|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-235 |
1.88e-102 |
|
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: 297.46 E-value: 1.88e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGD----QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpAEPGPDRGVVF 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-TGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRYSVFPHLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQ---------GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPRdrpeekERYGATITRDI 235
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARP------GRIVAEVEVDL 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-241 |
3.35e-100 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 293.53 E-value: 3.35e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEY----GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPlPAEPGPDRGVVF 79
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-VTGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRYSVFPHLTVLGNVLLGkelmaskykAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:COG1116 87 QEPALLPWLTVLDNVALG---------LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERprdRPeekerygATITRDISIWP 239
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA---RP-------GRIVEEIDVDL 227
|
..
gi 517136998 240 PR 241
Cdd:COG1116 228 PR 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
5.50e-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: 247.70 E-value: 5.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEP---LPAEpgpDRGV 77
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDvtgLPPE---KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 --VFQRYSVFPHLTVLGNVLLGkeLMASKYKAKlfgqARRSAIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQAL 155
Cdd:COG3842 80 gmVFQDYALFPHLTVAENVAFG--LRMRGVPKA----EIRARVAELLEL---VGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIA 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-212 |
1.68e-76 |
|
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: 231.64 E-value: 1.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIgmVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLR---------GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIA 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-212 |
4.07e-71 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 218.71 E-value: 4.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAePGPDR-------G 76
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDInklrrkvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 77 VVFQRYSVFPHLTVLGNVLLGkeLMaskykaKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALI 156
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLA--PI------KVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNEtQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVV 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-212 |
6.09e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 219.56 E-value: 6.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEP---LPAEpgpDRGV 77
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdLPPK---DRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 --VFQRYSVFPHLTVLGNvllgkelMAskykaklFG-QARRSAIDEARQLITEV----GLSGAETKYPAQLSGGMQQRLA 150
Cdd:COG3839 78 amVFQSYALYPHMTVYEN-------IA-------FPlKLRKVPKAEIDRRVREAaellGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 151 LAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIA 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-212 |
1.83e-68 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 215.40 E-value: 1.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSeLIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAE-PGPDRGV-- 77
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRERRVgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQRYSVFPHLTVLGNVLLG-KELMASKykaklfGQARRsaidEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALI 156
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGlRVRPPSK------AEIRA----RVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
2.25e-68 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 211.06 E-value: 2.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELI-IDSVWKEYGD----QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR 75
Cdd:COG1136 1 MSPLLeLRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 --------GVVFQRYSVFPHLTVLGNVLLGkelmaskykAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQ 147
Cdd:COG1136 81 arlrrrhiGFVFQFFNLLPELTALENVALP---------LLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 148 RLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAfTLATRVVAFE 215
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLR 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-218 |
5.65e-68 |
|
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: 208.58 E-value: 5.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR------GV 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplrrriGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQRYSVFPHLTVLGNVLLGkelmaskykaklfgqarrsaidearqlitevglsgaetkypaqLSGGMQQRLALAQALIM 157
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-214 |
6.55e-68 |
|
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: 210.17 E-value: 6.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQRYS 83
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVntVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVLGNVLLGKELmaskykAKLFGQARRSAIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:cd03300 83 LFPHLTVFENIAFGLRL------KKLPKAEIKERVAEALDL---VQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517136998 164 LDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAF 214
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-215 |
1.11e-67 |
|
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: 209.27 E-value: 1.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQI----VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---- 75
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 ----GVVFQRYSVFPHLTVLGNVLLGkelmaskykAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLAL 151
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELP---------LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517136998 152 AQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFtLATRVVAFE 215
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELR 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-212 |
1.64e-67 |
|
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: 209.45 E-value: 1.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELII--DSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--- 75
Cdd:COG1127 1 MSEPMIevRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 ----GVVFQRYSVFPHLTVLGNVLLG-KElmaskykaklFGQARRSAIDE-ARQLITEVGLSGAETKYPAQLSGGMQQRL 149
Cdd:COG1127 81 rrriGMLFQGGALFDSLTVFENVAFPlRE----------HTDLSEAEIRElVLEKLELVGLPGAADKMPSELSGGMRKRV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVA 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-215 |
1.95e-67 |
|
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: 208.54 E-value: 1.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR------GVVF 79
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrqkvGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRYSVFPHLTVLGNVLLGkeLMaskykaKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:cd03262 83 QQFNLFPHLTVLENITLA--PI------KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
2.15e-67 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 210.10 E-value: 2.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYG----DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAePGPDRG 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 77 VVFQRYSVFPHLTVLGNVLLGkelmaskykAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALI 156
Cdd:COG4525 80 VVFQKDALLPWLNVLDNVAFG---------LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLV 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-212 |
1.02e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 202.22 E-value: 1.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVFQ 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRrriGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVllgkelmasKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:COG1131 81 EPALYPDLTVRENL---------RFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-218 |
4.86e-64 |
|
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: 200.64 E-value: 4.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 3 ELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQ 80
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVgfVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLLGKELMASKYKAKLFGQARRsaideARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAK-----VHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-212 |
9.87e-64 |
|
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: 203.73 E-value: 9.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--GVVFQR 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRdyGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVLLGkeLMASKYKAKlfgqARRSAIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:TIGR03265 85 YALFPNLTVADNIAYG--LKNRGMGRA----EVAERVAELLDL---VGLPGSERKYPGQLSGGQQQRVALARALATSPGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:TIGR03265 156 LLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIV 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-222 |
2.88e-63 |
|
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: 198.46 E-value: 2.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpAEPGPDRGVVFQRYSVFPHLTVLGNVLLG- 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRMVVFQNYSLLPWLTVRENIALAv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 98 KELMASKYKAKlfgqaRRSAIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRA 177
Cdd:TIGR01184 80 DRVLPDLSKSE-----RRAIVEEHIAL---VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517136998 178 EIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVA----------------FERPRDRPE 222
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMltngpaanigqilevpFPRPRDRLE 212
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-230 |
4.65e-62 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 195.40 E-value: 4.65e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQR 81
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIgfVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVLLGKELmaskykaklfgQARRSAIDEAR--QLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEI-----------RKHPKAKIKARveELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEEKERYGAT 230
Cdd:TIGR00968 150 QVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKieqiGSPDEVYDHPAN 224
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-223 |
3.02e-61 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 195.69 E-value: 3.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGD-QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgPDR-----GVVF 79
Cdd:COG1125 4 FENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLD-PVElrrriGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRYSVFPHLTVLGNV-----LLGKElmaskyKAKlfgqaRRSAIDEarqLITEVGLSGAE--TKYPAQLSGGMQQRLALA 152
Cdd:COG1125 83 QQIGLFPHMTVAENIatvprLLGWD------KER-----IRARVDE---LLELVGLDPEEyrDRYPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEE 223
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRivqyDTPEE 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-212 |
7.41e-61 |
|
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: 192.33 E-value: 7.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----PAEPGPDR---GVV 78
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRrrmGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRYSVFPHLTVLGNVLLG-KElmaskykaklFGQARRSAIDE-ARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALI 156
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPlRE----------HTRLSEEEIREiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-216 |
8.99e-61 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 191.80 E-value: 8.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEY-GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR-------GV 77
Cdd:COG2884 4 FENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylrrriGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQRYSVFPHLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIM 157
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVT---------GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELED 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-212 |
6.13e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 184.57 E-value: 6.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVleNVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQR 81
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVsmLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVLLGkelMASKYKaklFGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:COG3840 80 NNLFPHLTVAQNIGLG---LRPGLK---LTAEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVL 201
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-212 |
1.04e-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: 183.61 E-value: 1.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIamVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNvllgkelMASKYKAKlfgQARRSAIDEARQLITEV-GLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03301 81 YALYPHMTVYDN-------IAFGLKLR---KVPKDEIDERVREVAELlQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIA 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-212 |
2.56e-55 |
|
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: 185.88 E-value: 2.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEY-----GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--- 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 ----GVVFQ--RYSVFPHLTVlgnvllGKELMASkykAKLFGQARRSAIDE-ARQLITEVGLS-GAETKYPAQLSGGMQQ 147
Cdd:COG1123 341 rrrvQMVFQdpYSSLNPRMTV------GDIIAEP---LRLHGLLSRAERRErVAELLERVGLPpDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 148 RLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-212 |
2.92e-55 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 178.74 E-value: 2.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpAEPGPDRGVVFQRYS 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLA---------GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517136998 164 LDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELV 200
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-218 |
3.92e-55 |
|
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: 178.07 E-value: 3.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYG----DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL-PAEPGPDRG-- 76
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 77 -VVFQRY--SVFPHLTVlgnvllgKELMASKYKAKLFGQARRsaidEARQLITEVGLSGAE-TKYPAQLSGGMQQRLALA 152
Cdd:COG1124 82 qMVFQDPyaSLHPRHTV-------DRILAEPLRIHGLPDREE----RIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-220 |
4.03e-55 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 178.33 E-value: 4.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpAEPGPDRGVVFQRYS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-AEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVLGNVLLGkelmaskykakLFGQARrsaiDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK11247 92 LLPWKKVIDNVGLG-----------LKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 164 LDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFE-------------RPRDR 220
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEegkigldltvdlpRPRRR 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-214 |
8.91e-55 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 180.91 E-value: 8.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 8 SVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQRYSVF 85
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVntVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PHLTVLGNVLLGKElMASKYKAKLfgqARRsaIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:PRK09452 99 PHMTVFENVAFGLR-MQKTPAAEI---TPR--VMEALRM---VQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517136998 166 EPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAF 214
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-212 |
6.25e-54 |
|
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: 174.80 E-value: 6.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGD-QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgPDR-----GVVF 79
Cdd:cd03295 3 FENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD-PVElrrkiGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRYSVFPHLTVLGNVLLgkelmaskyKAKLFGQARRSAIDEARQLITEVGLSGAE--TKYPAQLSGGMQQRLALAQALIM 157
Cdd:cd03295 82 QQIGLFPHMTVEENIAL---------VPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIA 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-218 |
1.33e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 174.13 E-value: 1.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 8 SVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR------GVVFQR 81
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqeaGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVLLGKelmaskykAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK09493 86 FYLFPHLTALENVMFGP--------LRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETqMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-216 |
1.39e-53 |
|
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: 173.04 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQ--IVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVF 79
Cdd:cd03225 2 LKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrrkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QrysvFP-----HLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQA 154
Cdd:cd03225 82 Q----NPddqffGPTVEEEVAFGLENL---------GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNEtQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-216 |
1.88e-53 |
|
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: 173.29 E-value: 1.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQI-VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVV 78
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQrysvFP-----HLTVLGNVLLGkeLMAskykaklFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQ 153
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFG--PEN-------LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
1.96e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 173.74 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPlPAEPGPDRGVVFQ 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-PRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSV---FPhLTVLGNVLLGkeLMASKYKAKLFGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIM 157
Cdd:COG1121 83 RAEVdwdFP-ITVRDVVLMG--RYGRRGLFRRPSRADREAVDEA---LERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVL 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-218 |
3.90e-53 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 172.37 E-value: 3.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRML-----LGQERPTRGTILLDGEPLPaEPGPDR----- 75
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIY-DLDVDVlelrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 --GVVFQRYSVFPhLTVLGNVLLGkelmaskykAKLFGQARRSAIDE-ARQLITEVGLSGaETK---YPAQLSGGMQQRL 149
Cdd:cd03260 82 rvGMVFQKPNPFP-GSIYDNVAYG---------LRLHGIKLKEELDErVEEALRKAALWD-EVKdrlHALGLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517136998 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
2.69e-52 |
|
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: 168.34 E-value: 2.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVFQ 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrriGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVllgkelmaskykaklfgqarrsaidearqlitevglsgaetkypaQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03230 81 EPSLYENLTVRENL---------------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVA 166
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-216 |
3.63e-52 |
|
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: 169.25 E-value: 3.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPlpAEPGPDR-GVVFQRYSV 84
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP--LEKERKRiGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 85 ---FPhLTVLGNVLLGKElmaskYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03235 80 drdFP-ISVRDVVLMGLY-----GHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-218 |
6.40e-52 |
|
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: 168.63 E-value: 6.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 21 NVSLTVaSRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAE------PGPDR--GVVFQRYSVFPHLTVLG 92
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinlPPQQRkiGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLGkelmaskykakLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:cd03297 95 NLAFG-----------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517136998 173 PGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-230 |
2.05e-51 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 171.81 E-value: 2.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--GVVFQRYS 83
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRkvGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVLGNVLLGKELMASKYKAKlfgqarRSAIDE-ARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTVLPRRERPN------AAAIKAkVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 163 LLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEEKERYGAT 230
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNieqaGTPDQVWREPAT 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-213 |
2.38e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 168.31 E-value: 2.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEY-GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR------- 75
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrrri 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 GVVFQRYSVFPHLTVLGNVLLGKELMASKYKAkLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQAL 155
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRS-LLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVA 213
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-211 |
4.48e-51 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 168.21 E-value: 4.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 7 DSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD----R----GVV 78
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelRrkkiSMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRYSVFPHLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQ---------GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRV 211
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRI 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-223 |
8.61e-51 |
|
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: 167.14 E-value: 8.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVV-- 78
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlGIArt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRYSVFPHLTVLGNVLLG------KELMASKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALA 152
