLQ 178
Cdd:TIGR01189 164 allaGLLRAHLA 175
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-215 |
1.34e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGP-----GP 77
Cdd:PRK09536 2 PMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsaraaSR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERAVVFQNHSLlpwlsCFDnvaLAVDQVFRRTMSKHERR--EW-------IEHNLARVQMSHALHKRPGEISGGMKQRVG 148
Cdd:PRK09536 78 RVASVPQDTSL-----SFE---FDVRQVVEMGRTPHRSRfdTWtetdraaVERAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 149 IARALAMKPKVLLLDEPFGALDaltrAHLQDTVMHIQQEL---NTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLD----INHQVRTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-226 |
1.42e-18 |
|
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: 84.47 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITT--PTEGGLL-----CDNREIAGPgP 77
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalCEKCGYVER-P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERA---------------VVFQNHSLlpwlSCFDNVALAVDQVFRRTMSKHERREWIEHNL------------------- 123
Cdd:TIGR03269 76 SKVgepcpvcggtlepeeVDFWNLSD----KLRRRIRKRIAIMLQRTFALYGDDTVLDNVLealeeigyegkeavgravd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 124 --ARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDE 201
Cdd:TIGR03269 152 liEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*
gi 556285678 202 AVLLSDRVLMMTNGPAATVGEILAV 226
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-235 |
1.53e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 26 NVSFDIVEGETISLIGHSGCGKS----TLLNLIAGITTPTEGGLLCDNREIAG---PGPERAVVFQNHSllpwlSCFDNV 98
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPcalRGRKIATIMQNPR-----SAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 99 alavdqvfrRTMSKHERrewiEHNLAR------VQMSHALH-------KR-----PGEISGGMKQRVGIARALAMKPKVL 160
Cdd:PRK10418 96 ---------HTMHTHAR----ETCLALgkpaddATLTAALEavglenaARvlklyPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 161 LLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVdLPRPRHRV 235
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL-FNAPKHAV 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-223 |
2.22e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntaSGeFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA 80
Cdd:PRK15439 8 APPLLCARSISKQY---SG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ------VVFQNHSLLPWLSCFDNVAlavdqvFRrtMSKHERR-EWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARAL 153
Cdd:PRK15439 84 hqlgiyLVPQEPLLFPNLSVKENIL------FG--LPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 154 AMKPKVLLLDEPFGaldALTRAHLQDTVMHIQ--QELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEI 223
Cdd:PRK15439 156 MRDSRILILDEPTA---SLTPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-198 |
2.40e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGPERAVVFQ 84
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-------IVTWGSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 85 nhsllpwlscfdnvalavdqvfrrtmskherrewiehnlarvQMshalhkrpgeiSGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:cd03221 70 ------------------------------------------QL-----------SGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190
....*....|....*....|....*....|....
gi 556285678 165 PFGALDALTRAHLQDTVmhiqQELNTTIVMITHD 198
Cdd:cd03221 97 PTNHLDLESIEALEEAL----KEYPGTVILVSHD 126
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-215 |
2.56e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASgeflALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA 80
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 ------VVFQNHSLLPWLSCFDNVALAvdqvfRRTMSKHERREWIEHN------LARVQMSHALHKRPGEISGGMKQRVG 148
Cdd:PRK10762 77 qeagigIIHQELNLIPQLTIAENIFLG-----REFVNRFGRIDWKKMYaeadklLARLNLRFSSDKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 149 IARALAMKPKVLLLDEPfgaLDALTrahlqDT-------VMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK10762 152 IAKVLSFESKVIIMDEP---TDALT-----DTeteslfrVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-219 |
2.84e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPG-PERAVVFQNhsLLPWLSCFDNV--- 98
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-------KISILGqPTRQALQKN--LVAYVPQSEEVdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 99 --ALAVDQV---------FRRTMSKHERrEWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFG 167
Cdd:PRK15056 93 fpVLVEDVVmmgryghmgWLRRAKKRDR-QIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 168 ALDALTRAHLQDTVMHIQQELNTTIVMiTHDVDEAVLLSDRVLM-----MTNGPAAT 219
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVS-THNLGSVTEFCDYTVMvkgtvLASGPTET 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-222 |
4.25e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLC-------DNREIAGPGPERAVVFQNHSLLPWLSCFD 96
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgkpldySKRGLLALRQQVATVFQDPEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 97 --------NVALAVDQVFRRtmskherrewIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGA 168
Cdd:PRK13638 97 sdiafslrNLGVPEAEITRR----------VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556285678 169 LDALTRAHLQDTVMHIQQELNtTIVMITHDVDEAVLLSDRVLMMTNGPAATVGE 222
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-230 |
5.28e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.25 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEG------GLLCDNREIAGPGPE 78
Cdd:NF033858 2 ARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGrvevlgGDMADARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 79 RAVVFQ--NHSLLPWLSCFDNValavdQVFRRT--MSKHERREWIEHNLARVQMsHALHKRP-GEISGGMKQRVGIARAL 153
Cdd:NF033858 78 IAYMPQglGKNLYPTLSVFENL-----DFFGRLfgQDAAERRRRIDELLRATGL-APFADRPaGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 154 AMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMI-THDVDEAVLLsDRVLMMTNgpaatvGEILAVDLPR 230
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMSVLVaTAYMEEAERF-DWLVAMDA------GRVLATGTPA 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-230 |
7.68e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 16 TASGEFLaLQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGPERAVVFQNHSLLPWLS-- 93
Cdd:COG4178 372 TPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-------RIARPAGARVLFLPQRPYLPLGTlr 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 ---CFDNVALAVDqvfrrtmskherREWIEHNLARVQMSHaLHKRPGEI-------SGGMKQRVGIARALAMKPKVLLLD 163
Cdd:COG4178 444 ealLYPATAEAFS------------DAELREALEAVGLGH-LAERLDEEadwdqvlSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 164 EPFGALDALTRAHLQDtvmHIQQEL-NTTIVMITHdvdEAVLLS--DRVLMMTNGPAatvGEILAVDLPR 230
Cdd:COG4178 511 EATSALDEENEAALYQ---LLREELpGTTVISVGH---RSTLAAfhDRVLELTGDGS---WQLLPAEAPA 571
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
7-215 |
3.12e-17 |
|
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: 78.14 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 7 VQAVSQRFNTASGeFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQNH 86
Cdd:cd03290 1 VQVTNGYFSWGSG-LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 87 SLL-----PWLScfdNVALAVDQVFRRTMSKHERREWIEhnLARVQ-----MSHALHKRPGE----ISGGMKQRVGIARA 152
Cdd:cd03290 80 SVAyaaqkPWLL---NATVEENITFGSPFNKQRYKAVTD--ACSLQpdidlLPFGDQTEIGErginLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 153 LAMKPKVLLLDEPFGALDALTRAHL-QDTVMHIQQELNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
3-233 |
3.86e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.56 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGIT---------------------TPT 61
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwhvtadrfrwngidllklSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 62 EggllcdNREIAGPgpERAVVFQNHSllpwlSCFDNVALAVDQVFRRTMSKHERREWIEHNLARVQMSHAL--------H 133
Cdd:COG4170 82 E------RRKIIGR--EIAMIFQEPS-----SCLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIELlhrvgikdH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 134 KR-----PGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDR 208
Cdd:COG4170 149 KDimnsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADT 228
|
250 260
....*....|....*....|....*...