Cdd:COG0411 85 FQNPRLFPELTVLENVLVAaharlgRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEE 223
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRviaeGTPAE 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-216 |
1.14e-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: 166.07 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgPDR----GVV- 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEiarlGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 -FQRYSVFPHLTVLGNVLLGKEL-MASKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALI 156
Cdd:cd03219 80 tFQIPRLFPELTVLENVMVAAQArTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-218 |
2.11e-50 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 165.96 E-value: 2.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGE--PLPAEPGPDR--------GVVFQ 80
Cdd:COG4161 10 CFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAirllrqkvGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLlgkelmasKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:COG4161 90 QYNLWPHLTVMENLI--------EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-212 |
4.40e-50 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 168.36 E-value: 4.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQR 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIcmVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVllgkelmasKYKAKLFGQA---RRSAIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:PRK11432 87 YALFPHMSLGENV---------GYGLKMLGVPkeeRKQRVKEALEL---VDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVI 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-212 |
6.27e-50 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 164.22 E-value: 6.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR-------GVVFQR-YSVF-PHL 88
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkeiQMVFQDpMSSLnPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TVLGNVllgKELMASKYKAKlfGQARRSAIdeARQLITEVGLSGA-ETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:cd03257 100 TIGEQI---AEPLRIHGKLS--KKEARKEA--VLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 168 FGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03257 173 TSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-213 |
9.28e-50 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 164.45 E-value: 9.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQRYSVFPHL 88
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELarriAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TVLGNVLLGKelmaSKYKaKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:COG1120 91 TVRELVALGR----YPHL-GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 169 GALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVA 213
Cdd:COG1120 166 SHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-212 |
3.97e-49 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 166.18 E-value: 3.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----PAEPGPDR----GVVFQRY 82
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENImkqsPVELREVRrkkiGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 83 SVFPHLTVLGNVLLGKELmaskykAKLFGQARRsaiDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPEL------LGWPEQERK---EKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 163 LLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:TIGR01186 152 LMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIV 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-212 |
4.01e-49 |
|
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: 162.12 E-value: 4.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDqIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGE---PLPAEPgPDRGVVFQ 80
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK-RDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLLGkeLMASKYKaklfgqarRSAIDEARQLITEV-GLSGAETKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:cd03299 79 NYALFPHMTVYKNIAYG--LKKRKVD--------KKEIERKVLEIAEMlGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVA 201
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-212 |
4.42e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 163.05 E-value: 4.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLR---MLlgqERPTRGTILLDGEPLPAEPGPDR----- 75
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRcinLL---ETPDSGEIRVGGEEIRLKPDRDGelvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 ------------GVVFQRYSVFPHLTVLGNVLLGKelmaskykAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSG 143
Cdd:COG4598 86 drrqlqrirtrlGMVFQSFNLWSHMTVLENVIEAP--------VHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517136998 144 GMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNEtQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVV 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-210 |
4.67e-49 |
|
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: 161.83 E-value: 4.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPA--EPG-----PDR-GVVFQRYSVFPHLT 89
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldEDArarlrARHvGFVFQSFQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGKELmaskykaklfgQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:COG4181 107 ALENVMLPLEL-----------AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMReaftLATR 210
Cdd:COG4181 176 NLDAATGEQIIDLLFELNRERGTTLVLVTHDPA----LAAR 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-218 |
9.08e-49 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 161.84 E-value: 9.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILL------DGEPLPAEPGPD 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 75 R------GVVFQRYSVFPHLTVLGNVLLGKELMAskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQR 148
Cdd:PRK11264 81 RqlrqhvGFVFQNFNLFPHRTVLENIIEGPVIVK--------GEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 149 LALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-237 |
1.28e-48 |
|
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: 163.82 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 34 LVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--GVVFQRYSVFPHLTVLGNVllgkelmasKYKAKLFG 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRhiNMVFQSYALFPHMTVEENV---------AFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 112 QARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQ 191
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 192 MTVVMVTHDMREAFTLATRVVAFERPR----DRPEE-----KERYGATITRDISI 237
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKiaqiGTPEEiyeepANLFVARFIGEINV 206
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-218 |
2.12e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 160.56 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEP--LPAEPGP--------DR 75
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDkairelrrNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 GVVFQRYSVFPHLTVLGNVLlgkelmasKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQAL 155
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLI--------EAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-212 |
4.26e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.83 E-value: 4.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD--RGV--VFQR 81
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVayVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 ySVFPHLTVLGNVLLGKELmaskykaklfgQARRSAIDEARQLITEVGLSGAETKYPA-QLSGGMQQRLALAQALIMKPK 160
Cdd:COG4619 83 -PALWGGTVRDNLPFPFQL-----------RERKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVL 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-218 |
5.22e-48 |
|
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: 158.81 E-value: 5.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 23 SLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQRYSVFPHLTVLGNVLLGKEL 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVsmLFQENNLFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 101 maskyKAKLFGQaRRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIH 180
Cdd:cd03298 98 -----GLKLTAE-DRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 517136998 181 TLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-215 |
1.29e-47 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 161.81 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 21 NVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEP---------LPAEpgpDR--GVVFQRYSVFPHLT 89
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargifLPPH---RRriGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGkelmaskYKaKLFGQARRSAIDEarqLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:COG4148 94 VRGNLLYG-------RK-RAPRAERRISFDE---VVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLE 208
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-211 |
7.72e-47 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 160.65 E-value: 7.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 21 NVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpAEPGPDR---------GVVFQRYSVFPHLTVL 91
Cdd:COG4175 45 DASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDI-TKLSKKElrelrrkkmSMVFQHFALLPHRTVL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 GNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGAL 171
Cdd:COG4175 124 ENVAFGLEIQ---------GVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSAL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517136998 172 DPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRV 211
Cdd:COG4175 195 DPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRI 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-213 |
1.87e-46 |
|
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: 155.42 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQ-IVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD----R---GV 77
Cdd:cd03256 3 VENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlRrqiGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQRYSVFPHLTVLGNVLLGKELMASKYKAkLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIM 157
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRLGRRSTWRS-LFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVA 213
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVG 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-223 |
4.13e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 158.46 E-value: 4.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQR 81
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPInmMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVLLGKElmaskyKAKLfgqARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLK------QDKL---PKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEE 223
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfvqiGEPEE 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-200 |
8.02e-46 |
|
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: 152.63 E-value: 8.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL---PAEPGPDRGVVFQ 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdaREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVllgkelmasKYKAKLFGqaRRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:COG4133 83 ADGLKPELTVRENL---------RFWAALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRlWNETQMTVVMVTHD 200
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-212 |
1.05e-45 |
|
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: 160.45 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELI-IDSVWKEY--GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPT---RGTILLDGEPL----PAE 70
Cdd:COG1123 1 MTPLLeVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelsEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 71 PGPDRGVVFQ--RYSVFPhLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQR 148
Cdd:COG1123 81 RGRRIGMVFQdpMTQLNP-VTVGDQIAEALENL---------GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517136998 149 LALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVV 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-212 |
1.77e-45 |
|
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: 153.09 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVFQ 80
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrqiGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVllgkelmasKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:COG4555 82 ERGLYDRLTVRENI---------RYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLWNEtQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVV 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-201 |
1.95e-45 |
|
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: 152.74 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQ----IVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR------ 75
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkarrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 -GVVFQRYSVFPHLTVLGNVllgkelmasKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQA 154
Cdd:cd03258 84 iGMIFQHFNLLSSRTVFENV---------ALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517136998 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEM 201
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-219 |
3.48e-45 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 151.48 E-value: 3.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERP---TRGTILLDGEPLPAEPGPDR--GVVFQRYSVFPH 87
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRriGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGkelMASKYKaklfGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:COG4136 91 LSVGENLAFA---LPPTIG----RAQRRARVEQA---LEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 168 FGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAfTLATRVVAFERPRD 219
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDLGNWQH 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-201 |
4.80e-45 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 154.85 E-value: 4.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR-------GVVFQRYSVFP 86
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraarrkiGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTVLGNVLLGKELmaskykAKLFGQARRSAIDEarqLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:COG1135 96 SRTVAENVALPLEI------AGVPKAEIRKRVAE---LLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190
....*....|....*....|....*....|....*
gi 517136998 167 PFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:COG1135 167 ATSALDPETTRSILDLLKDINRELGLTIVLITHEM 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-216 |
6.23e-45 |
|
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: 151.02 E-value: 6.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 9 VWKEYGDQIV-LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP-----AEPGPDR--GVVFQ 80
Cdd:cd03292 6 VTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgrAIPYLRRkiGVVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03292 86 DFRLLPDRNVYENVAFALEVT---------GVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-213 |
1.17e-44 |
|
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: 150.91 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQI-VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR------- 75
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 GVVFQRYSVFPHLTVLGNVLLGKeLMASKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQAL 155
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGR-LGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVA 213
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVG 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-216 |
1.91e-44 |
|
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: 151.45 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 16 QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR-------GVVFQrysvFPH- 87
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdlrkkvGLVFQ----FPEh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 ----LTVLGNVLLG-KELMASKYKAKlfgqaRRsaideARQLITEVGLSgaET---KYPAQLSGGMQQRLALAQALIMKP 159
Cdd:TIGR04521 94 qlfeETVYKDIAFGpKNLGLSEEEAE-----ER-----VKEALELVGLD--EEyleRSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-218 |
2.30e-44 |
|
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: 147.39 E-value: 2.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPdrgvvfqrysvf 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 phltvlgnvllgkelmaskykaklfgqarrsaidEARQLITEVGlsgaetkypaQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:cd00267 70 ----------------------------------ELRRRIGYVP----------QLSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517136998 166 EPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:cd00267 106 EPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
3.15e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.02 E-value: 3.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQRYSVFPHLTVLGNV 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 95 LLGkelmaskykAKLFGQARRSAIDEARQLITEVGLSGAE----TKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:pfam00005 81 RLG---------LLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-215 |
8.48e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 152.49 E-value: 8.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--V 78
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVgmV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRYSVFPHLTVLGNVLLGKELmASKYKAKLfgQARRSAIDEARQLitevglSGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKL-AGAKKEEI--NQRVNQVAEVLQL------AHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517136998 159 PKVLLLDEPFGALDPGI----RAEIHTLMKRLwnetQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALrvqmRIEISRLHKRL----GRTMIYVTHDQVEAMTLADKIVVLD 208
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
10-211 |
6.84e-43 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 149.46 E-value: 6.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 10 WKEYGdqivLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQRYSVFPH 87
Cdd:NF040840 11 WKEFK----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIayVYQNYMLFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGKELMaskykaklfgQARRSAIDEARQLITEV-GLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:NF040840 87 KTVFENIAFGLKLR----------KVPKEEIERKVKEIMELlGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 167 PFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRV 211
Cdd:NF040840 157 PLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRV 201
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-218 |
1.59e-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: 144.70 E-value: 1.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEY-GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpaEPGPDR--------- 75
Cdd:TIGR02673 4 FHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDV--NRLRGRqlpllrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 GVVFQRYSVFPHLTVLGNVLLGKELmasKYKAKLFGQARRSAIDEArqliteVGLSGAETKYPAQLSGGMQQRLALAQAL 155
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEV---RGKKEREIQRRVGAALRQ------VGLEHKADAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-213 |
2.40e-42 |
|
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: 142.96 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpaepgpdrgvvfqrysvfphltvlg 92
Cdd:cd03214 9 YGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 nvllgkelmaSKYKAKLFgqARRSAIdeARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:cd03214 64 ----------ASLSPKEL--ARKIAY--VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517136998 173 PGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVA 213
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVIL 170
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
13-227 |
2.80e-42 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 145.13 E-value: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRML-----LGQERPTRGTILLDGEPLPAePGPDR-------GVVFQ 80
Cdd:TIGR00972 11 YGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndLVPGVRIEGKVLFDGQDIYD-KKIDVvelrrrvGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPhLTVLGNVLLGKELMASKYKAKLFGQARRSAIDEArqLITEVG--LSgaetKYPAQLSGGMQQRLALAQALIMK 158
Cdd:TIGR00972 90 KPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAA--LWDEVKdrLH----DSALGLSGGQQQRLCIARALAVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTHDM--------REAFTLATRVVA-------FERPRDRpeE 223
Cdd:TIGR00972 163 PEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMqqaarisdRTAFFYDGELVEygpteqiFTNPKEK--R 238
|
....
gi 517136998 224 KERY 227
Cdd:TIGR00972 239 TEDY 242
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-227 |
3.16e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 145.18 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 8 SVWkeYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRML--LGQERP---TRGTILLDGEPLpAEPGPD----R--- 75
Cdd:COG1117 18 NVY--YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGEDI-YDPDVDvvelRrrv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 GVVFQRYSVFPHlTVLGNVLLGkelmaskykAKLFGQARRSAIDEA-RQLITEVGL----------SGAEtkypaqLSGG 144
Cdd:COG1117 95 GMVFQKPNPFPK-SIYDNVAYG---------LRLHGIKSKSELDEIvEESLRKAALwdevkdrlkkSALG------LSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 145 MQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTHDMREA--------FTLATRVVA--- 213
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAarvsdytaFFYLGELVEfgp 236
|
250
....*....|....*...
gi 517136998 214 ----FERPRDrpEEKERY 227
Cdd:COG1117 237 teqiFTNPKD--KRTEDY 252
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-212 |
7.55e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 146.91 E-value: 7.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEY-GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV-- 77
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQRYSVFPHLTVLGNvllgkelMAskYKAKLFGQARrsaiDEARQLITEV----GLSGAETKYPAQLSGGMQQRLALAQ 153
Cdd:PRK11650 81 VFQNYALYPHMSVREN-------MA--YGLKIRGMPK----AEIEERVAEAarilELEPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 154 ALIMKPKVLLLDEPFGALDPGIRA----EIHTLMKRLwnetQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVqmrlEIQRLHRRL----KTTSLYVTHDQVEAMTLADRVV 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-212 |
2.33e-41 |
|
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: 144.81 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERP---TRGTILLDGEPLPAEPGPD----RG----VVFQR-YSVF 85
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKElrkiRGreiqMIFQDpMTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 -PHLTVlGNVLlgKELMASKYKAKlfgqaRRSAIDEARQLITEVGLSGAET---KYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:COG0444 100 nPVMTV-GDQI--AEPLRIHGGLS-----KAEARERAIELLERVGLPDPERrldRYPHELSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-212 |
5.84e-41 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 141.26 E-value: 5.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 23 SLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQRYSVFPHLTVLGNVLLGKE- 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVsmLFQENNLFSHLTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 100 -LmaskykaKLFGQARRSAIDEARQliteVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAE 178
Cdd:PRK10771 99 gL-------KLNAAQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190
....*....|....*....|....*....|....
gi 517136998 179 IHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSL 201
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-212 |
6.04e-41 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 140.72 E-value: 6.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGD--QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVV 78
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqslGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRYSVFPHLTVLgnvllgkELMasKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:cd03263 81 PQFDALFDELTVR-------EHL--RFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIA 203
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-201 |
7.67e-41 |
|
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: 140.06 E-value: 7.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 9 VWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGP--------DRGVVFQ 80
Cdd:TIGR03608 4 ISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkaskfrreKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLLGkelmaSKYKaKLFGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:TIGR03608 84 NFALIENETVEENLDLG-----LKYK-KLSKKEKREKKKEA---LEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDM 201
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDP 194
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-218 |
2.02e-40 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 139.23 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 23 SLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQRYSVFPHLTVLGNVLLGkel 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVsmLFQENNLFAHLTVRQNIGLG--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 101 maSKYKAKLFGQARRSAIDEARQliteVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIH 180
Cdd:TIGR01277 95 --LHPGLKLNAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 517136998 181 TLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-216 |
1.80e-39 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 136.80 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR-----GVVFQRYSVFPH 87
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragiGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGkelmaskykaklfgqARRSAIDEARQLITEVglsgaETKYPA----------QLSGGMQQRLALAQALIM 157
Cdd:cd03224 90 LTVEENLLLG---------------AYARRRAKRKARLERV-----YELFPRlkerrkqlagTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLER 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-212 |
3.89e-39 |
|
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: 135.81 E-value: 3.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDG-EPLPAEPGPDR-GVVFQRYSVFPHL 88
Cdd:cd03268 8 KTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGkSYQKNIEALRRiGALIEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TVLGNVllgkelmasKYKAKLFGqARRSAIDEarqLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:cd03268 88 TARENL---------RLLARLLG-IRKKRIDE---VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 169 GALDP-GIrAEIHTLMkRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03268 155 NGLDPdGI-KELRELI-LSLRDQGITVLISSHLLSEIQKVADRIG 197
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-223 |
8.50e-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: 135.19 E-value: 8.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVFQRYSVFPH 87
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRrriGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLgkelmaskyKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:cd03265 88 LTGWENLYI---------HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 168 FGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEE 223
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRiiaeGTPEE 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-212 |
1.13e-38 |
|
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: 134.63 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVaSRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGVVF---Q 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLgnvllgkELMAskYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:cd03264 80 EFGVYPNFTVR-------EFLD--YIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLWNETqmTVVMVTHDMREAFTLATRVV 212
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVA 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-216 |
6.70e-38 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 133.18 E-value: 6.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVF--QRYSVFPH 87
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlGIGYvpEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGkelmaskykakLFGQARRSAIDEARQLITEVglsgaetkYP----------AQLSGGMQQRLALAQALIM 157
Cdd:COG0410 93 LTVEENLLLG-----------AYARRDRAEVRADLERVYEL--------FPrlkerrrqraGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLER 211
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
18-215 |
8.18e-38 |
|
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: 132.45 E-value: 8.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR-------GVVFQRYSVFPHLTV 90
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLvqlrrriGYIFQAHNLLGFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVLLGKELMAskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:TIGR02982 100 RQNVQMALELQP--------NLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 171 LDPGIRAEIHTLMKRLWNETQMTVVMVTHDMReAFTLATRVVAFE 215
Cdd:TIGR02982 172 LDSKSGRDVVELMQKLAKEQGCTILMVTHDNR-ILDVADRILQME 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-218 |
1.06e-37 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 130.58 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGD--QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GV 77
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQRYSVFpHLTVLGNVllgkelmaskykaklfgqarrsaidearqlitevglsgaetkypaqLSGGMQQRLALAQALIM 157
Cdd:cd03228 81 VPQDPFLF-SGTIRENI----------------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTHDMrEAFTLATRVVAFERPR 218
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-216 |
2.86e-37 |
|
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: 132.55 E-value: 2.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDG-EPLPAEPGPD-R---GVVFQRysvfPH- 87
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEiRkkvGMVFQN----PDn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 ----LTV-------LGNVLLGKELMaskykaklfgqarRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALI 156
Cdd:TIGR04520 89 qfvgATVeddvafgLENLGVPREEM-------------RKRVDEA---LKLVGMEDFRDREPHLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAfTLATRVVAFER 216
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNK 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-212 |
5.53e-37 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 131.63 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSE--LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD---- 74
Cdd:PRK10619 1 MSEnkLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 75 -------------RGVVFQRYSVFPHLTVLGNVLlgkelmasKYKAKLFGQARRSAIDEARQLITEVGLSG-AETKYPAQ 140
Cdd:PRK10619 81 vadknqlrllrtrLTMVFQHFNLWSHMTVLENVM--------EAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVH 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 141 LSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVV 212
Cdd:PRK10619 153 LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
7-223 |
6.86e-37 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 134.52 E-value: 6.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 7 DSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILL-DGE----PLPAEPGPDR------ 75
Cdd:TIGR03415 28 EEILDRTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVkDGDgsvdVANCDAATLRrlrthr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 -GVVFQRYSVFPHLTVLGNVLLGKElMASKYKAKlfgqaRRSAIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQA 154
Cdd:TIGR03415 108 vSMVFQQFALLPWRTVEENVAFGLE-MQGMPKAE-----RRKRVDEQLEL---VGLAQWADRKPGELSGGMQQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEE 223
Cdd:TIGR03415 179 FATEAPILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIMEGGRiiqhGTPEE 251
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-218 |
7.88e-37 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 137.20 E-value: 7.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 2 SELIIDSVWKEYGD-QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----G 76
Cdd:COG4988 335 PSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWrrqiA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 77 VVFQRySVFPHLTVLGNVLLGK------ELMASkykaklfgqARRSAIDE-----ARQLITEVGLSGaetkypAQLSGGM 145
Cdd:COG4988 415 WVPQN-PYLFAGTIRENLRLGRpdasdeELEAA---------LEAAGLDEfvaalPDGLDTPLGEGG------RGLSGGQ 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 146 QQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETqmTVVMVTHDMREAfTLATRVVAFERPR 218
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALL-AQADRILVLDDGR 548
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-216 |
1.43e-36 |
|
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: 137.27 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpAEPGPD--R---GVVFQRYSVFpHLTVLG 92
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL-RQIDPAslRrqiGVVLQDVFLF-SGTIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLGKElMASkyKAKLFGQARRSAIDE-----ARQLITEVGLSGaetkypAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:COG2274 568 NITLGDP-DAT--DEEIIEAARLAGLHDfiealPMGYDTVVGEGG------SNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517136998 168 FGALDPGIRAEIHTLMKRLWNetQMTVVMVTHDMrEAFTLATRVVAFER 216
Cdd:COG2274 639 TSALDAETEAIILENLRRLLK--GRTVIIIAHRL-STIRLADRIIVLDK 684
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
15-204 |
2.10e-36 |
|
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: 129.01 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--------GVVFQRYSVFP 86
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkklGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTVLGNV----LLGKelmaskykaklfgQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:TIGR02211 97 DFTALENVamplLIGK-------------KSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517136998 163 LLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREA 204
Cdd:TIGR02211 164 LADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-218 |
5.95e-36 |
|
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: 134.51 E-value: 5.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQRysvfPHL- 88
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrrriAVVPQR----PHLf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 --TVLGNVLLgkelmaskykaklfgqARRSAIDEA-RQLITEVGLSGAETKYP-----------AQLSGGMQQRLALAQA 154
Cdd:COG4987 422 dtTLRENLRL----------------ARPDATDEElWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 155 LIMKPKVLLLDEPFGALDPGIRAEIhtlMKRLWNETQ-MTVVMVTHDMREAfTLATRVVAFERPR 218
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQAL---LADLLEALAgRTVLLITHRLAGL-ERMDRILVLEDGR 546
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-218 |
2.05e-35 |
|
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: 129.85 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 22 VSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL-PAEPG----PDR---GVVFQRYSVFPHLTVLGN 93
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGiflpPEKrriGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKElmaskykaKLFGQARRSAIDEARQLItevGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:TIGR02142 96 LRYGMK--------RARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 174 GIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-233 |
4.83e-35 |
|
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: 127.51 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVFQRYSVFPH 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRrsiGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVllgkELMAskykaKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:TIGR01188 81 LTGRENL----EMMG-----RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517136998 168 FGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEE-KERYGATITR 233
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRiiaeGTPEElKRRLGKDTLE 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-212 |
1.29e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 126.38 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPG------PD-RG 76
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigylPEeRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 77 vvfqrysVFPHLTVlGNVLLgkelmaskYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALI 156
Cdd:COG4152 82 -------LYPKMKV-GEQLV--------YLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 157 MKPKVLLLDEPFGALDP----GIRAEIHTLMKRlwnetQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG4152 146 HDPELLILDEPFSGLDPvnveLLKDVIRELAAK-----GTTVIFSSHQMELVEELCDRIV 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-212 |
6.10e-34 |
|
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: 122.39 E-value: 6.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGVVFQRYS 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVLGNVLlgkelmaskYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:cd03269 81 LYPKMKVIDQLV---------YLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 164 LDEPFGALDPgIRAEihtLMKRLWNETQ---MTVVMVTHDMREAFTLATRVV 212
Cdd:cd03269 152 LDEPFSGLDP-VNVE---LLKDVIRELAragKTVILSTHQMELVEELCDRVL 199
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-200 |
7.84e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 123.30 E-value: 7.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD----RGVVFQRYSV-FPh 87
Cdd:COG4559 11 LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAVLPQHSSLaFP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGKElmaskykAKLFGQARRSAIdeARQLITEVGLSG-AETKYPaQLSGGMQQRLALAQALI-------MKP 159
Cdd:COG4559 90 FTVEEVVALGRA-------PHGSSAAQDRQI--VREALALVGLAHlAGRSYQ-TLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 160 KVLLLDEPFGALDPgirAEIHTLMK--RLWNETQMTVVMVTHD 200
Cdd:COG4559 160 RWLFLDEPTSALDL---AHQHAVLRlaRQLARRGGGVVAVLHD 199
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-212 |
1.68e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 122.50 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 17 IVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQRYSV--FPHLTV 90
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakyiGRVFQDPMMgtAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVLlgkelMASKyKAKLFGQAR---RSAIDEARQLITEVGLsGAETKYPAQ---LSGGMQQRLALAQALIMKPKVLLL 164
Cdd:COG1101 100 EENLA-----LAYR-RGKRRGLRRgltKKRRELFRELLATLGL-GLENRLDTKvglLSGGQRQALSLLMATLTKPKLLLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 165 DEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1101 173 DEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLI 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-201 |
2.65e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 124.14 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELI-IDSVWKEYGDQIV-LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD---- 74
Cdd:PRK11153 1 MIELKnISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 75 R---GVVFQRYSVFPHLTVLGNVLLGKELmASKYKAKLfgQARrsaIDEarqLITEVGLSGAETKYPAQLSGGMQQRLAL 151
Cdd:PRK11153 81 RrqiGMIFQHFNLLSSRTVFDNVALPLEL-AGTPKAEI--KAR---VTE---LLELVGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 152 AQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEM 201
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-208 |
4.90e-33 |
|
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: 120.20 E-value: 4.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGVVFQRYS 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVLGNVllgkelmasKYKAKLFGqARRSAIDEarqLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:TIGR03740 81 LYENLTARENL---------KVHTTLLG-LPDSRIDE---VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517136998 164 LDEPFGALDP-GIRaEIHTLMkRLWNETQMTVVMVTHDMREAFTLA 208
Cdd:TIGR03740 148 LDEPTNGLDPiGIQ-ELRELI-RSFPEQGITVILSSHILSEVQQLA 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-260 |
5.33e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.90 E-value: 5.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 9 VWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP------AEpgpDRGV--VFQ 80
Cdd:COG1129 10 ISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQ---AAGIaiIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLLGKELMaskyKAKLFGqaRRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:COG1129 87 ELNLVPNLSVAENIFLGREPR----RGGLID--WRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 161 VLLLDEPFGALDPgirAEIHTL---MKRLwNETQMTVVMVTHDMREAFTLATRVVAFerpRDrpeekeryGATI-TRDIS 236
Cdd:COG1129 161 VLILDEPTASLTE---REVERLfriIRRL-KAQGVAIIYISHRLDEVFEIADRVTVL---RD--------GRLVgTGPVA 225
|
250 260 270
....*....|....*....|....*....|...
gi 517136998 237 IWPPRR-----AG-ELSYFSPDR---DGPVVLQ 260
Cdd:COG1129 226 ELTEDElvrlmVGrELEDLFPKRaaaPGEVVLE 258
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-199 |
5.83e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 126.43 E-value: 5.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD-R---GVVFQRYSVFpHLT 89
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlRrqiGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGK------ELMASkykaklfgqARRSAIDE-ARQLI----TEVGLSGaetkypAQLSGGMQQRLALAQALIMK 158
Cdd:COG1132 430 IRENIRYGRpdatdeEVEEA---------AKAAQAHEfIEALPdgydTVVGERG------VNLSGGQRQRIAIARALLKD 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 159 PKVLLLDEPFGALDPG----IRAEIHTLMKrlwnetQMTVVMVTH 199
Cdd:COG1132 495 PPILILDEATSALDTEtealIQEALERLMK------GRTTIVIAH 533
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-223 |
7.09e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 120.87 E-value: 7.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPG---PDRGVV--FQRYSVFPH 87
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVL------LGKELMASKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK11300 95 MTVIENLLvaqhqqLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEE 223
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTplanGTPEE 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-215 |
1.38e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 123.22 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 3 ELIIDSVwkeyGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP----AEPGPDR--- 75
Cdd:PRK10070 32 EQILEKT----GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrkk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 -GVVFQRYSVFPHLTVLGNVLLGKELMASKYKAKlfgqaRRSAIDEARQliteVGLSGAETKYPAQLSGGMQQRLALAQA 154
Cdd:PRK10070 108 iAMVFQSFALMPHMTVLDNTAFGMELAGINAEER-----REKALDALRQ----VGLENYAHSYPDELSGGMRQRVGLARA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517136998 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-211 |
1.40e-32 |
|
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: 119.18 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVF- 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 -QRYSVFPHLTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIR---------GLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRV 211
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRA 203
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-201 |
1.59e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 121.76 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD-----RGV--VFQR-YSVF-PHLT 89
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMqmVFQDpYASLnPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 V---LGNVLlgkelmaskykaKLFGQARRSAIDE-ARQLITEVGLSgAE--TKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:COG4608 114 VgdiIAEPL------------RIHGLASKAERRErVAELLELVGLR-PEhaDRYPHEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 517136998 164 LDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDL 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-212 |
1.76e-32 |
|
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: 118.13 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 5 IIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEpgpDR----GVVFQ 80
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERrksiGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 --RYSVFPHlTVLGNVLLGKELmASKYKAKlfgqarrsaideARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:cd03226 79 dvDYQLFTD-SVREELLLGLKE-LDAGNEQ------------AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVV 212
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVL 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-212 |
2.27e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 117.72 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAepgpdrgVVFQRYSV---FPhLT 89
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA-------YVPQRSEVpdsLP-LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGkeLMASKYKAKLFGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:NF040873 74 VRDLVAMG--RWARRGLWRRLTRDDRAAVDDA---LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 170 ALDPGIRAEIHTLMKRlWNETQMTVVMVTHDMrEAFTLATRVV 212
Cdd:NF040873 149 GLDAESRERIIALLAE-EHARGATVVVVTHDL-ELVRRADPCV 189
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
3.06e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.12 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 16 QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--------GVVFQrysvFPH 87
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkplrkkvGIVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 L-----TVLGNVLLGkelmaskykAKLFGQARRSAIDEARQLITEVGLSGA-ETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK13634 96 HqlfeeTVEKDICFG---------PMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHK 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-212 |
7.38e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.95 E-value: 7.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----PAEPGPDRGVVFQRYSV-FPh 87
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwsPAELARRRAVLPQHSSLsFP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGKELMASKYKAKlfgqarRSAIDEArqlITEVGLSG-AETKYPaQLSGGMQQRLALAQALI------MKPK 160
Cdd:PRK13548 91 FTVEEVVAMGRAPHGLSRAED------DALVAAA---LAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 161 VLLLDEPFGALDpgIRAEIHTL--MKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK13548 161 WLLLDEPTSALD--LAHQHHVLrlARQLAHERGLAVIVVLHDLNLAARYADRIV 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-212 |
1.12e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.06 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAePGP----DRGV--VFQRYSV 84
Cdd:COG3845 13 KRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI-RSPrdaiALGIgmVHQHFML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 85 FPHLTVLGNVLLGKElmaskyKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:COG3845 92 VPNLTVAENIVLGLE------PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 165 DEPFGALDPgirAEIHTLMKRLWN--ETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG3845 166 DEPTAVLTP---QEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVT 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-214 |
2.43e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 116.87 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRML-----LGQERPTRGTILLDGEPL------PAEPGPDRGVVFQR 81
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIyspdvdPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVLLGkelmaskykAKLFGQAR-RSAIDEarqlITEVGLSGA----ETK-----YPAQLSGGMQQRLAL 151
Cdd:PRK14267 94 PNPFPHLTIYDNVAIG---------VKLNGLVKsKKELDE----RVEWALKKAalwdEVKdrlndYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 152 AQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNEtqMTVVMVTHDMREAFTLATrVVAF 214
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSD-YVAF 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-218 |
3.37e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.39 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIID--SVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--- 75
Cdd:PRK13536 37 MSTVAIDlaGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARari 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 GVVFQRYSVFPHLTVLGNVLLgkelmASKYkaklFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQAL 155
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLV-----FGRY----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRaeiHTLMKRLWN--ETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHAR---HLIWERLRSllARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-216 |
4.26e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.55 E-value: 4.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDgeplpaePGPDRGVVFQRYSVF 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-------KGLRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PHLTVLGNVLLG-KELMASKYK------------------AKLfgQARRSAID------EARQLITEVGLSGAETKYP-A 139
Cdd:COG0488 74 DDLTVLDTVLDGdAELRALEAEleeleaklaepdedlerlAEL--QEEFEALGgweaeaRAEEILSGLGFPEEDLDRPvS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 140 QLSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgiraeIHTLmkrLWNET-----QMTVVMVTHDmREaF--TLATRVV 212
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESI---EWLEEflknyPGTVLVVSHD-RY-FldRVATRIL 220
|
....
gi 517136998 213 AFER 216
Cdd:COG0488 221 ELDR 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-212 |
9.15e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.92 E-value: 9.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP------AEPGPDRGVVFQ--RYSVFPHlTV 90
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvklSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 lgnvllgkelmaskYKAKLFGQARRSAIDE-----ARQLITEVGLS--GAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK13637 102 --------------EKDIAFGPINLGLSEEeienrVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517136998 164 LDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
4-212 |
9.34e-31 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 115.30 E-value: 9.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGD----QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILL---DGEPLP--AEPGPD 74
Cdd:COG4107 9 LSVRGLSKRYGPgcgtVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYrdrDGGPRDlfALSEAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 75 R--------GVVFQRysvfPHL------TVLGNVllGKELMASKykAKLFGQARrsaiDEARQLITEVGLSGAETK-YPA 139
Cdd:COG4107 89 RrrlrrtdwGMVYQN----PRDglrmdvSAGGNI--AERLMAAG--ERHYGDIR----ARALEWLERVEIPLERIDdLPR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 140 QLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG4107 157 TFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTM 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-212 |
9.49e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.55 E-value: 9.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEY---------GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 72 GPDRG-------VVFQ--------RYSV-------FPHLTVLGnvllgkelmaskykaklfgQARRSAidEARQLITEVG 129
Cdd:PRK10419 81 RAQRKafrrdiqMVFQdsisavnpRKTVreiirepLRHLLSLD-------------------KAERLA--RASEMLRAVD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 130 LSGAE-TKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLA 208
Cdd:PRK10419 140 LDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFC 219
|
....