gi 556285678 209 VLMMTNGPAATVG---EILAvdlpRPRH 233
Cdd:COG4170 229 ITVLYCGQTVESGpteQILK----SPHH 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-211 |
8.25e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 8.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 6 QVQAVSQRFNTAS--GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGittpteggllcdnREIAGPGPERAVVF 83
Cdd:COG2401 26 RVAIVLEAFGVELrvVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-------------ALKGTPVAGCVDVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 84 QNHsllpwlscFDNVALAVDQVFRRTmSKHERREWiehnLARVQMSHA--LHKRPGEISGGMKQRVGIARALAMKPKVLL 161
Cdd:COG2401 93 DNQ--------FGREASLIDAIGRKG-DFKDAVEL----LNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556285678 162 LDEpFGA-LDALTRAHLQDTVMHIQQELNTTIVMITHDVD-EAVLLSDRVLM 211
Cdd:COG2401 160 IDE-FCShLDRQTAKRVARNLQKLARRAGITLVVATHHYDvIDDLQPDLLIF 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-215 |
9.57e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 9.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlcdnreIAGPGPERAV 81
Cdd:COG0488 313 KKVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------KLGETVKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 82 VFQNHSLL-PWLSCFDNVALAVDQvfrrtMSKHERREWiehnLARVQMSHA-LHKRPGEISGGMKQRVGIARALAMKPKV 159
Cdd:COG0488 383 FDQHQEELdPDKTVLDELRDGAPG-----GTEQEVRGY----LGRFLFSGDdAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 160 LLLDEPFGALDALTRAHLQDTvmhiqqeLNT---TIVMITHD---VDEavlLSDRVLMMTNG 215
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEA-------LDDfpgTVLLVSHDryfLDR---VATRILEFEDG 505
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-215 |
9.59e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 79.32 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSqrfntasGEflALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP---- 77
Cdd:PRK15439 266 APVLTVEDLT-------GE--GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrl 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERAVVF-----QNHSL-----LPWLSCfdnvALAVDQ--VFRRTMSKHERREWIEHNLArVQMSHAlHKRPGEISGGMKQ 145
Cdd:PRK15439 337 ARGLVYlpedrQSSGLyldapLAWNVC----ALTHNRrgFWIKPARENAVLERYRRALN-IKFNHA-EQAARTLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 146 RVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK15439 411 KVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-190 |
9.98e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.38 E-value: 9.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASgEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIagpgpera 80
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL-------- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 81 VVFQNHSLlpwlscFDNVALaVDQ---VFRRTMskherREWIEHNL---------ARVQMSHA----------LHKRPGE 138
Cdd:TIGR00958 546 VQYDHHYL------HRQVAL-VGQepvLFSGSV-----RENIAYGLtdtpdeeimAAAKAANAhdfimefpngYDTEVGE 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 139 ----ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQD-------TVMHIQQELNT 190
Cdd:TIGR00958 614 kgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQEsrsrasrTVLLIAHRLST 676
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-215 |
1.14e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 78.31 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTpteggllcDNREIAG-------- 74
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK--------DNWRVTAdrmrfddi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 75 ------PGPERAVVFQNHSLL---PWlSCFD---NVALAVDQVFRRTMSK---HERREW-----IE--HNLARVQMSHAL 132
Cdd:PRK15093 74 dllrlsPRERRKLVGHNVSMIfqePQ-SCLDpseRVGRQLMQNIPGWTYKgrwWQRFGWrkrraIEllHRVGIKDHKDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 133 HKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMM 212
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
...
gi 556285678 213 TNG 215
Cdd:PRK15093 233 YCG 235
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
14-223 |
1.25e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 79.16 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 14 FNTASGEF-LALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlcdnrEIAGPGperAVVFQNHSLLPWL 92
Cdd:PRK13545 29 FRSKDGEYhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSA---ALIAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 93 SCFDNVALavdQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALD-A 171
Cdd:PRK13545 101 TGIENIEL---KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 556285678 172 LTRAHLQDtvMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEI 223
Cdd:PRK13545 178 FTKKCLDK--MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDI 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-215 |
1.44e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.80 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGItTPTEGGLLCDNREIAG-PGPE----RAVVFQNHSLLPWLSCFDNV 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwSAAElarhRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 99 ALAVDQVFRRTMSKHErrewIEHNLARVQMSHALHKRPGEISGGMKQRVGIARAL-----AMKP--KVLLLDEPFGALDA 171
Cdd:COG4138 91 ALHQPAGASSEAVEQL----LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556285678 172 LTRAHLQDTVMHIQQeLNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:COG4138 167 AQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-215 |
1.97e-16 |
|
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: 75.97 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFNTASgEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCD------------ 68
Cdd:cd03248 8 LKGIVKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpisqyehkyl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 69 NREIAGPGPErAVVFQNhsllpwlSCFDNVALAVDQV-FRRTM---SKHERREWIEhnlarvQMSHALHKRPGE----IS 140
Cdd:cd03248 87 HSKVSLVGQE-PVLFAR-------SLQDNIAYGLQSCsFECVKeaaQKAHAHSFIS------ELASGYDTEVGEkgsqLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 141 GGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDtvMHIQQELNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQ--ALYDWPERRTVLVIAHRL-STVERADQILVLDGG 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-215 |
3.93e-16 |
|
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: 74.76 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVVFQNHSLLpwlscfdn 97
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlrsslTIIPQDPTLF-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 valavDQVFRRTMSkherrewIEHNLARVQMSHALHKRPG--EISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRA 175
Cdd:cd03369 95 -----SGTIRSNLD-------PFDEYSDEEIYGALRVSEGglNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556285678 176 HLQDTvmhIQQEL-NTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03369 163 LIQKT---IREEFtNSTILTIAHRL-RTIIDYDKILVMDAG 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-198 |
5.50e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.90 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnREIAGPGPERAVVFQNHSLLPWLSCFDNVALAV- 102
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------EARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 -------------------DQVFRRTMSKHER-REWIE----HNLAR---VQMsHALHKRPGE-----ISGGMKQRVGIA 150
Cdd:TIGR03719 95 eikdaldrfneisakyaepDADFDKLAAEQAElQEIIDaadaWDLDSqleIAM-DALRCPPWDadvtkLSGGERRRVALC 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 151 RALAMKPKVLLLDEPFGALDALTRAHLQdtvmHIQQELNTTIVMITHD 198
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLDAESVAWLE----RHLQEYPGTVVAVTHD 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-197 |
6.85e-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: 74.07 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 17 ASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE--RAVVFQNHS--LLPWL 92
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiaRGLLYLGHApgIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 93 SCFDNValavdQVFRRTMSkherREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDAL 172
Cdd:cd03231 89 SVLENL-----RFWHADHS----DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*.
gi 556285678 173 TRAHLQDTVM-HIQQelNTTIVMITH 197
Cdd:cd03231 160 GVARFAEAMAgHCAR--GGMVVLTTH 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-209 |
9.92e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 9.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 13 RFNTASGEF---LALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI----------AGPgper 79
Cdd:PRK11288 6 SFDGIGKTFpgvKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaAGV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 AVVFQNHSLLPWLSCFDNVALA--------VDqvfRRTMSKHERREwiehnLARVQMSHALHKRPGEISGGMKQRVGIAR 151
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGqlphkggiVN---RRLLNYEAREQ-----LEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRV 209
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAI 210
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-233 |
1.42e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPT--------EGGLLCDNREIAGPGPE-----RAVVFQNHSLLP 90
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPrlarlRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 91 WLSCFDNVALAVDQVFRRT-MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAM---------KPKVL 160
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAgALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556285678 161 LLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGpaATVGEILAVDLPRPRH 233
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADG--AIVAHGAPADVLTPAH 247
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-215 |
1.42e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 22 LALQNVSF--------------DIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVV 82
Cdd:PRK10522 323 LELRNVTFayqdngfsvgpinlTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyrklfSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 83 FQNHSLLPWLSCFDNVALAVDQVFrrtmskherrEWiehnLARVQMSHALHKRPGEI-----SGGMKQRVGIARALAMKP 157
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPANPALVE----------KW----LERLKMAHKLELEDGRIsnlklSKGQKKRLALLLALAEER 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDvDEAVLLSDRVLMMTNG 215
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNG 525
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-249 |
1.52e-15 |
|
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: 75.63 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIagpgpeRAVvfQNHSLlpwlscfdNVALAV- 102
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI------RDV--TQASL--------RAAIGIv 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 --DQV-FRRTmskherrewIEHNLA--RVQMSHA----------LHK-----------RPGE----ISGGMKQRVGIARA 152
Cdd:COG5265 438 pqDTVlFNDT---------IAYNIAygRPDASEEeveaaaraaqIHDfieslpdgydtRVGErglkLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 153 LAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVmITH------DVDEAVLLSDrvlmmtngpaatvGEILAv 226
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLV-IAHrlstivDADEILVLEA-------------GRIVE- 572
|
250 260
....*....|....*....|....*
gi 556285678 227 dlpRPRHRVQLADDSRYHHL--RQQ 249
Cdd:COG5265 573 ---RGTHAELLAQGGLYAQMwaRQQ 594
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-215 |
1.89e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 75.55 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGeflALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG-------- 76
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDrhtlrqfi 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 ---PERAVVFQNhsllpwlSCFDNVAL-----AVDQVFRRTMSKHERREWIEhnlarvQMSHALHKRPGE----ISGGMK 144
Cdd:TIGR01193 551 nylPQEPYIFSG-------SILENLLLgakenVSQDEIWAACEIAEIKDDIE------NMPLGYQTELSEegssISGGQK 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 145 QRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElntTIVMITHDVDEAVlLSDRVLMMTNG 215
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAK-QSDKIIVLDHG 684
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
2.39e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 1 MKPLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITtPT---EGGLLCDNREIAGPG- 76
Cdd:PRK13549 2 MEYLLEMKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 --PERA---VVFQNHSLLPWLSCFDNVALAvdqvfrRTMSKHERREWIEHN------LARVQMSHALHKRPGEISGGMKQ 145
Cdd:PRK13549 77 rdTERAgiaIIHQELALVKELSVLENIFLG------NEITPGGIMDYDAMYlraqklLAQLKLDINPATPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 146 RVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG------PAAT 219
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGrhigtrPAAG 229
|
...