gi 517136998 209 TRVV 212
Cdd:PRK10419 220 QRVM 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-208 |
1.18e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 115.25 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPA-------EPGPDRGVVFQRYSVFP 86
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsrlyTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTVLGNVL--------LGKELMASKYKAKLfgqarrsaidEArqliteVGLSGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:PRK11831 98 DMNVFDNVAyplrehtqLPAPLLHSTVMMKL----------EA------VGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLA 208
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIA 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-204 |
1.79e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 113.72 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--------GVVFQRYSVFPHLT 89
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakhvGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLgkelmaskyKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK10584 105 ALENVEL---------PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|....*
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREA 204
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-185 |
1.93e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.97 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgpdrgvVFQ 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP------MHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 R------Y-----SVFPHLTVLGNVLLGKELmaskykAKLFGQARRsaiDEARQLITEVGLSGAETKYPAQLSGGMQQRL 149
Cdd:COG1137 75 RarlgigYlpqeaSIFRKLTVEDNILAVLEL------RKLSKKERE---ERLEELLEEFGITHLRKSKAYSLSGGERRRV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517136998 150 ALAQALIMKPKVLLLDEPFGALDP----GIRAEIHTLMKR 185
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPiavaDIQKIIRHLKER 185
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-215 |
3.50e-30 |
|
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: 113.64 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRG-TILLDGEPLPAEPGPD-R---GVV----FQRYS 83
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWElRkriGLVspalQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 vfPHLTVLGNVLLGkelmaskykakLFGQARR----SAIDE--ARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIM 157
Cdd:COG1119 93 --RDETVLDVVLSG-----------FFDSIGLyrepTDEQRerARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-199 |
3.95e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 113.47 E-value: 3.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRML-----LGQERPTRGTILLDGEPLPAEPGPD- 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 75 -RGV--VFQRYSVFPHLTVLGNVLLGKEL-MASKYKAKLFGQARRsAIDEArQLITEVGlsgAETKYPA-QLSGGMQQRL 149
Cdd:PRK14247 81 rRRVqmVFQIPNPIPNLSIFENVALGLKLnRLVKSKKELQERVRW-ALEKA-QLWDEVK---DRLDAPAgKLSGGQQQRL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNEtqMTVVMVTH 199
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTH 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-212 |
4.18e-30 |
|
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: 118.25 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQErPTRGTILLDGEPLPAEPGPDR-------GVVFQR-YSVF-PHLT 89
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALrplrrrmQVVFQDpFGSLsPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VL-----GNVLLGKELMAskykaklfgQARRsaiDEARQLITEVGLS-GAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:COG4172 381 VGqiiaeGLRVHGPGLSA---------AERR---ARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517136998 164 LDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVM 497
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
9-218 |
4.44e-30 |
|
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: 113.75 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 9 VWKEyGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR-------GVVFQR 81
Cdd:TIGR02769 18 FGAK-QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRrafrrdvQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 Y--SVFPHLTVlgNVLLGKELmasKYKAKLFGQARRSAIDEarqLITEVGL-SGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:TIGR02769 97 SpsAVNPRMTV--RQIIGEPL---RHLTSLDESEQKARIAE---LLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:TIGR02769 169 PKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
14-201 |
1.14e-29 |
|
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: 116.71 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKS----TFLRMLLGQERPTRGTILLDGEPLPAEP--------GPDRGVVFQR 81
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSerelrrirGNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 --YSVFPHLTVlgnvllGKELMAS-KYKAKLFGQARRSaidEARQLITEVGLSGAETK---YPAQLSGGMQQRLALAQAL 155
Cdd:COG4172 101 pmTSLNPLHTI------GKQIAEVlRLHRGLSGAAARA---RALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-200 |
1.15e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.52 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGT--------ILLDGEPLPAEPGPDRGVVFQRYSVFPHLT 89
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADALAQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVllgkelmasKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK10535 103 AAQNV---------EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190
....*....|....*....|....*....|.
gi 517136998 170 ALDPGIRAEIHTLMKRLwNETQMTVVMVTHD 200
Cdd:PRK10535 174 ALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-235 |
1.24e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.36 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIID--SVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--- 75
Cdd:PRK13537 3 MSVAPIDfrNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 GVVFQRYSVFPHLTVLGNVLlgkelmaskykakLFGQARRSAIDEARQLI-TEVGLSGAETKYPAQ---LSGGMQQRLAL 151
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLL-------------VFGRYFGLSAAAARALVpPLLEFAKLENKADAKvgeLSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 152 AQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVVAFERPRDRPEEKERygATI 231
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPH--ALI 226
|
....
gi 517136998 232 TRDI 235
Cdd:PRK13537 227 ESEI 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-212 |
1.75e-29 |
|
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: 109.06 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPlpaepgpdrgvvfqrysvfphltv 90
Cdd:cd03216 8 KRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 lgnvllgkelmaskykaklfgQARRSAIDeARQLitevglsGAETKYpaQLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:cd03216 64 ---------------------VSFASPRD-ARRA-------GIAMVY--QLSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517136998 171 LDPGIRAEIHTLMKRLWNEtQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVT 153
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-204 |
2.46e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.80 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRM------LLGQERpTRGTILLDGEPL------PAEPGPDRGVVFQ 80
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFR-VEGKVTFHGKNLyapdvdPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHlTVLGNVLLGKELMAskYKA---KLFGQARRSAI--DEARQLITEVGLSgaetkypaqLSGGMQQRLALAQAL 155
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYGARING--YKGdmdELVERSLRQAAlwDEVKDKLKQSGLS---------LSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTHDMREA 204
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQA 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-213 |
2.56e-29 |
|
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: 115.85 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQRYSVFPHlTVLGN 93
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWrdqiAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKeLMASkyKAKLFGQARRSAIDEARQ-----LITEVGLSGAEtkypaqLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:TIGR02857 416 IRLAR-PDAS--DAEIREALERAGLDEFVAalpqgLDTPIGEGGAG------LSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 169 GALDPGIRAEIHTLMKRLWNetQMTVVMVTHDmREAFTLATRVVA 213
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVV 528
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-214 |
6.91e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.25 E-value: 6.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIID----SVWkeYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRML-----LGQERPTRGTILLDGEPLPAeP 71
Cdd:PRK14239 1 MTEPILQvsdlSVY--YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYS-P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 72 GPDR-------GVVFQRYSVFPhLTVLGNVLLGKELMASKYKAKLFGQARRSAI-----DEARQLITEVGLSgaetkypa 139
Cdd:PRK14239 78 RTDTvdlrkeiGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKgasiwDEVKDRLHDSALG-------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 140 qLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTHDMREAFTLATRVVAF 214
Cdd:PRK14239 149 -LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFF 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-200 |
1.18e-28 |
|
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: 107.89 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEpgpDRGVVFQRYSVFphlTVLGN 93
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYS---RKGLLERRQRVG---LVFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 -------VLLGKELMASKYKAKLFGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:TIGR01166 77 pddqlfaADVDQDVAFGPLNLGLSEAEVERRVREA---LTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|....
gi 517136998 167 PFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHD 200
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRL-RAEGMTVVISTHD 186
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
1.66e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 109.36 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELI----IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRML-----LGQERPTRGTILLDGEPL-PAE 70
Cdd:PRK14258 1 MSKLIpaikVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIyERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 71 PGPDR-----GVVFQRYSVFPhLTVLGNVLLGKELMASKYKAKLFGQArRSAIDEArQLITEVglSGAETKYPAQLSGGM 145
Cdd:PRK14258 81 VNLNRlrrqvSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIV-ESALKDA-DLWDEI--KHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 146 QQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPRDRPEEKE 225
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLV 235
|
....*
gi 517136998 226 RYGAT 230
Cdd:PRK14258 236 EFGLT 240
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-200 |
2.81e-28 |
|
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: 112.84 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDrgvVFQRYSVF---PHL-- 88
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRRVSVCaqdAHLfd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 -TVLGNVLLGK------ELMASKYKAKLfGQARRSAIDEARQLITEVGlsgaetkypAQLSGGMQQRLALAQALIMKPKV 161
Cdd:TIGR02868 423 tTVRENLRLARpdatdeELWAALERVGL-ADWLRALPDGLDTVLGEGG---------ARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMkrLWNETQMTVVMVTHD 200
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-212 |
3.09e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.95 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD-R---GVVFQRY-SVFPHLT 89
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvRrqvGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13635 99 VQDDVAFGLENI---------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTlATRVV 212
Cdd:PRK13635 170 MLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVI 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-218 |
1.10e-27 |
|
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: 106.30 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQ----IVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---G 76
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARrrlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 77 VVFQRYSVFPHLTVLGNVLlgkelmaskYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALI 156
Cdd:cd03266 82 FVSDSTGLYDRLTARENLE---------YFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-216 |
1.30e-27 |
|
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: 104.61 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----PAEPGPDRGVVFQRYSVFPHlT 89
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsqwdPNELGDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVllgkelmaskykaklfgqarrsaidearqlitevglsgaetkypaqLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:cd03246 92 IAENI----------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517136998 170 ALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMrEAFTLATRVVAFER 216
Cdd:cd03246 126 HLDVEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILVLED 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-214 |
1.32e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.38 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD-R---GVVFQRY-SVFPHLTVLG 92
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEiRkkiGIIFQNPdNQFIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLG---KELMASKYKAKlfgqarrsaIDEARQlitEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13632 104 DIAFGlenKKVPPKKMKDI---------IDDLAK---KVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAfTLATRVVAF 214
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVF 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-223 |
1.44e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 107.61 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--------GVVFQrysvFPHLTV 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklrkkvSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVLLgKELMaskYKAKLFGQARRSAIDEARQLITEVGLS-GAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13641 99 FENTVL-KDVE---FGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 170 ALDPGIRAEIHTLMKRlWNETQMTVVMVTHDMREAFTLATRVVAFERPR----DRPEE 223
Cdd:PRK13641 175 GLDPEGRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHGKlikhASPKE 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-218 |
1.68e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.14 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPA-----EPGPDR---GVVFQrysvFPHL-- 88
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRkkvGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 ---TVLGNVLLGKELmaskykaklFGQARRSAIDEARQLITEVGLSGA-ETKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:PRK13649 99 feeTVLKDVAFGPQN---------FGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 165 DEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-218 |
1.83e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.55 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILL---DGEP--LPAEPGPDR--- 75
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLrdLYALSEAERrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 -----GVVFQ--RYSVFPHLTVLGNVllGKELMASKykAKLFGQARRSA--------IDEARqlITEVglsgaetkyPAQ 140
Cdd:PRK11701 87 lrtewGFVHQhpRDGLRMQVSAGGNI--GERLMAVG--ARHYGDIRATAgdwlerveIDAAR--IDDL---------PTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 141 LSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-172 |
2.22e-27 |
|
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: 105.70 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLlgqER---PTRGTILLDGEPLPAEPGPDR----GVVFQRysvfPH 87
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDLNLRWLrsqiGLVSQE----PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 L---TVLGNVLLGKE--LMASKYKAKLFGQARRSAIDEARQLITEVGLSGaetkypAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:cd03249 88 LfdgTIAENIRYGKPdaTDEEVEEAAKKANIHDFIMSLPDGYDTLVGERG------SQLSGGQKQRIAIARALLRNPKIL 161
|
170
....*....|
gi 517136998 163 LLDEPFGALD 172
Cdd:cd03249 162 LLDEATSALD 171
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-218 |
3.32e-27 |
|
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: 105.21 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILL--DGEPLPAEPGPDR----------GVVFQRYSVF 85
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPReilalrrrtiGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PHLTVLgnvllgkELMASKYKAKlfGQARRSAIDEARQLITEVGLsgAE---TKYPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:COG4778 106 PRVSAL-------DVVAEPLLER--GVDREEARARARELLARLNL--PErlwDLPPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 163 LLDEPFGALDPGIRAE----IHTLMKRlwnetQMTVVMVTHDM--REAftLATRVVAFERPR 218
Cdd:COG4778 175 LLDEPTASLDAANRAVvvelIEEAKAR-----GTAIIGIFHDEevREA--VADRVVDVTPFS 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-216 |
3.44e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.87 E-value: 3.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLG---QERPTRGTILLDGEPLPAEPGPDR------- 75
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVQREGRLARdirksra 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 --GVVFQRYSVFPHLTVLGNVLLGKeLMASKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQ 153
Cdd:PRK09984 87 ntGYIFQQFNLVNRLSVLENVLIGA-LGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 154 ALIMKPKVLLLDEPFGALDP-GIRAEIHTLmkRLWNETQ-MTVVMVTHDMREAFTLATRVVAFER 216
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPeSARIVMDTL--RDINQNDgITVVVTLHQVDYALRYCERIVALRQ 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-212 |
7.03e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 7.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQRY-SVFPHLT 89
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIrhkiGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGKELMASKYkaklfgQARRSAIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13650 99 VEDDVAFGLENKGIPH------EEMKERVNEALEL---VGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAfTLATRVV 212
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVL 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-201 |
2.26e-26 |
|
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: 107.58 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTI-LLDGEPLP--AEPGPDR--------GVVFQRYSVFPH 87
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVdmTKPGPDGrgrakryiGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVL------LGKEL--MASKYKAKLFGQARrsaiDEARQLITevglsgaetKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:TIGR03269 380 RTVLDNLTeaigleLPDELarMKAVITLKMVGFDE----EKAEEILD---------KYPDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 160 KVLLLDEPFGALDPGIRAEI-HTLMKRLwNETQMTVVMVTHDM 201
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVtHSILKAR-EEMEQTFIIVSHDM 488
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-204 |
2.76e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 102.97 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR--------GVVFQRYSVFPHLT 89
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnqklGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNV----LLGkelmaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:PRK11629 104 ALENVamplLIG-------------KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517136998 166 EPFGALDPGIRAEIHTLMKRLwNETQMTV-VMVTHDMREA 204
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGEL-NRLQGTAfLVVTHDLQLA 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-235 |
3.33e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 103.64 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRG-----TILLDGEPL-----PAEPGPDRGVVFQRY 82
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyrdVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 83 SVFPhLTVLGNVLLGKElmaskyKAKLFGQARRSAIDEARqlITEVGLSGAE----TKYPAQLSGGMQQRLALAQALIMK 158
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVR------AHKLVPRKEFRGVAQAR--LTEVGLWDAVkdrlSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNetQMTVVMVTHDMREAFTLATRVVAF-------ERPRDR----PEEKE-- 225
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFfdgrlveEGPTEQlfssPKHAEta 259
|
250
....*....|
gi 517136998 226 RYGATITRDI 235
Cdd:PRK14271 260 RYVAGLSGDV 269
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-216 |
3.54e-26 |
|
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: 99.83 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDgeplpaepgpdrgvvfqrys 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 vfphltvlgnvllgkelmaskykaklfgqarrsaidearqlitevglSGAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:cd03221 61 -----------------------------------------------STVKIGYFEQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 164 LDEPFGALD-PGIRAEIHTLmkrlwNETQMTVVMVTHDmrEAF--TLATRVVAFER 216
Cdd:cd03221 94 LDEPTNHLDlESIEALEEAL-----KEYPGTVILVSHD--RYFldQVATKIIELED 142
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-214 |
3.58e-26 |
|
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: 100.97 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVF-----QRYSVFPHLT 89
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYvpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLgkelmaskykaklfgqarrsaidearqlitevglsgaetkyPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:cd03215 95 VAENIAL-----------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 170 ALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAF 214
Cdd:cd03215 134 GVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVM 177
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-199 |
4.87e-26 |
|
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: 101.28 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP-AEPGPDRGVVF--QRYSVFPHLTV 90
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeQRDEPHENILYlgHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVllgkelmasKYKAKLFGQARRSaIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:TIGR01189 91 LENL---------HFWAAIHGGAQRT-IEDA---LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 517136998 171 LDPGIRAEIHTLMkRLWNETQMTVVMVTH 199
Cdd:TIGR01189 158 LDKAGVALLAGLL-RAHLARGGIVLLTTH 185
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
1.96e-25 |
|
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: 100.36 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----PAEPGPDRGVVFQRYSVFpHLTVLGN 93
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldPADLRRNIGYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGK------ELMASkykaklfgqARRSAIDE-----ARQLITEVGLSGaetkypAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:cd03245 98 ITLGApladdeRILRA---------AELAGVTDfvnkhPNGLDLQIGERG------RGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517136998 163 LLDEPFGALDpgIRAEIHtLMKRLWNET-QMTVVMVTHDMReAFTLATRVVAFERPR 218
Cdd:cd03245 163 LLDEPTSAMD--MNSEER-LKERLRQLLgDKTLIIITHRPS-LLDLVDRIIVMDSGR 215
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-201 |
2.16e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 102.35 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPaepGPDRG----------VVFQR-Y-SVFP 86
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL---KADPEaqkllrqkiqIVFQNpYgSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTVlGNVLlgKELMAskYKAKLFGQARRsaiDEARQLITEVGLSgAE--TKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:PRK11308 108 RKKV-GQIL--EEPLL--INTSLSAAERR---EKALAMMAKVGLR-PEhyDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 517136998 165 DEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-203 |
2.42e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgPDR-----GVV 78
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-PEIyrqqvSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRYSVFPHlTVLGNVLLGKELMASKYKAKLFgqarrsAIDEARQLITEVGLsgaeTKYPAQLSGGMQQRLALAQALIMK 158
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIF------LDDLERFALPDTIL----TKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMRE 203
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-199 |
4.87e-25 |
|
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: 99.47 E-value: 4.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPA---------------EPgpdrgVVF 79
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylhskvslvgqEP-----VLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRysvfphlTVLGNV---LLGKELM-----ASKYKAKLFGQARRSAIDearqliTEVGLSGaetkypAQLSGGMQQRLAL 151
Cdd:cd03248 101 AR-------SLQDNIaygLQSCSFEcvkeaAQKAHAHSFISELASGYD------TEVGEKG------SQLSGGQKQRVAI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 152 AQALIMKPKVLLLDEPFGALDPGIRAEIHTLMkRLWNETQmTVVMVTH 199
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQAL-YDWPERR-TVLVIAH 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-210 |
5.15e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.58 E-value: 5.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEP---LPAEPGPDRGV 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDislLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VF--QRYSVFPHLTVLGNvllgkeLMASKYKAKLFGQARRSaiDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQAL 155
Cdd:PRK10895 81 GYlpQEASIFRRLSVYDN------LMAVLQIRDDLSAEQRE--DRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATR 210
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCER 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-212 |
5.86e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 103.63 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKST----FLRMLlgqerPTRGTILLDGEPL----PAEPGPDR---GVVFQ-- 80
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLhnlnRRQLLPVRhriQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLLGKELmaskYKAKLFGQARRSAIDEARQlitEVGLSgAETK--YPAQLSGGMQQRLALAQALIMK 158
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRV----HQPTLSAAQREQQVIAVME---EVGLD-PETRhrYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVI 497
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-214 |
6.25e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.77 E-value: 6.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQR 81
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELakrlAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVlgnvllgKELMAskykaklFG-----QARRSAIDEA--RQLITEVGLSGAETKYPAQLSGGMQQRLALAQA 154
Cdd:COG4604 84 NHINSRLTV-------RELVA-------FGrfpysKGRLTAEDREiiDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAF 214
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-199 |
1.87e-24 |
|
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: 96.85 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIvLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERP--TRGTILLDGEPLPAEPGPDR-GVVFQRY 82
Cdd:cd03213 13 VKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKIiGYVPQDD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 83 SVFPHLTVlgnvllgKELMasKYKAKLFGqarrsaidearqlitevglsgaetkypaqLSGGMQQRLALAQALIMKPKVL 162
Cdd:cd03213 92 ILHPTLTV-------RETL--MFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190
....*....|....*....|....*....|....*..