gi 556285678 220 VGE 222
Cdd:PRK13549 230 MTE 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-215 |
3.00e-15 |
|
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: 74.86 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 4 LIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITT--PTEGGLLCDNREIAGPG---PE 78
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNirdTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 79 RA---VVFQNHSLLPWLSCFDNVALAVDQVFRRTMSKHERREWIEHNLAR-VQMSHALHKRP-GEISGGMKQRVGIARAL 153
Cdd:TIGR02633 77 RAgivIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLReLQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 154 AMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-243 |
3.25e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.59 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEG-----------GLLCDNREIAGPGPERAVVFQNHSLLPwL 92
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggRSIFNYRDVLEFRRRVGMLFQRPNPFP-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 93 SCFDNVALAVDQvfRRTMSKHERREWIEHNLARVQMSHALHKR----PGEISGGMKQRVGIARALAMKPKVLLLDEPFGA 168
Cdd:PRK14271 116 SIMDNVLAGVRA--HKLVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 169 LDALTRAHLQDTVMHIQQELntTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILAVdLPRPRHrvqlADDSRY 243
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL-FSSPKH----AETARY 261
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-197 |
3.69e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGIT--TPTEGGLLCDNREIAGPGP-ERA-----VVFQNHSLLPWLSCF 95
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPdERAragifLAFQYPVEIPGVSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVALAVDQVFRRTMSKHERREWIEHNLARVQMSHALHKRP--GEISGGMKQRVGIARALAMKPKVLLLDEPFGALD--A 171
Cdd:COG0396 96 NFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidA 175
|
170 180
....*....|....*....|....*.
gi 556285678 172 LtRAhLQDTVMHIQQElNTTIVMITH 197
Cdd:COG0396 176 L-RI-VAEGVNKLRSP-DRGILIITH 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-217 |
3.78e-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: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 30 DIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAgpgperavvFQNHSLLPwlscfDNVALAVDQVFRRT 109
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKA-----DYEGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 110 MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELN 189
Cdd:cd03237 87 KDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|....*...
gi 556285678 190 TTIVMITHDVDEAVLLSDRVLMMTNGPA 217
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-221 |
2.66e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.00 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAG-ITTPTEGGllcDNREIAGPGPER-------AVVFQNHSLLPWLSCF 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKGS---GSVLLNGMPIDAkemraisAYVQQDDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DnvALAVDQVFR--RTMSKHERREWIEHNLARVQMSHALHKRPGE------ISGGMKQRVGIARALAMKPKVLLLDEPFG 167
Cdd:TIGR00955 118 E--HLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556285678 168 ALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG 221
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-197 |
3.29e-14 |
|
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: 68.33 E-value: 3.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSqrFNTASGEFLaLQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCdnreiagpgPERAVVFq 84
Cdd:cd03223 1 IELENLS--LATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLL- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 85 nhsLLPWLSCFDNVALavdqvfrrtmskherrewiehnlaRVQMSHALHKrpgEISGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:cd03223 68 ---FLPQRPYLPLGTL------------------------REQLIYPWDD---VLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|...
gi 556285678 165 PFGALDALTrahlQDTVMHIQQELNTTIVMITH 197
Cdd:cd03223 118 ATSALDEES----EDRLYQLLKELGITVISVGH 146
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-215 |
3.84e-14 |
|
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: 71.39 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 26 NVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPT-EGGLLCDNREIAGPGPERAVVF---------QNHSLLPWLSCF 95
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAgiamvpedrKRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVALAVDQVFRRTMSKHERREW--IEHNLARVQMSHALHKRP-GEISGGMKQRVGIARALAMKPKVLLLDEPFGALDAL 172
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 556285678 173 TRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR02633 438 AKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-209 |
4.35e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITtPT---EG-----GLLCDNREIAGPgpERA---VVFQNHSLLPW 91
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGeilfdGEVCRFKDIRDS--EALgivIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 92 LSCFDNVALAVDQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDA 171
Cdd:NF040905 93 LSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNE 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 556285678 172 LTRAHLQDTVMHIQQELNTTIvMITHDVDEAVLLSDRV 209
Cdd:NF040905 173 EDSAALLDLLLELKAQGITSI-IISHKLNEIRRVADSI 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
24-222 |
5.24e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.45 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPT--EGGLLCDNREIAGPGPER-AVVFQNHSLLPWLSCFDNVAL 100
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 101 AVDQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGE-----ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRA 175
Cdd:PLN03211 164 CSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 176 HLQDTVMHIQQElNTTIVMITHDVDEAVL-LSDRVLMMTNGPAATVGE 222
Cdd:PLN03211 244 RLVLTLGSLAQK-GKTIVTSMHQPSSRVYqMFDSVLVLSEGRCLFFGK 290
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-215 |
6.52e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 2 KPLIQVQAVSQRfntASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGP---- 77
Cdd:COG3845 255 EVVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrerr 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERAVVF-----QNHSLLPWLSCFDNVALavDQVFRRTMSkheRREWIEHNLARvqmSHALHK------RPGEI------- 139
Cdd:COG3845 332 RLGVAYipedrLGRGLVPDMSVAENLIL--GRYRRPPFS---RGGFLDRKAIR---AFAEELieefdvRTPGPdtparsl 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 140 SGGMKQRVGIARALAMKPKVLLLDEPFGALDAltrahlqDTVMHIQQEL------NTTIVMITHDVDEAVLLSDRVLMMT 213
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDV-------GAIEFIHQRLlelrdaGAAVLLISEDLDEILALSDRIAVMY 476
|
..
gi 556285678 214 NG 215
Cdd:COG3845 477 EG 478
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-228 |
1.11e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREI---AGPGPERAV--VFQNHSLLPWLS 93
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyASKEVARRIglLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAV---DQVFRRTmsKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALD 170
Cdd:PRK10253 98 VQELVARGRyphQPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556285678 171 ALTRAHLQDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVG---EILAVDL 228
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGapkEIVTAEL 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-229 |
1.35e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEG-----GLLCDNREIAgpgP 77
Cdd:NF033858 265 PAIEARGLTMRF----GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeawlfGQPVDAGDIA---T 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 78 ERAVVF--QNHSLLPWLSCFDNVAL-AvdQVFRrtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALA 154
Cdd:NF033858 338 RRRVGYmsQAFSLYGELTVRQNLELhA--RLFH--LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVDEAvLLSDRVLMMtngpaaTVGEILAVDLP 229
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLM------HAGRVLASDTP 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-197 |
1.52e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 25 QNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDN------------REIAGPGPERAVVFQN------- 85
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwRSKIGVVSQDPLLFSNsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 86 ---HSL--LPWL-------------------SCFDNVALAVDQVFRRTMSK---HERREW--IEH----NLARVQMSH-- 130
Cdd:PTZ00265 482 yslYSLkdLEALsnyynedgndsqenknkrnSCRAKCAGDLNDMSNTTDSNeliEMRKNYqtIKDsevvDVSKKVLIHdf 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 131 --ALHKR--------PGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITH 197
Cdd:PTZ00265 562 vsALPDKyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-215 |
2.00e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 26 NVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERA----VVF-----QNHSLLPWLSCFD 96
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangIVYisedrKRDGLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 97 NVALAVDQVFRRTMSKherrewIEHNLARVQMSHALH----KRP------GEISGGMKQRVGIARALAMKPKVLLLDEPF 166
Cdd:PRK10762 350 NMSLTALRYFSRAGGS------LKHADEQQAVSDFIRlfniKTPsmeqaiGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556285678 167 GALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-212 |
2.07e-13 |
|
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: 69.94 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTpTEGGLLCDnreiagpgperAVVFQNHSLLPWLSCFDNVALAV- 102
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID-----------GVSWNSVTLQTWRKAFGVIPQKVf 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 --DQVFRRTMSKHERreWIEHNLARVQ----MSHALHKRPGEI-----------SGGMKQRVGIARALAMKPKVLLLDEP 165
Cdd:TIGR01271 1303 ifSGTFRKNLDPYEQ--WSDEEIWKVAeevgLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556285678 166 FGALDALTRAHLQDTVMHIQQelNTTIVMITHDVdEAVLLSDRVLMM 212
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQSFS--NCTVILSEHRV-EALLECQQFLVI 1424
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-199 |
5.03e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.15 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 21 FLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGpERAVVFQNHSLLPWLSCFDNVAL 100
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-------KVDRNG-EVSVIAISAGLSGQLTGIENIEF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 101 AVDQV-FRRTMSKHERREWIEHNlarvQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEpfgALDALTRAHLQD 179
Cdd:PRK13546 109 KMLCMgFKRKEIKAMTPKIIEFS----ELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQK 181
|
170 180
....*....|....*....|..
gi 556285678 180 TVMHIQQ--ELNTTIVMITHDV 199
Cdd:PRK13546 182 CLDKIYEfkEQNKTIFFVSHNL 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-229 |
5.21e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 15 NTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV------VFQN--- 85
Cdd:PRK09700 270 NVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVkkgmayITESrrd 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 86 HSLLPWLSCFDNVALA---VDQVFRRTM---SKHERREWIEHNLARVQMS-HALHKRPGEISGGMKQRVGIARALAMKPK 158
Cdd:PRK09700 350 NGFFPNFSIAQNMAISrslKDGGYKGAMglfHEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 159 VLLLDEPFGALDALTRAHLQdTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMM---------TNGPAATVGEILAVDLP 229
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIY-KVMRQLADDGKVILMVSSELPEIITVCDRIAVFcegrltqilTNRDDMSEEEIMAWALP 508
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-215 |
6.45e-13 |
|
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: 65.75 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 20 EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnreiagpgPERAVVFQNHSLLPwlscfdnva 99
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVS-------------VEGDIHYNGIPYKE--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 100 laVDQVFRRTMSKHERREWIEHNLA-RVQMSHALHKRPGE----ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTR 174
Cdd:cd03233 77 --FAEKYPGEIIYVSEEDVHFPTLTvRETLDFALRCKGNEfvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 556285678 175 AHLQDTVMHIQQELN-TTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:cd03233 155 LEILKCIRTMADVLKtTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-223 |
7.47e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.12 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 34 GETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPEravVFQNHSLLPWLSCFDNVALAVDQVFRRTMSKH 113
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 114 ERREWIEH----NLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQElN 189
Cdd:TIGR01257 2042 VPAEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-G 2120
|
170 180 190
....*....|....*....|....*....|....
gi 556285678 190 TTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEI 223
Cdd:TIGR01257 2121 RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI 2154
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-215 |
8.96e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPE---RAVVFQNHSL------------ 88
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYLPQQLpaaegmtvrelv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 ----LPWlscfdNVALAVdqvFRRtmskhERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDE 164
Cdd:PRK10575 107 aigrYPW-----HGALGR---FGA-----ADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 556285678 165 PFGALDAltrAHLQDTVMHIQ---QELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK10575 174 PTSALDI---AHQVDVLALVHrlsQERGLTVIAVLHDINMAARYCDYLVALRGG 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-215 |
1.41e-12 |
|
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: 63.55 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 34 GETISLIGHSGCGKSTLLNLIAGITTPTEGGLLcdnrEIAGpgperavvfqnhsllpwlscfdnvalavdqvfrrtmskh 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI----YIDG--------------------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 114 errEWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTV-----MHIQQEL 188
Cdd:smart00382 39 ---EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|..
gi 556285678 189 NTTIVMITHDV-----DEAVLLSDRVLMMTNG 215
Cdd:smart00382 116 NLTVILTTNDEkdlgpALLRRRFDRRIVLLLI 147
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-215 |
4.00e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 27 VSFDIVEGETISLIGHSGCGKSTLLNLIAGiTTPTEGGLLCDNREIAG-PGPE----RAVVFQNHSLLPWLSCFDNVALA 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAwSAAElarhRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 102 VDQVFRRTMSKHERREWIEhnlaRVQMSHALHKRPGEISGGMKQRVGIARAL-----AMKP--KVLLLDEPFGALDALTR 174
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAE----ALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556285678 175 AHLqDTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK03695 170 AAL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
139-214 |
6.30e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 6.30e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 139 ISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVMITHDVdEAVLLSDRVLMMTN 214
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1433
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-197 |
7.20e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERavvfqNHSLL--------- 89
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-----HQDLLylghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 90 PWLSCFDNVAlavdqvFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGAL 169
Cdd:PRK13538 87 TELTALENLR------FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190
....*....|....*....|....*....|..
gi 556285678 170 D----ALTRAHLQDtvmHIQQelNTTIVMITH 197
Cdd:PRK13538 161 DkqgvARLEALLAQ---HAEQ--GGMVILTTH 187
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-197 |
9.15e-12 |
|
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: 64.77 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 16 TASGEFLaLQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGItTPTEGGLLCDnreiagpgPERAVVFqnhsLLPWLSCF 95
Cdd:TIGR00954 461 TPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTK--------PAKGKLF----YVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVAL--------AVDQVFRRTMSKHErrewIEHNLARVQMSHALHKRPG---------EISGGMKQRVGIARALAMKPK 158
Cdd:TIGR00954 527 TLGTLrdqiiypdSSEDMKRRGLSDKD----LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*....
gi 556285678 159 VLLLDEPFGALDaltrAHLQDTVMHIQQELNTTIVMITH 197
Cdd:TIGR00954 603 FAILDECTSAVS----VDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-215 |
1.16e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 63.33 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTpTEGGLLCDnreiagpgperAVVFQNHSLLPWLSCFDNVALAV- 102
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQID-----------GVSWNSVPLQKWRKAFGVIPQKVf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 --DQVFRRTMSKHERreWIEHNLARVQ----MSHALHKRPGEI-----------SGGMKQRVGIARALAMKPKVLLLDEP 165
Cdd:cd03289 88 ifSGTFRKNLDPYGK--WSDEEIWKVAeevgLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556285678 166 FGALDALTRAHLQDTVMHIQQelNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQAFA--DCTVILSEHRI-EAMLECQRFLVIEEN 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-227 |
1.39e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.20 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 14 FNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPG-----PERAVVfQNHSL 88
Cdd:TIGR00957 644 FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG-------HVHMKGsvayvPQQAWI-QNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 LpwlscfDNValavdqVFRRTMSKHERREWIEHN--LARVQM-----SHALHKRPGEISGGMKQRVGIARALAMKPKVLL 161
Cdd:TIGR00957 716 R------ENI------LFGKALNEKYYQQVLEACalLPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 162 LDEPFGALDALTRAHLQDTVMHIQQEL-NTTIVMITHDVdEAVLLSDRVLMMTNGPAATVG---EILAVD 227
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHIFEHVIGPEGVLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGsyqELLQRD 852
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-215 |
1.42e-11 |
|
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: 61.77 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGI--TTPTEGGLLCDNREIAGPGP-ERA-----VVFQNHSLLPWLScF 95
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERArlgifLAFQYPPEIPGVK-N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVALAVDQVFrrtmskherrewiehnlarvqmshalhkrpgeiSGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRA 175
Cdd:cd03217 95 ADFLRYVNEGF---------------------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556285678 176 HLQDTVMHIQQElNTTIVMITHDVDEAVLL-SDRVLMMTNG 215
Cdd:cd03217 142 LVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDG 181
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-226 |
5.08e-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: 60.03 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIagittpteggllcdnreIAGPGPERAVvfqnhSLLPwlSCFDNVALAV 102
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-----------------LYASGKARLI-----SFLP--KFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 DQVfrRTMskherrewIEHNLARVQMSHALhkrpGEISGGMKQRVGIARALAMKPK--VLLLDEPFGALDALTRAHLQDT 180
Cdd:cd03238 66 DQL--QFL--------IDVGLGYLTLGQKL----STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEV 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556285678 181 VMHIQQELNtTIVMITHDVDeaVL-LSDRVLMMTNGPAATVGEILAV 226
Cdd:cd03238 132 IKGLIDLGN-TVILIEHNLD--VLsSADWIIDFGPGSGKSGGKVVFS 175
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-173 |
8.05e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 8.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 22 LALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGP--GPERAVVFQNH--SLLPWLS---- 93
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlcTYQKQLCFVGHrsGINPYLTlren 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 C-----FDNVALAVDQVFRrtmskherrewiehnlaRVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGA 168
Cdd:PRK13540 95 ClydihFSPGAVGITELCR-----------------LFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
....*
gi 556285678 169 LDALT 173
Cdd:PRK13540 158 LDELS 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-210 |
9.26e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 31 IVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNR--------EIAGPGPeravvfqnhsllpwlscfdnvalaV 102
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqyiKPDYDGT------------------------V 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 DQVFRRTMSKHeRREWIEHNLAR-VQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTV 181
Cdd:PRK13409 418 EDLLRSITDDL-GSSYYKSEIIKpLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180 190
....*....|....*....|....*....|..