gi 517136998 163 LLDEPFGALDPGIRAEIHTLMKRLWNeTQMTVVMVTH 199
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIH 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-212 |
2.03e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVasRA--FVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAePGP----DRGVVF-----QRYSVFP 86
Cdd:COG1129 267 VVRDVSFSV--RAgeILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI-RSPrdaiRAGIAYvpedrKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTVLGNVLLgkelmASKYKAKLFGQARRSAIDE-ARQLITEVGLSGAETKYPAQ-LSGGMQQRLALAQALIMKPKVLLL 164
Cdd:COG1129 344 DLSIRENITL-----ASLDRLSRGGLLDRRRERAlAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 165 DEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRIL 465
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
2.20e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVA--SRafVALVGPSGCGKSTFLRMLLGQERPTRGTIlldgeplpaEPGPdrGVVF-- 79
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDrgDR--IGLIGPNGAGKSTLLKLLAGELEPDSGTV---------KLGE--TVKIgy 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 --QRYSVF-PHLTVLGNVLLGKELMASKykaklfgqarrsaidEARQLITEVGLSGAE-TKYPAQLSGGMQQRLALAQAL 155
Cdd:COG0488 383 fdQHQEELdPDKTVLDELRDGAPGGTEQ---------------EVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517136998 156 IMKPKVLLLDEPFGALDpgiraeIHTL--MKRLWNETQMTVVMVTHDmREaF--TLATRVVAFE 215
Cdd:COG0488 448 LSPPNVLLLDEPTNHLD------IETLeaLEEALDDFPGTVLLVSHD-RY-FldRVATRILEFE 503
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-204 |
2.42e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.16 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAepgpdrgvvFQRYSVFPHLTVLG 92
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM---------LSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLG------KELMA---SKYKAkLFGqaRRSAIDEAR--QLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK11231 83 QHHLTpegitvRELVAygrSPWLS-LWG--RLSAEDNARvnQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREA 204
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQA 201
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-218 |
5.76e-24 |
|
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: 97.21 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTI---LLDGEP--LPAEPGPDR--------GV 77
Cdd:TIGR02323 11 KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyiMRSGAEleLYQLSEAERrrlmrtewGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQRYSVFPHLTVLGNVLLGKELMASKykAKLFGQARRSAIDEARQLitEVGLSGAETKyPAQLSGGMQQRLALAQALIM 157
Cdd:TIGR02323 91 VHQNPRDGLRMRVSAGANIGERLMAIG--ARHYGNIRATAQDWLEEV--EIDPTRIDDL-PRAFSGGMQQRLQIARNLVT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:TIGR02323 166 RPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGR 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-199 |
7.61e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.57 E-value: 7.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP---------------AEPgpdrgVVF 79
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydhhylhrqvalvgQEP-----VLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRysvfphlTVLGNVLLG------KELMASKYKAKLfgqarRSAIDEARQLI-TEVGLSGaetkypAQLSGGMQQRLALA 152
Cdd:TIGR00958 568 SG-------SVRENIAYGltdtpdEEIMAAAKAANA-----HDFIMEFPNGYdTEVGEKG------SQLSGGQKQRIAIA 629
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517136998 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRlwneTQMTVVMVTH 199
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSR----ASRTVLLIAH 672
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-202 |
1.25e-23 |
|
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: 95.51 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 21 NVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERP----TRGTILLDGEPLPAEP--GPDRGVVFQ--RYSVFPHLTvlg 92
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSirGRHIATIMQnpRTAFNPLFT--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 nvllgkelMASKYKAKLfgQARRSAIDEARQLITE----VGLSGAET---KYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:TIGR02770 81 --------MGNHAIETL--RSLGKLSKQARALILEaleaVGLPDPEEvlkKYPFQLSGGMLQRVMIALALLLEPPFLIAD 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 517136998 166 EPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMR 202
Cdd:TIGR02770 151 EPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLG 187
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-211 |
2.16e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.91 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP------AEPGPDRGVVFQRY--SVFPHlT 89
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkkslLEVRKTVGIVFQNPddQLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13639 96 VEEDVAFGPLNL---------GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517136998 170 ALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRV 211
Cdd:PRK13639 167 GLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKV 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-216 |
2.28e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGT-----ILLDGEPLPAEPGPDR---GVVFQrysvFPHL-- 88
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdIVVSSTSKQKEIKPVRkkvGVVFQ----FPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 ---TVLGNVLLGKELmaskykaklFGQARRSAIDEARQLITEVGLSGA-ETKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:PRK13643 98 feeTVLKDVAFGPQN---------FGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 165 DEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:PRK13643 169 DEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEK 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-212 |
3.31e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.00 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPG-----PDR---GVVFQrysvFPHlTV 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRkriGMVFQ----FPE-SQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVLLGKELMaskYKAKLFGQARRSAIDEARQLITEVGLS-GAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13646 98 LFEDTVEREII---FGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVI 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-204 |
3.79e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.20 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQR-YSVFPHLTVLGN 93
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLrkhiGIVFQNpDNQFVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKELMASKYKaklfgqarrSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK13648 105 VAFGLENHAVPYD---------EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190
....*....|....*....|....*....|.
gi 517136998 174 GIRAEIHTLMKRLWNETQMTVVMVTHDMREA 204
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-204 |
4.65e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERP---TRGTILLDGEPLPAEPGPD----RGVVFQRY-SVFPHLT 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDirekVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK13640 102 VGDDVAFGLENR---------AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190
....*....|....*....|....*....|....*
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREA 204
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-199 |
4.86e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 94.21 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 2 SELIIDSVWKEY-GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgpdR----- 75
Cdd:cd03254 1 GEIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---Rkslrs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 --GVVFQRYSVFPHlTVLGNVLLGKELMASKYKAKLFGQARrsAIDEARQLI----TEVGLSGaetkypAQLSGGMQQRL 149
Cdd:cd03254 78 miGVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAG--AHDFIMKLPngydTVLGENG------GNLSQGERQLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 150 ALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETqmTVVMVTH 199
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAH 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-216 |
5.45e-23 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 93.75 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAepgPDRGVVFQrysvfPHLTV 90
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL---LGLGGGFN-----PELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVllgkelmasKYKAKLFGQARrsaiDEARQLITEV-GLSGAETKYPAQL---SGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:cd03220 102 RENI---------YLNGRLLGLSR----KEIDEKIDEIiEFSELGDFIDLPVktySSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 167 PFGALDPGIRAEIHTLMKRLWnETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-216 |
6.60e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 21 NVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL-PAEPG----PDR---GVVFQRYSVFPHLTVLG 92
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfDAEKGiclpPEKrriGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLGkelMASKYKAKlFGQArrsaidearqliteVGLSGAE---TKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK11144 96 NLRYG---MAKSMVAQ-FDKI--------------VALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQ 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-223 |
1.28e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 12 EYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPA----EPGPDRGVVFQRYSVFPH 87
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlsarAASRRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGKELMASKYKAklFGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:PRK09536 92 FDVRQVVEMGRTPHRSRFDT--WTETDRAAVERA---MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 168 FGALDpgIRAEIHTL-MKRLWNETQMTVVMVTHDMreafTLATR------VVAFERPRD--RPEE 223
Cdd:PRK09536 167 TASLD--INHQVRTLeLVRRLVDDGKTAVAAIHDL----DLAARycdelvLLADGRVRAagPPAD 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-199 |
1.58e-22 |
|
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: 96.41 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQE--RPTRGTIL----------------LDGEPL 67
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpsKVGEPC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 68 PA-----EP------GPDR----------GVVFQR-YSVFPHLTVLGNVLlgKELMASKYKAKlfgqarrSAIDEARQLI 125
Cdd:TIGR03269 83 PVcggtlEPeevdfwNLSDklrrrirkriAIMLQRtFALYGDDTVLDNVL--EALEEIGYEGK-------EAVGRAVDLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517136998 126 TEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTH 199
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-201 |
1.83e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.25 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 7 DSVWKEY-GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP-----AEPGPDR--GVV 78
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRqiGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRYSVFPHLTVLGNVLLgkELMASKYKAKLFGQARRSAIDEarqliteVGLSGAETKYPAQLSGGMQQRLALAQALIMK 158
Cdd:PRK10908 85 FQDHHLLMDRTVYDNVAI--PLIIAGASGDDIRRRVSAALDK-------VGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRlWNETQMTVVMVTHDM 201
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEE-FNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-218 |
2.17e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD----RGVVFQRY--SVFPH 87
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfVGLVFQNPddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 lTVLGNVLLGKELMAskykakLFGQARRSAIDEARQLiteVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:PRK13652 95 -TVEQDIAFGPINLG------LDEETVAHRVSSALHM---LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517136998 168 FGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-212 |
3.15e-22 |
|
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: 92.01 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEplpaEPGPDR-------GVVF-QRY 82
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRkkflrriGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 83 SVFPHLTVLGnvllGKELMASKYKAKLFG-QARRSAIDEARQLitevglsGAETKYPA-QLSGGMQQRLALAQALIMKPK 160
Cdd:cd03267 105 QLWWDLPVID----SFYLLAAIYDLPPARfKKRLDELSELLDL-------EELLDTPVrQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVL 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-214 |
4.14e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTI---LLDGEPLPAEPGPDR------------------- 75
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEKvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 ------GVVFQ--RYSVFPHlTVLGNVLLGkelmaskykAKLFGQARRSAIDEARQLITEVGLSgaET---KYPAQLSGG 144
Cdd:PRK13651 102 eirrrvGVVFQfaEYQLFEQ-TIEKDIIFG---------PVSMGVSKEEAKKRAAKYIELVGLD--ESylqRSPFELSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 145 MQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVVAF 214
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-199 |
4.59e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 95.17 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEY-GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP--AEPGPDRGV-VFQR 81
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSslSHSVLRQGVaMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 82 YSVFPHLTVLGNVLLGKELMASKYKAKLfgqarrsaidEARQLITEV-GLS-GAETKYPAQ---LSGGMQQRLALAQALI 156
Cdd:PRK10790 423 DPVVLADTFLANVTLGRDISEEQVWQAL----------ETVQLAELArSLPdGLYTPLGEQgnnLSVGQKQLLALARVLV 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETqmTVVMVTH 199
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAH 533
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-202 |
7.98e-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: 94.43 E-value: 7.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----PAEPGPDRGVVFQRYSVFPhlt 89
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwdREELGRHIGYLPQDVELFD--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 vlGNVllgKELMAskykakLFGQARRSAIDEARQLI--------------TEVGLSGaetkypAQLSGGMQQRLALAQAL 155
Cdd:COG4618 420 --GTI---AENIA------RFGDADPEKVVAAAKLAgvhemilrlpdgydTRIGEGG------ARLSGGQRQRIGLARAL 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 156 IMKPKVLLLDEPFGALDP-GIRAEIHTL--MKrlwnETQMTVVMVTHDMR 202
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDeGEAALAAAIraLK----ARGATVVVITHRPS 528
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-211 |
1.13e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.26 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----------PAEPGPDRGVVFQRYSV 84
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 85 FPHLTVLGNVllgkelmasKYKAKLFGQARRSAIDE-ARQLITEVGLSGA---ETKYPA-QLSGGMQQRLALAQALIMKP 159
Cdd:PRK14246 102 FPHLSIYDNI---------AYPLKSHGIKEKREIKKiVEECLRKVGLWKEvydRLNSPAsQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWNEtqMTVVMVTHDMREAFTLATRV 211
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYV 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-199 |
1.43e-21 |
|
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: 88.91 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVFQRysvfPHL--- 88
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSsliSVLNQR----PYLfdt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TVLGNvlLGKelmaskykaklfgqarrsaidearqlitevglsgaetkypaQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:cd03247 90 TLRNN--LGR-----------------------------------------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190
....*....|....*....|....*....|..
gi 517136998 169 GALDPGIRAEI-HTLMKRLWNEtqmTVVMVTH 199
Cdd:cd03247 127 VGLDPITERQLlSLIFEVLKDK---TLIWITH 155
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
35-201 |
1.60e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.08 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 35 VGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPA-------EPGPDRGVVFQR--YSVFPHLTVlGNVLlGKELMAskY 105
Cdd:PRK15079 53 VGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddewrAVRSDIQMIFQDplASLNPRMTI-GEII-AEPLRT--Y 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 106 KAKLFGQARRsaiDEARQLITEVGL-SGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMK 184
Cdd:PRK15079 129 HPKLSRQEVK---DRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQ 205
|
170
....*....|....*..