gi 556285678 182 MHIQQELNTTIVMITHDV---DeavLLSDRVL 210
Cdd:PRK13409 497 RRIAEEREATALVVDHDIymiD---YISDRLM 525
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-215 |
1.12e-10 |
|
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: 61.46 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNReiagpgperaVVFQnhSLLPWL---SCFDNV-- 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----------ISFS--PQTSWImpgTIKDNIif 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 99 ALAVDQVFRRTMSKHERrewIEHNLARVQMSHALHKRPGEI--SGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAH 176
Cdd:TIGR01271 510 GLSYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGItlSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190
....*....|....*....|....*....|....*....
gi 556285678 177 LQDTVMhIQQELNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:TIGR01271 587 IFESCL-CKLMSNKTRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-215 |
1.22e-10 |
|
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: 61.35 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFNTASGE--FlALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER--- 79
Cdd:COG4615 328 LELRGVTYRYPGEDGDegF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrq 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 80 --AVVFQNHSLlpwlscFDNVALAVDQVFRRTMskherREWiehnLARVQMSHALHKRPGEI-----SGGMKQRVGIARA 152
Cdd:COG4615 407 lfSAVFSDFHL------FDRLLGLDGEADPARA-----REL----LERLELDHKVSVEDGRFsttdlSQGQRKRLALLVA 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 153 LAMKPKVLLLDEpfGALDaltrahlQDTV------MHIQQEL---NTTIVMITHDvDEAVLLSDRVLMMTNG 215
Cdd:COG4615 472 LLEDRPILVFDE--WAAD-------QDPEfrrvfyTELLPELkarGKTVIAISHD-DRYFDLADRVLKMDYG 533
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-198 |
1.28e-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: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlcdnreIAGPGPERAVVFQ 84
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI------EIGETVKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 85 NHSLL-PWLSCFDNVALAVDQVfrrTMSKHE--RREWIehnlARVQMSHA-LHKRPGEISGGMKQRVGIARALAMKPKVL 160
Cdd:TIGR03719 393 SRDALdPNKTVWEEISGGLDII---KLGKREipSRAYV----GRFNFKGSdQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190
....*....|....*....|....*....|....*...
gi 556285678 161 LLDEPFGALDALTRAHLQDTVmhiqQELNTTIVMITHD 198
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEAL----LNFAGCAVVISHD 499
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-198 |
1.79e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnREIAGPGPERAVVFQNHSLLPWLSCFDNVALAV- 102
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG------EARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 -------------------DQVFRRTMSKHER-REWIE----HNL-ARVQMS-HALHKRPGE-----ISGGMKQRVGIAR 151
Cdd:PRK11819 97 evkaaldrfneiyaayaepDADFDALAAEQGElQEIIDaadaWDLdSQLEIAmDALRCPPWDakvtkLSGGERRRVALCR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQdtvmHIQQELNTTIVMITHD 198
Cdd:PRK11819 177 LLLEKPDMLLLDEPTNHLDAESVAWLE----QFLHDYPGTVVAVTHD 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-224 |
2.01e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 27 VSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV----VF-----QNHSLLPWLSCFDN 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIragiMLcpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VALAVdqvfRRtmsKHERREWI-----EHNLARVQMSHALHKRP------GEISGGMKQRVGIARALAMKPKVLLLDEPF 166
Cdd:PRK11288 352 INISA----RR---HHLRAGCLinnrwEAENADRFIRSLNIKTPsreqliMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556285678 167 GALDALTRAHLQDtVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNGpaATVGEIL 224
Cdd:PRK11288 425 RGIDVGAKHEIYN-VIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREG--RIAGELA 479
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-215 |
2.37e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 26 NVSFDIVEGETISLIGHSGCGKSTLLNLIAGI-TTPTEGGLLCDNREIAGPGPERAVVF---------QNHSLLPWLSCF 95
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQgiamvpedrKRDGIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DNVALAV-DQVFRRTMSKHERRE-WIEHNLAR--VQMSHAlHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDA 171
Cdd:PRK13549 360 KNITLAAlDRFTGGSRIDDAAELkTILESIQRlkVKTASP-ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556285678 172 LTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK13549 439 GAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-230 |
4.88e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG-----------PERAVVFQNhsllpwl 92
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGltdlrrvlsiiPQSPVLFSG------- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 93 scfdNVALAVDqvfrrTMSKHERREWIEhNLARVQMSHALHKRP----------GE-ISGGMKQRVGIARALAMKPKVLL 161
Cdd:PLN03232 1325 ----TVRFNID-----PFSEHNDADLWE-ALERAHIKDVIDRNPfgldaevsegGEnFSVGQRQLLSLARALLRRSKILV 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 162 LDEPFGALDALTRAHLQDTvmhIQQELNT-TIVMITHDVDeAVLLSDRVLMMTNgpaatvGEILAVDLPR 230
Cdd:PLN03232 1395 LDEATASVDVRTDSLIQRT---IREEFKScTMLVIAHRLN-TIIDCDKILVLSS------GQVLEYDSPQ 1454
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-231 |
5.26e-10 |
|
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: 58.71 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNReiagpgperaVVFQnhSLLPWL---SCFDNVAL 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----------ISFS--SQFSWImpgTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 101 AV--DQVFRRTMSKherrewiehnlaRVQMSHALHKRP-------GE----ISGGMKQRVGIARALAMKPKVLLLDEPFG 167
Cdd:cd03291 121 GVsyDEYRYKSVVK------------ACQLEEDITKFPekdntvlGEggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 168 ALDALTRAHLQDTVMhIQQELNTTIVMITHDVdEAVLLSDRVLMMTNGPAATVGEILAVDLPRP 231
Cdd:cd03291 189 YLDVFTEKEIFESCV-CKLMANKTRILVTSKM-EHLKKADKILILHEGSSYFYGTFSELQSLRP 250
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-207 |
5.94e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 14 FNTAS----GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLcdnreiAGPGPERAVVFQNH--- 86
Cdd:PLN03073 511 FSDASfgypGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF------RSAKVRMAVFSQHHvdg 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 87 ------SLLPWLSCFDNVAlavDQVFRrtmsKHERREWIEHNLARVQMShalhkrpgEISGGMKQRVGIARALAMKPKVL 160
Cdd:PLN03073 585 ldlssnPLLYMMRCFPGVP---EQKLR----AHLGSFGVTGNLALQPMY--------TLSGGQKSRVAFAKITFKKPHIL 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 161 LLDEPFGALDAltrahlqDTVMHIQQEL---NTTIVMITHD-------VDEAVLLSD 207
Cdd:PLN03073 650 LLDEPSNHLDL-------DAVEALIQGLvlfQGGVLMVSHDehlisgsVDELWVVSE 699
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-218 |
7.62e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV---------------VFQNHS 87
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalvteerrstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 88 LlpwlsCFDNVALAVDQVFRRTMSKHERR-----EWIEHNLARVQMSHALHKrpGEISGGMKQRVGIARALAMKPKVLLL 162
Cdd:PRK10982 343 I-----GFNSLISNIRNYKNKVGLLDNSRmksdtQWVIDSMRVKTPGHRTQI--GSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 163 DEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNGPAA 218
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-197 |
1.04e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 19 GEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAG--ITTPTEGGLLCDNREIAGPGPE-RA-----VVFQNHSLLP 90
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEeRAhlgifLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 91 WLSCFDNVALAVDQVfRRTMSKHERR-----EWIEHNLARVQMS-HALHKRPGE-ISGGMKQRVGIARALAMKPKVLLLD 163
Cdd:CHL00131 98 GVSNADFLRLAYNSK-RKFQGLPELDpleflEIINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 556285678 164 EPFGAL--DAL-TRAHLQDTVMhiqqELNTTIVMITH 197
Cdd:CHL00131 177 ETDSGLdiDALkIIAEGINKLM----TSENSIILITH 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-217 |
1.49e-09 |
|
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: 57.87 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 30 DIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNR------EIAGPGPERavvfqnhsllpwlscfdnvalaVD 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqYISPDYDGT----------------------VE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 104 QVFRRTMSKHERREWIEHNLAR-VQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVM 182
Cdd:COG1245 420 EFLRSANTDDFGSSYYKTEIIKpLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|....*...
gi 556285678 183 HIQQELNTTIVMITHDV---DeavLLSDRVLMMTNGPA 217
Cdd:COG1245 500 RFAENRGKTAMVVDHDIyliD---YISDRLMVFEGEPG 534
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-215 |
1.63e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG-----------PERAVVFQNhsllpwl 92
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlmdlrkvlgiiPQAPVLFSG------- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 93 scfdNVALAVDqvfrrTMSKHERREWIEhNLARVQMSHALHKRP----------GE-ISGGMKQRVGIARALAMKPKVLL 161
Cdd:PLN03130 1328 ----TVRFNLD-----PFNEHNDADLWE-SLERAHLKDVIRRNSlgldaevseaGEnFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 162 LDEPFGALDALTRAHLQDTvmhIQQELNT-TIVMITHDVDeAVLLSDRVLMMTNG 215
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKT---IREEFKScTMLIIAHRLN-TIIDCDRILVLDAG 1448
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-198 |
1.73e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDN------------REIAGpgperavvfqnhsllpw 91
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEG----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 92 lSCFDNVALAVDQVFRRTMSKHERREWIEHN--------LARVQ--MSHA-------------------LHKRPGEISGG 142
Cdd:PRK11147 82 -TVYDFVAEGIEEQAEYLKRYHDISHLVETDpseknlneLAKLQeqLDHHnlwqlenrinevlaqlgldPDAALSSLSGG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 143 MKQRVGIARALAMKPKVLLLDEPFGALDAltrahlqDTVMHIQQELNT---TIVMITHD 198
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDI-------ETIEWLEGFLKTfqgSIIFISHD 212
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-173 |
5.09e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPER-----AVVFQNhsllPWL---SC 94
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrsrlAVVSQT----PFLfsdTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 95 FDNVALAvdqvfRRTMSKHErrewIEH--NLARV-----QMSHALHKRPGE----ISGGMKQRVGIARALAMKPKVLLLD 163
Cdd:PRK10789 406 ANNIALG-----RPDATQQE----IEHvaRLASVhddilRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILD 476
|
170
....*....|
gi 556285678 164 EPFGALDALT 173
Cdd:PRK10789 477 DALSAVDGRT 486
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-223 |
5.82e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.90 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLnLIAGITTPTEG------GLLCDNREI--AGPG 76
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGrrpwrf*TWCANRRAlrRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 PERAVVFQNHSLLPWLSCFDNVALAVDqvfrrtMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMK 156
Cdd:NF000106 89 *HRPVR*GRRESFSGRENLYMIGR*LD------LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556285678 157 PKVLLLDEPFGALDALTRAHLQDTVMHIQQElNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEI 223
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-217 |
6.85e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.12 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 30 DIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGPERAVVFQNHSLlpwlscfdnvalavdqvfrrt 109
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-------NDEWDGITPVYKPQYIDL--------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 110 mskherrewiehnlarvqmshalhkrpgeiSGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELN 189
Cdd:cd03222 73 ------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....*...
gi 556285678 190 TTIVMITHDVDEAVLLSDRVLMMTNGPA 217
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-203 |
1.31e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNR-EIAgpgperavVFQNH--SLLPWLSCFDNVAL 100
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA--------YFDQHraELDPEKTVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 101 AVDQVfrrTMSKHERrewieHNLARVQ---------MS--HALhkrpgeiSGGMKQRVGIARaLAMKPKVLL-LDEPFGA 168
Cdd:PRK11147 407 GKQEV---MVNGRPR-----HVLGYLQdflfhpkraMTpvKAL-------SGGERNRLLLAR-LFLKPSNLLiLDEPTND 470
|
170 180 190
....*....|....*....|....*....|....*...
gi 556285678 169 LDALTRAHLQDTVMHIQqelnTTIVMITHD---VDEAV 203
Cdd:PRK11147 471 LDVETLELLEELLDSYQ----GTVLLVSHDrqfVDNTV 504
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-222 |
1.42e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDnREIAGPgPERAVVFqNHSLLPWLSCFD--NVALA 101
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYV-PQQAWIM-NATVRGNILFFDeeDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 102 VDQVfrrtmskheRREWIEHNLArvQMSHALHKRPGE----ISGGMKQRVGIARALAMKPKVLLLDEPFGALDaltrAHL 177
Cdd:PTZ00243 753 ADAV---------RVSQLEADLA--QLGGGLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD----AHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 556285678 178 QDTVMH--IQQEL-NTTIVMITHDVdEAVLLSDRVLMMTNGPAATVGE 222
Cdd:PTZ00243 818 GERVVEecFLGALaGKTRVLATHQV-HVVPRADYVVALGDGRVEFSGS 864
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-215 |
3.09e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLcDNREIAGPGPEravvfqnhslLPWLScfdNVALAVD 103
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSV-VIRGSVAYVPQ----------VSWIF---NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 104 QVFRrtmSKHE-RREWIEHNLARVQmsHALHKRPGE-----------ISGGMKQRVGIARALAMKPKVLLLDEPFGALDA 171
Cdd:PLN03232 699 ILFG---SDFEsERYWRAIDVTALQ--HDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 556285678 172 LTRAHLQDTVMhiQQELN-TTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:PLN03232 774 HVAHQVFDSCM--KDELKgKTRVLVTNQL-HFLPLMDRIILVSEG 815
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-216 |
3.21e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 17 ASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGllcdNREIAGpgpERAVVFQnhslLPWL---S 93
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA----SVVIRG---TVAYVPQ----VSWIfnaT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAVDqvFRRTmskherREWIEHNLARVQmsHALHKRPG-----------EISGGMKQRVGIARALAMKPKVLLL 162
Cdd:PLN03130 695 VRDNILFGSP--FDPE------RYERAIDVTALQ--HDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 163 DEPFGALDALTRAHLQDTVmhIQQEL-NTTIVMITHD------VDEAVLLSDRVL--------MMTNGP 216
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDKC--IKDELrGKTRVLVTNQlhflsqVDRIILVHEGMIkeegtyeeLSNNGP 831
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-198 |
6.36e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 3 PLIQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGPERAVV 82
Cdd:PRK10636 311 PLLKMEKVSAGY----GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIGLAKGIKLGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 83 FQNHSLlpwlscfdnVALAVDQVFRRTMSKHERREwIEHNLARVQMSHALH-----KRPGEISGGMKQRVGIARALAMKP 157
Cdd:PRK10636 380 FAQHQL---------EFLRADESPLQHLARLAPQE-LEQKLRDYLGGFGFQgdkvtEETRRFSGGEKARLVLALIVWQRP 449
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556285678 158 KVLLLDEPFGALDALTRAHLQDTVMhiqqELNTTIVMITHD 198
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALI----DFEGALVVVSHD 486
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-183 |
9.56e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 22 LALQNVSFDIVEG-----------ETISLI-GHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAG-PGPERAVVFQNHSL 88
Cdd:PRK13541 2 LSLHQLQFNIEQKnlfdlsitflpSAITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 LPWLSCFDNVALavdqvfrrtMSK-HERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFG 167
Cdd:PRK13541 82 KLEMTVFENLKF---------WSEiYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170
....*....|....*..