gi 517136998 185 RLWNETQMTVVMVTHDM 201
Cdd:PRK15079 206 QLQREMGLSLIFIAHDL 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-199 |
1.68e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD-RG---VVFQRYSVFPHlT 89
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaisVVSQRVHLFSA-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGKElmaskykaklfgqarrSAIDEA-RQLITEVGLSG-AETKYP---------AQLSGGMQQRLALAQALIMK 158
Cdd:PRK11160 430 LRDNLLLAAP----------------NASDEAlIEVLQQVGLEKlLEDDKGlnawlgeggRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTH 199
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITH 532
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-204 |
1.74e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.92 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR----GVVFQRY-SVFPHLTVLGN 93
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLrrkiGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK13642 103 VAFGMENQ---------GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190
....*....|....*....|....*....|.
gi 517136998 174 GIRAEIHTLMKRLWNETQMTVVMVTHDMREA 204
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEA 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-212 |
1.80e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.14 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 3 ELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGE---PLpaepgpDRGVVF 79
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLL------ELGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QrysvfPHLTVLGNVLLGkelmaskykAKLFGqARRSAIDEARQLI---TEVGlsgaetKY---PAQ-LSGGMQQRLALA 152
Cdd:COG1134 100 H-----PELTGRENIYLN---------GRLLG-LSRKEIDEKFDEIvefAELG------DFidqPVKtYSSGMRARLAFA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 153 QALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVV 212
Cdd:COG1134 159 VATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAI 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-199 |
2.07e-21 |
|
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: 89.07 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 10 WKEYGDQI--VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGeplpaepgpdrGVVFqrYSVFPH 87
Cdd:cd03250 10 WDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAY--VSQEPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 L---TVLGNVLLGKELMASKYKAKLfgqarrsaidEARQLI-----------TEVGLSGAetkypaQLSGGMQQRLALAQ 153
Cdd:cd03250 77 IqngTIRENILFGKPFDEERYEKVI----------KACALEpdleilpdgdlTEIGEKGI------NLSGGQKQRISLAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 154 ALIMKPKVLLLDEPFGALDPGIRAEI--HTLMKRLWNETqmTVVMVTH 199
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNK--TRILVTH 186
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-216 |
2.37e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.45 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEpgpDRGVVFQRYS 83
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS---KRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VfphLTVLGNVllGKELMASKYKAKLFGQARRSAIDE---ARQLITEVGLSGAE--TKYPAQ-LSGGMQQRLALAQALIM 157
Cdd:PRK13638 79 V---ATVFQDP--EQQIFYTDIDSDIAFSLRNLGVPEaeiTRRVDEALTLVDAQhfRHQPIQcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMtVVMVTHDMREAFTLATRVVAFER 216
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQ 211
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-214 |
2.46e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----PAEPGPDRGVVFQRYSVFPHL 88
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyaSKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TVlgnvllgKELMA-SKYKAK-LFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PRK10253 97 TV-------QELVArGRYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 167 PFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAF 214
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-218 |
4.08e-21 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 93.15 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 9 VWKEYGDQIVlENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVFQRYSVF 85
Cdd:TIGR01257 937 IFEPSGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqslGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PHLTVLGNVLlgkelmaskYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:TIGR01257 1016 HHLTVAEHIL---------FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517136998 166 EPFGALDPGIRAEIHTLMkrLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-203 |
5.13e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 88.83 E-value: 5.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpaepgpdR-----------GVVFQRYS 83
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-------RevtldslrraiGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFpHLTVLGNVLLGKeLMASK---YKAklfgqARRSAIDEA-----RQLITEVGLSGaetkypAQLSGGMQQRLALAQAL 155
Cdd:cd03253 86 LF-NDTIGYNIRYGR-PDATDeevIEA-----AKAAQIHDKimrfpDGYDTIVGERG------LKLSGGEKQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwnETQMTVVMVTHDMRE 203
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLST 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-199 |
8.78e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.62 E-value: 8.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPlPAEPGPDRGVVF--QRYSVFPHLTVL 91
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYlgHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 GNVllgkelmasKYKAKLFGQaRRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGAL 171
Cdd:PRK13539 92 ENL---------EFWAAFLGG-EELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*...
gi 517136998 172 DPGIRAEIHTLMKRLWNETQMtVVMVTH 199
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGI-VIAATH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-199 |
1.44e-20 |
|
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: 86.78 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPaepgpdrgvvFQRYS 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD----------FQRDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVLGNVLLGKELMASKYKAKLFgqARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:cd03231 71 IARGLLYLGHAPGIKTTLSVLENLRFW--HADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 517136998 164 LDEPFGALDPGIRAEIHTLMKRLWNETQMtVVMVTH 199
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGM-VVLTTH 183
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-212 |
2.40e-20 |
|
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: 86.94 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERP---TRGTILLDGEPLPAEPGPDR-GVVFQRYSVFP 86
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCvAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTV-----LGNVLLGKELMASKYKAKLfgqarrsaidEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:cd03234 95 GLTVretltYTAILRLPRKSSDAIRKKR----------VEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMR-EAFTLATRVV 212
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQL-ARRNRIVILTIHQPRsDLFRLFDRIL 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-199 |
2.67e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLdgeplpaePGPDRgVVF--QR-YsvFPHLTvL 91
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR-VLFlpQRpY--LPLGT-L 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 GNVLLgkelmaskYKAklfgQARRSAIDEARQLITEVGLS------GAETKYPAQLSGGMQQRLALAQALIMKPKVLLLD 165
Cdd:COG4178 443 REALL--------YPA----TAEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190
....*....|....*....|....*....|....
gi 517136998 166 EPFGALDPGIRAEIHTLMKRLWNETqmTVVMVTH 199
Cdd:COG4178 511 EATSALDEENEAALYQLLREELPGT--TVISVGH 542
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-218 |
3.40e-20 |
|
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: 86.77 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLP-AEPGPDR---GVVFQRYSVFpHLTVLGN 93
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlADPAWLRrqvGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKELMASK---YKAKLFGqarrsAIDEARQLI----TEVGLSGaetkypAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:cd03252 96 IALADPGMSMErviEAAKLAG-----AHDFISELPegydTIVGEQG------AGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 167 PFGALDPGIRAEIHTLMKRLWneTQMTVVMVTHDMrEAFTLATRVVAFERPR 218
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRL-STVKNADRIIVMEKGR 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-218 |
5.45e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 86.29 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKS----TFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGV--VFQ--RYSV 84
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIatIMQnpRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 85 FPHLTvlgnvllgkelMASKYKAKLFGQARRSAIDEARQLITEVGLSGAET---KYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK10418 93 NPLHT-----------MHTHARETCLALGKPADDATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGR 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-199 |
5.49e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAepgpdrgvvfQRYSVFPHLTVLGN 93
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR----------QRDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 vLLG--KELMAS---KYKAKLFGQARRsaiDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:PRK13538 82 -QPGikTELTALenlRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|.
gi 517136998 169 GALDPGIRAEIHTLMKRLWNETQMtVVMVTH 199
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGGM-VILTTH 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-213 |
8.79e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.99 E-value: 8.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPA--EPGPDRGVVF--QRYSVFPHLTV 90
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsSKAFARKVAYlpQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVLLGKelmaSKYKAKL--FGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:PRK10575 103 RELVAIGR----YPWHGALgrFGAADREKVEEA---ISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 169 GALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVA 213
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVA 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-210 |
9.48e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.32 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGP-----DR 75
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimreAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 76 GVVFQRYSVFPHLTVLGNVLLGKeLMASKykaklfgQARRSAIDEARQLITEvgLSGAETKYPAQLSGGMQQRLALAQAL 155
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGG-FFAER-------DQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 156 IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATR 210
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADR 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
11-212 |
2.18e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.14 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPG-----PDRGVVFQRysvf 85
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdirNKAGMVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PH-----LTVLGNVLLGKELMASKYKAKlfgqarRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:PRK13633 94 PDnqivaTIVEEDVAFGPENLGIPPEEI------RERVDES---LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 161 VLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTlATRVV 212
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRII 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-199 |
3.24e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.82 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 3 ELIIDSvwkeYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQeRPTRGTILLDGEPLPA-EPGPDR---GVV 78
Cdd:PRK11174 354 DLEILS----PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRElDPESWRkhlSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRysvfPHL---TVLGNVLLGKELMAskyKAKLFGQARRSAIDE-----ARQLITEVGLSGAetkypaQLSGGMQQRLA 150
Cdd:PRK11174 429 GQN----PQLphgTLRDNVLLGNPDAS---DEQLQQALENAWVSEflpllPQGLDTPIGDQAA------GLSVGQAQRLA 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 151 LAQALIMKPKVLLLDEPFGALDpgIRAEiHTLMKRLWNETQ-MTVVMVTH 199
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLD--AHSE-QLVMQALNAASRrQTTLMVTH 542
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-212 |
4.18e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKS----TFLRMLlgqerPT------RGTILLDGEP-LPAEPGPDRGVVFQRYS-VF 85
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESlLHASEQTLRGVRGNKIAmIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PHLTVLGNVLLGKELMASKYKAKLFGQARRSAIDEARQLITEVGLSGAETK---YPAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:PRK15134 99 QEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 163 LLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVA 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-212 |
7.23e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKS-TFL----------------RMLLgqERPTRGTILLdGEPLPAE----PGPDRGV 77
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALalmrlleqagglvqcdKMLL--RRRSRQVIEL-SEQSAAQmrhvRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQRysvfpHLTVLGNVLLGKELMASKYKAKLfGQARRSAIDEARQLITEVGLSGAET---KYPAQLSGGMQQRLALAQA 154
Cdd:PRK10261 109 IFQE-----PMTSLNPVFTVGEQIAESIRLHQ-GASREEAMVEAKRMLDQVRIPEAQTilsRYPHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 155 LIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVL 240
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-212 |
8.32e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 83.63 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEP----GPDRGVVFQRY--SVFPhLTVLG 92
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwvRSKVGLVFQDPddQVFS-STVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PRK13647 100 DVAFGPVNM---------GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517136998 173 PGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVV 212
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVI 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-198 |
1.66e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.53 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpaEPGpDRGVVFQRYSVF---PHLTVLGNVL 95
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL--HFG-DYSYRSQRIRMIfqdPSTSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 96 LGKEL-MASKYKAKLFGQARRSAIDEArqlITEVGL-SGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK15112 106 ISQILdFPLRLNTDLEPEQREKQIIET---LRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180
....*....|....*....|....*
gi 517136998 174 GIRAEIHTLMKRLWNETQMTVVMVT 198
Cdd:PRK15112 183 SMRSQLINLMLELQEKQGISYIYVT 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-212 |
2.58e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.83 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEplpaEPGPDR-------GVVF-QRYSVFPHLTV 90
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY----VPFKRRkefarriGVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVLLGKELmaskYK--AKLFgqarRSAIDEarqLITEVGLSGAETKyPA-QLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:COG4586 114 IDSFRLLKAI----YRipDAEY----KKRLDE---LVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 168 FGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-240 |
3.25e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTIL---LDGEPLPAEPGPDR--GVVFQR-YSVFPHLTVLG 92
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKlvGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLGKELMAskykakLFGQARRSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PRK13644 98 DLAFGPENLC------LPPIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 173 PGIRAEIHTLMKRLwNETQMTVVMVTHDMREaFTLATRVVAFERPRDRPE-EKERYGATIT-RDISIWPP 240
Cdd:PRK13644 169 PDSGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEgEPENVLSDVSlQTLGLTPP 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-212 |
3.78e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.98 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 3 ELIIDSVWKEYGDQI-----VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPA-------- 69
Cdd:PRK13645 6 DIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikev 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 70 -EPGPDRGVVFQ--RYSVFPHlTVLGNVLLGKELMaskykaklfGQARRSAIDEARQLITEVGLSGAETKY-PAQLSGGM 145
Cdd:PRK13645 86 kRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNL---------GENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517136998 146 QQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
36-204 |
4.19e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.02 E-value: 4.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 36 GPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVFQRYSVFPHLTVLGNVLLgkelmaskyKAKLFGQ 112
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRrrvGYMSQAFSLYGELTVRQNLEL---------HARLFHL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 113 ARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQM 192
Cdd:NF033858 370 PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGV 449
|
170
....*....|..
gi 517136998 193 TVVMVTHDMREA 204
Cdd:NF033858 450 TIFISTHFMNEA 461
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-214 |
6.95e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVF-----QRYSVFPHLT 89
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYipedrLGRGLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGKelmaskYKAKLFGQA---RRSAIDE-ARQLITEVGLSGAETKYPA-QLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:COG3845 353 VAENLILGR------YRRPPFSRGgflDRKAIRAfAEELIEEFDVRTPGPDTPArSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 165 DEPFGALDPGIRAEIHTLMKRLWNEtQMTVVMVTHDMREAFTLATRVVAF 214
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVM 475
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-201 |
8.58e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELI-IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILldgeplpAEPGPDRGVVF 79
Cdd:PRK09544 1 MTSLVsLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRYSVFPHLTvlgnvLLGKELMaskykaKLFGQARRSAIDEARQLITEVGLsgaeTKYPAQ-LSGGMQQRLALAQALIMK 158
Cdd:PRK09544 74 QKLYLDTTLP-----LTVNRFL------RLRPGTKKEDILPALKRVQAGHL----IDAPMQkLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-201 |
9.34e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 81.33 E-value: 9.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIV----LENVSLTVASRAFVALVGPSGCGKSTFLRMLLG----QERPTRGTILLDGEPLPAEP- 71
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQDLQRISe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 72 -------GPDRGVVFQ--RYSVFPHLTVlgnvllGKELM-ASKYKAklfGQARRSAIDEARQLITEVGLSGAETK---YP 138
Cdd:PRK11022 81 kerrnlvGAEVAMIFQdpMTSLNPCYTV------GFQIMeAIKVHQ---GGNKKTRRQRAIDLLNQVGIPDPASRldvYP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 139 AQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-199 |
1.17e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 82.48 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 2 SELIIDSVWKEYG-DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPaepGPDRGVVFQ 80
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK---DIDRHTLRQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHL------TVLGNVLLGKELMASKYKAKlfgqaRRSAIDEARQLITEVGLsGAETKYPAQ---LSGGMQQRLAL 151
Cdd:TIGR01193 549 FINYLPQEpyifsgSILENLLLGAKENVSQDEIW-----AACEIAEIKDDIENMPL-GYQTELSEEgssISGGQKQRIAL 622
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 152 AQALIMKPKVLLLDEPFGALDpgIRAEiHTLMKRLWNETQMTVVMVTH 199
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLD--TITE-KKIVNNLLNLQDKTIIFVAH 667
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
34-201 |
1.47e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.92 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 34 LVGPSGCGKS--TFLRM-LLGQERPTRGTILLDGEP---LP--------AEpgpDRGVVFQ--RYSVFPHLTVlgnvllG 97
Cdd:PRK09473 47 IVGESGSGKSqtAFALMgLLAANGRIGGSATFNGREilnLPekelnklrAE---QISMIFQdpMTSLNPYMRV------G 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 98 KELMASKYKAKlfGQARRSAIDEARQLITEVGLSGAETK---YPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPG 174
Cdd:PRK09473 118 EQLMEVLMLHK--GMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT 195
|
170 180
....*....|....*....|....*..
gi 517136998 175 IRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:PRK09473 196 VQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-172 |
2.23e-17 |
|
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: 78.81 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQI--VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD-R---GVVF 79
Cdd:cd03251 3 FKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlRrqiGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 80 QRYSVFpHLTVLGNVLLGKElmaskykaklfGQARRSAIDEAR-----QLI--------TEVGLSGaetkypAQLSGGMQ 146
Cdd:cd03251 83 QDVFLF-NDTVAENIAYGRP-----------GATREEVEEAARaanahEFImelpegydTVIGERG------VKLSGGQR 144
|
170 180
....*....|....*....|....*.
gi 517136998 147 QRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALD 170
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-201 |
2.65e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgpdRGVVFQRYSVFPHLTVLGNVLLGk 98
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR---KGLMKLRESVGMVFQDPDNQLFS- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 99 elmASKYKAKLFG----QARRSAIDE-ARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK13636 98 ---ASVYQDVSFGavnlKLPEDEVRKrVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180
....*....|....*....|....*...