gi 556285678 168 ALDALTRAHLQD-TVMH 183
Cdd:PRK13541 153 NLSKENRDLLNNlIVMK 169
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-198 |
1.01e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 25 QNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQNHSLLpwlscfDNVAL---- 100
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVL------DTVIMghte 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 101 --AVDQVFRRTMSKHERREWIEHNLARVQMSHA-----------------------LHKRP-GEISGGMKQRVGIARALA 154
Cdd:PRK15064 92 lwEVKQERDRIYALPEMSEEDGMKVADLEVKFAemdgytaearagelllgvgipeeQHYGLmSEVAPGWKLRVLLAQALF 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVmhiqQELNTTIVMITHD 198
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHD 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-221 |
1.24e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 22 LALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG-----------PERAVVFQNhSLLP 90
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlrfkitiiPQDPVLFSG-SLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 91 WLSCFDNVAlavdqvfrrtmskhERREWIEHNLARVQ---------MSHALHKRPGEISGGMKQRVGIARALAMKPKVLL 161
Cdd:TIGR00957 1379 NLDPFSQYS--------------DEEVWWALELAHLKtfvsalpdkLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 162 LDEPFGALDALTRAHLQDTVMhiQQELNTTIVMITHDVDeAVLLSDRVLMMTNGPAATVG 221
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLN-TIMDYTRVIVLDKGEVAEFG 1501
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-218 |
2.73e-07 |
|
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: 50.44 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 33 EGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlCDN-------REIAGP-----------GPERAVVF-QNHSLLPwls 93
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF-DDPpdwdeilDEFRGSelqnyftklleGDVKVIVKpQYVDLIP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 cfdnvaLAVDQVFRRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALT 173
Cdd:cd03236 101 ------KAVKGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556285678 174 RAHLQDTVMHIQQELNTTIVmITHDVdeAVL--LSDRVLMMTNGPAA 218
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLV-VEHDL--AVLdyLSDYIHCLYGEPGA 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-215 |
3.36e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTpteGGLLCDNREIAGpGPERAVVF--------QNHSLLPWLSCF 95
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVN-GRPLDSSFqrsigyvqQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 96 DnvALAVDQVFRR--TMSKHERREWIEHNLARVQM---SHALHKRPGE-ISGGMKQRVGIARALAMKPKVLL-LDEPFGA 168
Cdd:TIGR00956 855 E--SLRFSAYLRQpkSVSKSEKMEYVEEVIKLLEMesyADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556285678 169 LDALTRAH----LQDTVMHIQqelntTIVMITHDvDEAVLLS--DRVLMMTNG 215
Cdd:TIGR00956 933 LDSQTAWSicklMRKLADHGQ-----AILCTIHQ-PSAILFEefDRLLLLQKG 979
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-215 |
5.00e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 20 EFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGittPTEGGLLCDNREIA--GPGPER-------AVVF--QNHSL 88
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGVITydGITPEEikkhyrgDVVYnaETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 89 LPWLSCFDNVALA---------VDQVFRRTMSKHERrewiEHNLARVQMSHALHKRPGE-----ISGGMKQRVGIARALA 154
Cdd:TIGR00956 150 FPHLTVGETLDFAarcktpqnrPDGVSREEYAKHIA----DVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556285678 155 MKPKVLLLDEPFGALDALTRAHLQDTVMHIQQELNTTIVM-ITHDVDEAVLLSDRVLMMTNG 215
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEG 287
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-215 |
5.40e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 23 ALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAV------VFQNHSLLPWLSCFD 96
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengismVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 97 NVALA--------VDQ--VFRRTMSKHERREwIEHNlARVQMshalhkrpGEISGGMKQRVGIARALAMKPKVLLLDEPF 166
Cdd:PRK10982 93 NMWLGryptkgmfVDQdkMYRDTKAIFDELD-IDID-PRAKV--------ATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 556285678 167 GALDALTRAHLQdTVMHIQQELNTTIVMITHDVDEAVLLSDRVLMMTNG 215
Cdd:PRK10982 163 SSLTEKEVNHLF-TIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-210 |
7.43e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGiTTPTEGGllcdnreiagpgperAVVFQNHSLLPWLSCfDNVALAV- 102
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKN-EISADGG---------------SYTFPGNWQLAWVNQ-ETPALPQp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 103 --------DQVFRRTMSK----------------HERREWIEHNLARVQMSHALH---------KRP-GEISGGMKQRVG 148
Cdd:PRK10636 80 aleyvidgDREYRQLEAQlhdanerndghaiatiHGKLDAIDAWTIRSRAASLLHglgfsneqlERPvSDFSGGWRMRLN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 149 IARALAMKPKVLLLDEPFGALDAltrahlqDTVMHIQQELNT---TIVMITHDVDEAVLLSDRVL 210
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDL-------DAVIWLEKWLKSyqgTLILISHDRDFLDPIVDKII 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-201 |
1.04e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 28 SFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDnreiagpgperavvFQNhsllPWLSCFDNVALAVDQVFR 107
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--------------FSH----ITRLSFEQLQKLVSDEWQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 108 RT----MSKHER------REWIE---HNLARVQM-------SHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFG 167
Cdd:PRK10938 85 RNntdmLSPGEDdtgrttAEIIQdevKDPARCEQlaqqfgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190
....*....|....*....|....*....|....
gi 556285678 168 ALDALTRAHLQDTVMHIQQElNTTIVMITHDVDE 201
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQS-GITLVLVLNRFDE 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
24-213 |
1.08e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGL-LCDNREIAGPGPERAVVFQNH-SLLPWLSCF----DN 97
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQDHAYDFENDlTLFDWMSQWrqegDD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 valavDQVFRRTmskherrewiehnLARVQMSH-ALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDaltrah 176
Cdd:PRK15064 415 -----EQAVRGT-------------LGRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD------ 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 556285678 177 lqdtvMHIQQELNT-------TIVMITHDVDEAVLLSDRVLMMT 213
Cdd:PRK15064 471 -----MESIESLNMalekyegTLIFVSHDREFVSSLATRIIEIT 509
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-171 |
1.78e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 47.24 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 15 NTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTP--TEGGLLCDNREIaGPGPERAV--VFQNHSLLP 90
Cdd:cd03232 14 PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPL-DKNFQRSTgyVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 91 WLSCfdnvalavdqvfrrtmskherREWIEhnlarvqMSHALHkrpgEISGGMKQRVGIARALAMKPKVLLLDEPFGALD 170
Cdd:cd03232 93 NLTV---------------------REALR-------FSALLR----GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
.
gi 556285678 171 A 171
Cdd:cd03232 141 S 141
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-209 |
4.76e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 33 EGETISLIGHSGCGKSTLLNLIAGITTPTEGgllcdnrEIAGPGPERAVV--FQNHSLLPWLSCFDN----VAL---AVD 103
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG-------DYDEEPSWDEVLkrFRGTELQDYFKKLANgeikVAHkpqYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 104 Q---VFRRT----MSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAh 176
Cdd:COG1245 171 LipkVFKGTvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRL- 249
|
170 180 190
....*....|....*....|....*....|....*...