gi 517136998 174 GIRAEIHTLMKRLWNETQMTVVMVTHDM 201
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDI 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-204 |
3.33e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 13 YGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTI-LLDGeplpaepgpDRGVVFQRYSVFPHLTVL 91
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGG---------DMADARHRRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 --GnvlLGKELMA--SKYK-----AKLFGQA---RRSAIDEarqLITEVGLSGAETKyPA-QLSGGMQQRLALAQALIMK 158
Cdd:NF033858 82 pqG---LGKNLYPtlSVFEnldffGRLFGQDaaeRRRRIDE---LLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517136998 159 PKVLLLDEPFGALDPGIRAEIHTLMKRLWNET-QMTVVMVTHDMREA 204
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEA 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-211 |
5.09e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 6 IDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGE-------PLPAEPGPdrGVV 78
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhKLAAQLGI--GII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 FQRYSVFPHLTVLGNVLLGKELMaskykAKLFGQarrSAID------EARQLITEVGLSGAETKYPAQLSGGMQQRLALA 152
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLT-----KKVCGV---NIIDwremrvRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 153 QALIMKPKVLLLDEPFGALdpgIRAEIHTL---MKRLWNETQmTVVMVTHDMREAFTLATRV 211
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSL---TNKEVDYLfliMNQLRKEGT-AIVYISHKLAEIRRICDRY 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-202 |
6.08e-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: 77.37 E-value: 6.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEpLPAEPGPDRGVVFQRYSVF-----PHL---TV 90
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNK-NESEPSFEATRSRNRYSVAyaaqkPWLlnaTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVLLGKELMASKYKAKLFGQARRSAID---EARQliTEVGLSGAetkypaQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDllpFGDQ--TEIGERGI------NLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 517136998 168 FGALDpgIRAEIHTLMK---RLWNETQMTVVMVTHDMR 202
Cdd:cd03290 168 FSALD--IHLSDHLMQEgilKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-215 |
1.60e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.82 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLdGEPLpaepgpDRGVVFQ-RYSVFPHLT 89
Cdd:TIGR03719 330 KAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------KLAYVDQsRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 V-------LGNVLLGKELMASkykaklfgqarrsaideaRQLITEVGLSGAET-KYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:TIGR03719 403 VweeisggLDIIKLGKREIPS------------------RAYVGRFNFKGSDQqKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 162 LLLDEPFGALDpgiraeIHTLmkRLWNETQM----TVVMVTHDMREAFTLATRVVAFE 215
Cdd:TIGR03719 465 LLLDEPTNDLD------VETL--RALEEALLnfagCAVVISHDRWFLDRIATHILAFE 514
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-211 |
1.63e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGP-------DRGVVFQR--YSVFPHLT 89
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqalrrDIQFIFQDpyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VlgnvllGKELMAS-KYKAKLFGQARRSAIDEarqLITEVGLSGAET-KYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:PRK10261 420 V------GDSIMEPlRVHGLLPGKAAAARVAW---LLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517136998 168 FGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRV 211
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-226 |
4.48e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQE--RPTRGTILLDGEPLPAEpgpdrgvvfqrysvfphLTVLGNVl 95
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGRE-----------------ASLIDAI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 96 lgkelmaskykaklfgqARRSAIDEARQLITEVGLSGAET--KYPAQLSGGMQQRLALAQALIMKPKVLLLDEpFGA-LD 172
Cdd:COG2401 107 -----------------GRKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCShLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 173 PGIRAEIHTLMKRLWNETQMTVVMVTH--DMREAftLATRVVAFERPRDRPEEKER 226
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVVATHhyDVIDD--LQPDLLIFVGYGGVPEEKRR 222
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-199 |
1.08e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 74.33 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQE--RPTRGTILLDGEPLPAEPGPDR-----GVVFQRYSVFP 86
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERaragiFLAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTVL------GNVLLGKELMASKYKAKLFGQARRSAIDEA---RQLitEVGLSGAETKypaqlsggmqqRLALAQALIM 157
Cdd:COG0396 91 GVSVSnflrtaLNARRGEELSAREFLKLLKEKMKELGLDEDfldRYV--NEGFSGGEKK-----------RNEILQMLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 158 KPKVLLLDEPFGALD-PGIRAEIHTLMKRLwnETQMTVVMVTH 199
Cdd:COG0396 158 EPKLAILDETDSGLDiDALRIVAEGVNKLR--SPDRGILIITH 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-199 |
1.24e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 10 WKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERP---TRGTILLDGEPLPAEPGPDR-GVVFQRYSVF 85
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIsAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PHLTVLGNVLLGKELmasKYKAKLFGQARRSAIDEarqLITEVGL-SGAETK--YPAQ---LSGGMQQRLALAQALIMKP 159
Cdd:TIGR00955 112 PTLTVREHLMFQAHL---RMPRRVTKKEKRERVDE---VLQALGLrKCANTRigVPGRvkgLSGGERKRLAFASELLTDP 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWNEtQMTVVMVTH 199
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-199 |
1.76e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 72.94 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQE--RPTRGTILLDGEPLPAEPGPDR-----G 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlgiF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 77 VVFQRYSVFPHLTVlgnvllgkelmaskykaklfgqarrsaIDEARQLitEVGLSGAETKypaqlsggmqqRLALAQALI 156
Cdd:cd03217 81 LAFQYPPEIPGVKN---------------------------ADFLRYV--NEGFSGGEKK-----------RNEILQLLL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517136998 157 MKPKVLLLDEPFGALD-PGIRAeIHTLMKRLWNETqMTVVMVTH 199
Cdd:cd03217 121 LEPDLAILDEPDSGLDiDALRL-VAEVINKLREEG-KSVLIITH 162
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-183 |
2.57e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQeRPT---RGTILLDGEPLPAEPGPD---RGVV--FQRY 82
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDterAGIAiiHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 83 SVFPHLTVLGNVLLGKELMASKYkaklfgqarrsaID------EARQLITEVGLS-GAETKYpAQLSGGMQQRLALAQAL 155
Cdd:PRK13549 92 ALVKELSVLENIFLGNEITPGGI------------MDydamylRAQKLLAQLKLDiNPATPV-GNLGLGQQQLVEIAKAL 158
|
170 180
....*....|....*....|....*...
gi 517136998 156 IMKPKVLLLDEPFGALdpgIRAEIHTLM 183
Cdd:PRK13549 159 NKQARLLILDEPTASL---TESETAVLL 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-183 |
3.20e-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: 75.25 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLG--QERPTRGTILLDGEPLPAEPGPD---RGVV 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASNIRDterAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 79 F--QRYSVFPHLTVLGNVLLGKELMASKYKAKLFGQARRsaideARQLITEVGLSGAETKYP-AQLSGGMQQRLALAQAL 155
Cdd:TIGR02633 82 IihQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLR-----AKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180
....*....|....*....|....*...
gi 517136998 156 IMKPKVLLLDEPFGALdpgIRAEIHTLM 183
Cdd:TIGR02633 157 NKQARLLILDEPSSSL---TEKETEILL 181
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-200 |
4.59e-15 |
|
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: 74.59 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPtrgtilLDGEPLPAePGPDRGVVFQRYSVFPHLTVLGN 93
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARPQ-PGIKVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLG----KELMA-------------SKYKAKLFGQARRSAIDEAR---QLITEVGLSGAETKYP------AQLSGGMQQ 147
Cdd:TIGR03719 89 VEEGvaeiKDALDrfneisakyaepdADFDKLAAEQAELQEIIDAAdawDLDSQLEIAMDALRCPpwdadvTKLSGGERR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517136998 148 RLALAQALIMKPKVLLLDEPFGALDpgirAEIHTLMKRLWNETQMTVVMVTHD 200
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-215 |
6.11e-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: 72.44 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 32 VALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgpdrgvvfQRYSVFPHLTVlgnvllgKELMASKYKAKLfg 111
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP--------QYIKADYEGTV-------RDLLSSITKDFY-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 112 qarrsaidEARQLITEV----GLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLW 187
Cdd:cd03237 91 --------THPYFKTEIakplQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*...
gi 517136998 188 NETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-214 |
7.17e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 21 NVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL-PAEP--GPDRGVVFQRYS-----VFPHLTVLG 92
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsPRSPldAVKKGMAYITESrrdngFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLGKELMASKYKAK--LFGQARRSAIDEARQLITEVGLSGAETKYpAQLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:PRK09700 361 NMAISRSLKDGGYKGAmgLFHEVDEQRTAENQRELLALKCHSVNQNI-TELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517136998 171 LDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVVAF 214
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVF 482
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-172 |
8.86e-15 |
|
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: 73.98 E-value: 8.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpaepgpdrgvvfQRY---SVFPHLTVLG-N 93
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL------------ADYtlaSLRRQVALVSqD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKELMASKYKAKLFGQARRSAIDEARQ--------------LITEVGLSGAetkypaQLSGGMQQRLALAQALIMKP 159
Cdd:TIGR02203 415 VVLFNDTIANNIAYGRTEQADRAEIERALAaayaqdfvdklplgLDTPIGENGV------LLSGGQRQRLAIARALLKDA 488
|
170
....*....|...
gi 517136998 160 KVLLLDEPFGALD 172
Cdd:TIGR02203 489 PILILDEATSALD 501
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-212 |
1.13e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 20 ENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD---RGVVF-----QRYSVFPHLTVL 91
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDairAGIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 GNVLLGKELMASKykAKLFGQARRSAiDEARQLITE--VGLSGAETKYpAQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK11288 350 DNINISARRHHLR--AGCLINNRWEA-ENADRFIRSlnIKTPSREQLI-MNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 170 ALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK11288 426 GIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-214 |
1.47e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL---PAEPGPDRGV--VFQRYSVFPHLTVLGN 93
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAGVaiIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKelMASKykaklFGQARRSA-IDEARQLITEVGLS---GAETKYpaqLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK11288 100 LYLGQ--LPHK-----GGIVNRRLlNYEAREQLEHLGVDidpDTPLKY---LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 170 ALDpgIRaEIHTLMK---RLWNETQMtVVMVTHDMREAFTLATRVVAF 214
Cdd:PRK11288 170 SLS--AR-EIEQLFRvirELRAEGRV-ILYVSHRMEEIFALCDAITVF 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-211 |
2.25e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 8 SVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL-PAEPGPDRG----VVFQRY 82
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKAHQlgiyLVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 83 SVFPHLTVLGNVllgkelmaskykakLFGQARRSAiDEAR--QLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPK 160
Cdd:PRK15439 96 LLFPNLSVKENI--------------LFGLPKRQA-SMQKmkQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 161 VLLLDEPFGALDPgirAEIHTLMKRLwNETQMT---VVMVTHDMREAFTLATRV 211
Cdd:PRK15439 161 ILILDEPTASLTP---AETERLFSRI-RELLAQgvgIVFISHKLPEIRQLADRI 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-172 |
3.55e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.92 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpaepgpdR-----------GVVFQRYSVFPH 87
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI-------RtvtraslrrniAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 lTVLGNVLLGKElmaSKYKAKLFGQARRSAIDE--ARQ---LITEVGLSGAetkypaQLSGGMQQRLALAQALIMKPKVL 162
Cdd:PRK13657 424 -SIEDNIRVGRP---DATDEEMRAAAERAQAHDfiERKpdgYDTVVGERGR------QLSGGERQRLAIARALLKDPPIL 493
|
170
....*....|
gi 517136998 163 LLDEPFGALD 172
Cdd:PRK13657 494 ILDEATSALD 503
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-199 |
3.91e-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: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRML-----LGQ---ERPTRGTILLdgepLPaepgpdrgvvfQRysvfP 86
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpWGSgriGMPEGEDLLF----LP-----------QR----P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTvLGNVllgkelmaskykaklfgqarrsaideARQLItevglsgaetkYP--AQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:cd03223 74 YLP-LGTL--------------------------REQLI-----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 517136998 165 DEPFGALDPGIRAEIHTLMKRLwnetQMTVVMVTH 199
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-212 |
4.30e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL----PAEpGPDRGVVFQRYSVFPHLTVLGnv 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrsPQD-GLANGIVYISEDRKRDGLVLG-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 95 LLGKELMA-------SKYKAKLFGQARRSAIDEARQLITevglsgaeTKYPAQ------LSGGMQQRLALAQALIMKPKV 161
Cdd:PRK10762 345 MSVKENMSltalryfSRAGGSLKHADEQQAVSDFIRLFN--------IKTPSMeqaiglLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLWNETqMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-219 |
4.68e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpAEPGPDR------GVVFQRYSVFPHLTVLG 92
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPKSsqeagiGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLGKELMASkykaklFGqarrsAID------EARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PRK10762 99 NIFLGREFVNR------FG-----RIDwkkmyaEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 167 PFGALdpgIRAEIHTLMK--RLWNETQMTVVMVTHDMREAFTLATRVVAFerpRD 219
Cdd:PRK10762 168 PTDAL---TDTETESLFRviRELKSQGRGIVYISHRLKEIFEICDDVTVF---RD 216
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-199 |
4.79e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD-RG---VVFQRYSVFPHlTV 90
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSrlaVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 LGNVLLGKElmaskykaklfgQARRSAIDEARQLI--------------TEVGLSGaetkypAQLSGGMQQRLALAQALI 156
Cdd:PRK10789 406 ANNIALGRP------------DATQQEIEHVARLAsvhddilrlpqgydTEVGERG------VMLSGGQKQRISIARALL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517136998 157 MKPKVLLLDEPFGALDPGIRAEI-HTLmkRLWNEtQMTVVMVTH 199
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQIlHNL--RQWGE-GRTVIISAH 508
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-179 |
5.00e-14 |
|
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: 71.77 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpaepgpdR-----------GVVfqrysvfP 86
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-------RdvtqaslraaiGIV-------P 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 87 HLTVL------GNVLLGKeLMASkyKAKLFGQARRSAIDEarqLI--------TEVGLSGaetkypAQLSGGMQQRLALA 152
Cdd:COG5265 439 QDTVLfndtiaYNIAYGR-PDAS--EEEVEAAARAAQIHD---FIeslpdgydTRVGERG------LKLSGGEKQRVAIA 506
|
170 180
....*....|....*....|....*..
gi 517136998 153 QALIMKPKVLLLDEPFGALDPGIRAEI 179
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAI 533
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
7.68e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILL---------DGEPLPAEPGPDR-----------GV 77
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSKKiknfkelrrrvSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VFQ--RYSVFPHlTVLGNVLLGK-ELMASKYKAKlfgqarrsaiDEARQLITEVGL-SGAETKYPAQLSGGMQQRLALAQ 153
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPvALGVKKSEAK----------KLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVVAFER 216
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDK 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-212 |
7.77e-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: 71.01 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQ-ERPTRGTILLDGEPL----PAEpGPDRGVVF-----QRYSVFPHL 88
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirnPAQ-AIRAGIAMvpedrKRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TVLGNVLLGKeLMASKYKAKLFGQARRSAIDEArqlITEVGLSGAETKYP-AQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:TIGR02633 355 GVGKNITLSV-LKSFCFKMRIDAAAELQIIGSA---IQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517136998 168 FGALDPGIRAEIHTLMKRLWNETqMTVVMVTHDMREAFTLATRVV 212
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVL 474
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-200 |
1.41e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 12 EYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLdGEPLP--------AEPGPDRgvvfqrys 83
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfdqhrAELDPEK-------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 vfphlTVLGNVLLGK-ELMASKYKAK--------LFGQARrsaidearqlitevglsgAETKYPAqLSGGMQQRLALAQa 154
Cdd:PRK11147 399 -----TVMDNLAEGKqEVMVNGRPRHvlgylqdfLFHPKR------------------AMTPVKA-LSGGERNRLLLAR- 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517136998 155 LIMKPKVLL-LDEPFGALDpgiraeIHT--LMKRLWNETQMTVVMVTHD 200
Cdd:PRK11147 454 LFLKPSNLLiLDEPTNDLD------VETleLLEELLDSYQGTVLLVSHD 496
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-200 |
1.69e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.33 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGqERPTRGTILLDGEPLPAEPGPD----RGVVFQRYS------VFPHL 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAElarhRAYLSQQQSppfampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TvlgnvllgkelmaskykaklFGQARRSAIDEARQLITEV-GLSGAETKYP---AQLSGGMQQRLALAQALIM------- 157
Cdd:COG4138 91 A--------------------LHQPAGASSEAVEQLLAQLaEALGLEDKLSrplTQLSGGEWQRVRLAAVLLQvwptinp 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 158 KPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHD 200
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHD 192
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-216 |
2.72e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQerptrgtILLDGEPLPAEpgpdRGVVFQ 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGE-------VLLDDGRIIYE----QDLIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVL---------LGKEL---------MASKYKAKLFGQ-ARRSAIDEARQL------ITEV----GLS 131
Cdd:PRK11147 70 RLQQDPPRNVEGTVYdfvaegieeQAEYLkryhdishlVETDPSEKNLNElAKLQEQLDHHNLwqlenrINEVlaqlGLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 132 gAETKYpAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgiraeIHTLmkrLWNET-----QMTVVMVTHDmrEAF- 205
Cdd:PRK11147 150 -PDAAL-SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD------IETI---EWLEGflktfQGSIIFISHD--RSFi 216
|
250
....*....|..