gi 556285678 177 lqdTVMHIQQEL---NTTIVMITHDVdeAVL--LSDRV 209
Cdd:COG1245 250 ---NVARLIRELaeeGKYVLVVEHDL--AILdyLADYV 282
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-197 |
5.20e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 12 QRFNTASGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIA-----GIttPTEGGLLCDNREIAGPG---------- 76
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILHVEQEVVGDDttalqcvlnt 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 77 --------PERAVVFQNHSLLPWLSCF------DNVALAVDQVFRRTMSKHERREWIEHNLARVQMSHAL---------- 132
Cdd:PLN03073 259 diertqllEEEAQLVAQQRELEFETETgkgkgaNKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILaglsftpemq 338
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556285678 133 HKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQD----------TVMHIQQELNTTIVMITH 197
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETyllkwpktfiVVSHAREFLNTVVTDILH 413
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-198 |
7.13e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 5 IQVQAVSQRFntasGEFLALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLlcdnrEIaGPGPERAVVFQ 84
Cdd:PRK11819 325 IEAENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-----KI-GETVKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 85 NH-SLLPWLSCFDNVALAVDQVfrrtmskherrewiehNLARVQM-SHAL-----------HKRPGEISGGMKQRVGIAR 151
Cdd:PRK11819 395 SRdALDPNKTVWEEISGGLDII----------------KVGNREIpSRAYvgrfnfkggdqQKKVGVLSGGERNRLHLAK 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 556285678 152 ALAMKPKVLLLDEPFGALDALTRAHLQDTVmhiqQELNTTIVMITHD 198
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRALEEAL----LEFPGCAVVISHD 501
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-209 |
2.63e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 31 IVEGETISLIGHSGCGKSTLLNLIAGITTPTegglLCDNREiaGPGPE------RAVVFQNHsllpwlscFDNVA----- 99
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN----LGDYEE--EPSWDevlkrfRGTELQNY--------FKKLYngeik 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 100 -----LAVDQ---VF--------RRTMSKHERREWIEhnlaRVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLD 163
Cdd:PRK13409 162 vvhkpQYVDLipkVFkgkvrellKKVDERGKLDEVVE----RLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 556285678 164 EPFGALDALTRAhlqdTVMHIQQEL--NTTIVMITHDVdeAVL--LSDRV 209
Cdd:PRK13409 238 EPTSYLDIRQRL----NVARLIRELaeGKYVLVVEHDL--AVLdyLADNV 281
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
38-215 |
7.70e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 38 SLIGHSGCGKSTLLNLIAGITTpteGGLLCDNREIAGpGPERAVVF--------QN--HSllPWLSCFDNVALAVDQVFR 107
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAGRKT---GGYIEGDIRISG-FPKKQETFarisgyceQNdiHS--PQVTVRESLIYSAFLRLP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 108 RTMSKHERREWIEHNLARVQMSH---ALHKRPG--EISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVm 182
Cdd:PLN03140 984 KEVSKEEKMMFVDEVMELVELDNlkdAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV- 1062
|
170 180 190
....*....|....*....|....*....|....*....
gi 556285678 183 hiQQELNT--TIVMITH----DVDEAVllsDRVLMMTNG 215
Cdd:PLN03140 1063 --RNTVDTgrTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-221 |
7.76e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 22 LALQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPG-----------PERAVVF-----QN 85
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGlrelrrqfsmiPQDPVLFdgtvrQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 86 hsLLPWL-SCFDNVALAVDQVFRRTMSKHErREWIEhnlARVQMSHAlhkrpgEISGGMKQRVGIARALAMK-PKVLLLD 163
Cdd:PTZ00243 1404 --VDPFLeASSAEVWAALELVGLRERVASE-SEGID---SRVLEGGS------NYSVGQRQLMCMARALLKKgSGFILMD 1471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 556285678 164 EPFGALD-ALTRaHLQDTVMHIQQelNTTIVMITHDVdEAVLLSDRVLMMTNGPAATVG 221
Cdd:PTZ00243 1472 EATANIDpALDR-QIQATVMSAFS--AYTVITIAHRL-HTVAQYDKIIVMDHGAVAEMG 1526
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-225 |
2.01e-04 |
|
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: 41.47 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLlnliAGITTPTEG------GLLCDNREIAGPGPERAVvfqnhSLLPWLScfdn 97
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL----AFDTIYAEGqrryveSLSAYARQFLGQMDKPDV-----DSIEGLS---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 98 VALAVDQvfrRTMSKHER------------------REWIEHNLA---RVQMSH-ALHKRPGEISGGMKQRVGIARALAM 155
Cdd:cd03270 78 PAIAIDQ---KTTSRNPRstvgtvteiydylrllfaRVGIRERLGflvDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 156 KPKVLL--LDEPFGALDALTRAHLQDTVMHIQQELNTTIVmITHDvDEAVLLSDRVLMMtnGPAATV--GEILA 225
Cdd:cd03270 155 GLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLV-VEHD-EDTIRAADHVIDI--GPGAGVhgGEIVA 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
139-198 |
3.05e-04 |
|
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: 40.42 E-value: 3.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 139 ISGGMKQRVGIARALA---MKPKVL-LLDEPFGALDALTRAHLQDTVMHIQQELNTTIVmITHD 198
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHL 140
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-170 |
3.25e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.93 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 24 LQNVSFDIVEGETISLIGHSGCGKSTLLNLIAGIT--TPTEGGLLCDNREIAGPGPE-RA-----VVFQNHSLLPWLS-- 93
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEdRAgegifMAFQYPVEIPGVSnq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 94 CFDNVALAVDQVFRR--TMSKHERREWIEHNLARVQMSHALHKRPGEI--SGGMKQRVGIARALAMKPKVLLLDEPFGAL 169
Cdd:PRK09580 97 FFLQTALNAVRSYRGqePLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEPELCILDESDSGL 176
|
.
gi 556285678 170 D 170
Cdd:PRK09580 177 D 177
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
116-174 |
4.21e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 4.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 116 REWiehnLARVQMSHALHKRP-GEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTR 174
Cdd:PRK10938 382 QQW----LDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-170 |
4.38e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.60 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 29 FDIVEGETISLIGHSGCGKSTLLNLIAGITTPTEGGLLCDNREIAGPGPERAVVFQNH--SLLPWLSCFDNVAlavdqvF 106
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKADLSTLENLH------F 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556285678 107 RRTMSKHERREWIEHNLARVQMSHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALD 170
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
140-215 |
7.81e-04 |
|
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: 39.89 E-value: 7.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556285678 140 SGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDTVMhiQQELNTTIVMITHDVdEAVLLSDRVLMMTNG 215
Cdd:cd03288 158 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVM--TAFADRTVVTIAHRV-STILDADLVLVLSRG 230
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
32-56 |
8.50e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.06 E-value: 8.50e-04
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
30-56 |
8.54e-04 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 40.10 E-value: 8.54e-04
10 20
....*....|....*....|....*..
gi 556285678 30 DIVEGETISLIGHSGCGKSTLLNLIAG 56
Cdd:COG1162 162 ELLKGKTSVLVGQSGVGKSTLINALLP 188
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
30-56 |
1.41e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 1.41e-03
10 20
....*....|....*....|....*..
gi 556285678 30 DIVEGETISLIGHSGCGKSTLLNLIAG 56
Cdd:cd01854 81 ELLKGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-198 |
1.55e-03 |
|
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: 38.74 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 22 LALQNV-SFDIVEG----ETISLI-GHSGCGKSTLLNLIAGITT---PTEGGLLCDNREIAGPGPERAVV---FQN---- 85
Cdd:cd03240 4 LSIRNIrSFHERSEieffSPLTLIvGQNGAGKTTIIEALKYALTgelPPNSKGGAHDPKLIREGEVRAQVklaFENangk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556285678 86 -HSLLPWLSCFDNVAlavdqvfrrtMSKHERREWIehnlarvqmshaLHKRPGEISGGMKQ------RVGIARALAMKPK 158
Cdd:cd03240 84 kYTITRSLAILENVI----------FCHQGESNWP------------LLDMRGRCSGGEKVlasliiRLALAETFGSNCG 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 556285678 159 VLLLDEPFGALDALTRAH-LQDTVMHIQQELNTTIVMITHD 198
Cdd:cd03240 142 ILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
30-56 |
1.81e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 39.03 E-value: 1.81e-03
10 20
....*....|....*....|....*..
gi 556285678 30 DIVEGETISLIGHSGCGKSTLLNLIAG 56
Cdd:PRK00098 160 PLLAGKVTVLAGQSGVGKSTLLNALAP 186
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
36-63 |
4.53e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.06 E-value: 4.53e-03
10 20 30
....*....|....*....|....*....|.
gi 556285678 36 TISLIGHSGCGKSTLLNLIAG---ITTPTEG 63
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGakaIVSDYPG 31
|
|
| |