gi 517136998 206 -TLATRVVAFER 216
Cdd:PRK11147 217 rNMATRIVDLDR 228
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-201 |
3.40e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.39 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERP----TRGTILLDGEPLPAEPGPDR--------GVVFQ--RYS 83
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERrkiigreiAMIFQepSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVlgnvllGKELM----ASKYKAKL---FGQARRSAIdearQLITEVGLSGAE---TKYPAQLSGGMQQRLALAQ 153
Cdd:COG4170 102 LDPSAKI------GDQLIeaipSWTFKGKWwqrFKWRKKRAI----ELLHRVGIKDHKdimNSYPHELTEGECQKVMIAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517136998 154 ALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQ-MTVVMVTHDM 201
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARL-NQLQgTSILLISHDL 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-211 |
3.62e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.05 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQeRPT---RGTILLDGEPL------PAEpgpDRGVVF--QRYSVFPH 87
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCrfkdirDSE---ALGIVIihQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGKElmaskykaklfgQARRSAID------EARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:NF040905 93 LSIAENIFLGNE------------RAKRGVIDwnetnrRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 162 LLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRV 211
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSI 209
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-228 |
3.74e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.54 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 17 IVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQ----ERP----TRGTILLDGEPLPAEPGPD----RGVVFQRYS- 83
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltggGAPrgarVTGDVTLNGEPLAAIDAPRlarlRAVLPQAAQp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPhLTVLGNVLLGKELMASKYKAklFGQARRSAIDEARQLITEVGLSGAETkypAQLSGGMQQRLALAQAL-------- 155
Cdd:PRK13547 95 AFA-FSAREIVLLGRYPHARRAGA--LTHRDGEIAWQALALAGATALVGRDV---TTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 156 -IMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHD----MREAFTLAT----RVVAFERPRD--RPEEK 224
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDpnlaARHADRIAMladgAIVAHGAPADvlTPAHI 248
|
....*
gi 517136998 225 ER-YG 228
Cdd:PRK13547 249 ARcYG 253
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-201 |
5.83e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.82 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPlpaepgpdrGVVFQRySVFPHLTVLGN 93
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV---------AYVPQQ-AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKELMASKYKAKLfgqarrsaidEARQLI-----------TEVGLSGaetkypAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:TIGR00957 719 ILFGKALNEKYYQQVL----------EACALLpdleilpsgdrTEIGEKG------VNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517136998 163 LLDEPFGALDPGIRAEI--HTL--MKRLWNETQmtvVMVTHDM 201
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIfeHVIgpEGVLKNKTR---ILVTHGI 822
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
58-211 |
7.99e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 58 GTILLDGEPL----PAEpGPDRGVVF-----QRYSVFPHLTVLGNVLLgkelmaskykAKLFGQARRSAIDEARQLIT-- 126
Cdd:PRK13549 318 GEIFIDGKPVkirnPQQ-AIAQGIAMvpedrKRDGIVPVMGVGKNITL----------AALDRFTGGSRIDDAAELKTil 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 127 -EVGLSGAETKYP----AQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNEtQMTVVMVTHDM 201
Cdd:PRK13549 387 eSIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSEL 465
|
170
....*....|
gi 517136998 202 REAFTLATRV 211
Cdd:PRK13549 466 PEVLGLSDRV 475
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-172 |
1.01e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLG--QERPTRGTILLDGEPLPAEPGPDRGVVFQRYSVFPHLTVLG 92
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVLLGKELMASKYKAKlfgQARRSAideARQLITEVGLSGAET-----KYPAQLSGGMQQRLALAQALIMKPKVLLLDEP 167
Cdd:PLN03211 160 TLVFCSLLRLPKSLTK---QEKILV---AESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
....*
gi 517136998 168 FGALD 172
Cdd:PLN03211 234 TSGLD 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
11-218 |
1.28e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.07 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCG--KSTFLRMLLGQE---RPTR-GTILLDGEPLPAEPGPDRGVVFQRYSV 84
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRf*TWCANRRALRRTIG*HRPVR*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 85 FPHLTVLgnVLLGKELMASkykaklfgqaRRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLL 164
Cdd:NF000106 101 FSGRENL--YMIGR*LDLS----------RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 165 DEPFGALDPGIRAEIhtlmkrlWNETQ------MTVVMVTHDMREAFTLATRVVAFERPR 218
Cdd:NF000106 169 DEPTTGLDPRTRNEV-------WDEVRsmvrdgATVLLTTQYMEEAEQLAHELTVIDRGR 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-201 |
1.85e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL-PAEPGPDRGVVFQRYSV---FPhltvlgnV 94
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrQALQKNLVAYVPQSEEVdwsFP-------V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 95 LLGKELMASKYKAklFGQARRsAIDEARQLITE----VGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGA 170
Cdd:PRK15056 96 LVEDVVMMGRYGH--MGWLRR-AKKRDRQIVTAalarVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190
....*....|....*....|....*....|.
gi 517136998 171 LDPGIRAEIHTLMKRLWNETQmTVVMVTHDM 201
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGK-TMLVSTHNL 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-211 |
2.82e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.96 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 33 ALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPdrgvVFQRYSVFPHLTVLGNVLLGKELMAskYKAKLFGQ 112
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD----VHQNMGYCPQFDAIDDLLTGREHLY--LYARLRGV 2042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 113 ARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRaeihtlmKRLWN---- 188
Cdd:TIGR01257 2043 PAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR-------RMLWNtivs 2115
|
170 180
....*....|....*....|....*
gi 517136998 189 --ETQMTVVMVTHDMREAFTLATRV 211
Cdd:TIGR01257 2116 iiREGRAVVLTSHSMEECEALCTRL 2140
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-200 |
3.16e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 12 EYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDgeplpaePGPDRGVVFQRYSVFPHLTVL 91
Cdd:PRK15064 10 QFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-------PNERLGKLRQDQFAFEEFTVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 GNVLLGKELMaskYKAKlfgqARRSAI---------D-------------------EAR--QLITEVGLsGAEtkypaQL 141
Cdd:PRK15064 83 DTVIMGHTEL---WEVK----QERDRIyalpemseeDgmkvadlevkfaemdgytaEARagELLLGVGI-PEE-----QH 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517136998 142 SGGMQQ-------RLALAQALIMKPKVLLLDEPFGALDpgiraeIHTL--MKRLWNETQMTVVMVTHD 200
Cdd:PRK15064 150 YGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNLD------INTIrwLEDVLNERNSTMIIISHD 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-172 |
4.95e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLdGEPLpaepgpDRGVVFQ-RYSVFPHLT 89
Cdd:PRK11819 332 KSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------KLAYVDQsRDALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 V-------LGNVLLGKELMASkykaklfgqarrsaideaRQLITEVGLSGAE-TKYPAQLSGGMQQRLALAQALIMKPKV 161
Cdd:PRK11819 405 VweeisggLDIIKVGNREIPS------------------RAYVGRFNFKGGDqQKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|.
gi 517136998 162 LLLDEPFGALD 172
Cdd:PRK11819 467 LLLDEPTNDLD 477
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-200 |
1.20e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 22 VSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEpGPDR-----GVVFQRYSVFPHltvlgnvLL 96
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE-QPEDyrklfSAVFTDFHLFDQ-------LL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 97 GKElmaskykaklfGQARRSAIDEA----RQLITEVGLSGAETKYPaQLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PRK10522 414 GPE-----------GKPANPALVEKwlerLKMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180
....*....|....*....|....*...
gi 517136998 173 PGIRAEIHTLMKRLWNETQMTVVMVTHD 200
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-199 |
1.21e-11 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 62.51 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 3 ELIIDSVWKEYGD--QIVLENVSLTVASRAFVALVGPSGCGKST----FLRMLlgqeRPTRGTILLDGEPL--------- 67
Cdd:cd03244 2 DIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDIskiglhdlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 68 ------PAEPgpdrgVVFQ---RYSVFPHltvlgNVLLGKELMASKYKAKLfgqarRSAIDE-ARQLITEVGLSGaetky 137
Cdd:cd03244 78 srisiiPQDP-----VLFSgtiRSNLDPF-----GEYSDEELWQALERVGL-----KEFVESlPGGLDTVVEEGG----- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517136998 138 pAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIH-TLMKRLwneTQMTVVMVTH 199
Cdd:cd03244 138 -ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQkTIREAF---KDCTVLTIAH 196
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
34-215 |
1.27e-11 |
|
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: 64.43 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 34 LVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEpgpDRG-------VVFQRYSVFPHltvlgnvllgkelmaskyk 106
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD---NREayrqlfsAVFSDFHLFDR------------------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 107 akLFGQARRSAIDEARQLITEVGLSGAeTKYPA------QLSGGMQQRLALAQALIMKPKVLLLDEpFGA-LDPGIRA-- 177
Cdd:COG4615 421 --LLGLDGEADPARARELLERLELDHK-VSVEDgrfsttDLSQGQRKRLALLVALLEDRPILVFDE-WAAdQDPEFRRvf 496
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517136998 178 --EIHTLMKRLwnetQMTVVMVTHDMReAFTLATRVVAFE 215
Cdd:COG4615 497 ytELLPELKAR----GKTVIAISHDDR-YFDLADRVLKMD 531
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-199 |
1.58e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.27 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLlgqerpTR------GTILLDGEPLpaepgpdrgvvfQRY---SVF 85
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLL------TRfydideGEILLDGHDL------------RDYtlaSLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PHLTVLG-NVLLGKELMASK--YKAKlfGQARRSAIDEARQ--------------LITEVGLSGAetkypaQLSGGMQQR 148
Cdd:PRK11176 417 NQVALVSqNVHLFNDTIANNiaYART--EQYSREQIEEAARmayamdfinkmdngLDTVIGENGV------LLSGGQRQR 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 149 LALAQALIMKPKVLLLDEPFGALDP----GIRAEIHTLMKrlwnetQMTVVMVTH 199
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTeserAIQAALDELQK------NRTSLVIAH 537
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-215 |
2.26e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 36 GPSGCGKSTFLRMLLGQERPTRGTILLDGEPLpaepgpDRGVVFQRYSVFPHLTVLGNVLLGKELMasKYKAKLFGQARR 115
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA------TRGDRSRFMAYLGHLPGLKADLSTLENL--HFLCGLHGRRAK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 116 SAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP-GIRAEIHTLMKRLwnETQMTV 194
Cdd:PRK13543 116 QMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLeGITLVNRMISAHL--RGGGAA 190
|
170 180
....*....|....*....|.
gi 517136998 195 VMVTHDMREAFTLATRVVAFE 215
Cdd:PRK13543 191 LVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
3.46e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLdgeplpAEpGPDRGVVFQ-RY 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SE-NANIGYYAQdHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 83 SVFPH-LTVLgnvllgkELMASKYKAKLFGQARRSAIdeARQLitevgLSGAETKYPAQ-LSGGMQQRLALAQALIMKPK 160
Cdd:PRK15064 393 YDFENdLTLF-------DWMSQWRQEGDDEQAVRGTL--GRLL-----FSQDDIKKSVKvLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 161 VLLLDEPFGALDpgiRAEIHTLMKRLWNeTQMTVVMVTHDmREaF--TLATRVV 212
Cdd:PRK15064 459 VLVMDEPTNHMD---MESIESLNMALEK-YEGTLIFVSHD-RE-FvsSLATRII 506
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
18-211 |
4.56e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.13 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLG----QERPTRGTILLDG-EPLPAEPGPDRGVVFQRYSVF---PHLT 89
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDiDLLRLSPRERRKLVGHNVSMIfqePQSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 VLGNVLLGKELMAS----KYKAKL---FGQARRSAIdearQLITEVGLS---GAETKYPAQLSGGMQQRLALAQALIMKP 159
Cdd:PRK15093 102 LDPSERVGRQLMQNipgwTYKGRWwqrFGWRKRRAI----ELLHRVGIKdhkDAMRSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 160 KVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRV 211
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-202 |
5.67e-11 |
|
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: 60.50 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDrgvVFQRYSVFPHLTVL--GNVL 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSSLTIIPQDPTLfsGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 96 LGKELMASKYKAKLFGQARrsaidearqlITEVGLSgaetkypaqLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGI 175
Cdd:cd03369 100 SNLDPFDEYSDEEIYGALR----------VSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180
....*....|....*....|....*..
gi 517136998 176 RAEIHTLMKRLWNETqmTVVMVTHDMR 202
Cdd:cd03369 161 DALIQKTIREEFTNS--TILTIAHRLR 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-207 |
6.36e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 9 VWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPL---PAEPGPDRGV--VFQRYS 83
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGIsmVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 84 VFPHLTVLGNVLLGkelmasKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK10982 84 LVLQRSVMDNMWLG------RYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 517136998 164 LDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTL 207
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQL 200
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-200 |
7.00e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.18 E-value: 7.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPlpaepgpdRGVVFQRYSVfPHLTVLGN 93
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV--------RMAVFSQHHV-DGLDLSSN 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLgkelmaskYKAKLFGQARRSAIdeaRQLITEVGLSGAETKYPA-QLSGGMQQRLALAQALIMKPKVLLLDEPFGALD 172
Cdd:PLN03073 591 PLL--------YMMRCFPGVPEQKL---RAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180
....*....|....*....|....*....
gi 517136998 173 -PGIRAEIHTLMKrlwneTQMTVVMVTHD 200
Cdd:PLN03073 660 lDAVEALIQGLVL-----FQGGVLMVSHD 683
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-211 |
8.61e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 21 NVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDR---GVVF-----QRYSVFPHLTVLG 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarGLVYlpedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 93 NVllgkelMASKYKAKLFGQ--ARRSAIDEARQLITEVGLSGAETkyPAQ-LSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:PRK15439 361 NV------CALTHNRRGFWIkpARENAVLERYRRALNIKFNHAEQ--AARtLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517136998 170 ALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRV 211
Cdd:PRK15439 433 GVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRV 473
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-216 |
8.90e-11 |
|
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: 58.92 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 31 FVALVGPSGCGKSTFLRMLLGQ-ERPTRGTILLDGEPLpaepgpdrgvvfqrysvfphltvlgnvllgkelmaskykakl 109
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARElGPPGGGVIYIDGEDI------------------------------------------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 110 fgqarrsaideaRQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEI-----HTLMK 184
Cdd:smart00382 42 ------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLL 109
|
170 180 190
....*....|....*....|....*....|..
gi 517136998 185 RLWNETQMTVVMVTHDMREAFTLATRVVAFER 216
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-200 |
9.93e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 9.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPtrgtilLDGEPLPAePGPDRGVVFQRYSVFPHLTVLGN 93
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARPA-PGIKVGYLPQEPQLDPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLG-KELMASKYK----AKLFG------------QARRSAIDEA-------RQLitEV-----GLSGAETKYpAQLSGG 144
Cdd:PRK11819 91 VEEGvAEVKAALDRfneiYAAYAepdadfdalaaeQGELQEIIDAadawdldSQL--EIamdalRCPPWDAKV-TKLSGG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517136998 145 MQQRLALAQALIMKPKVLLLDEPFGALDpgirAE-IHTLMKRLwNETQMTVVMVTHD 200
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFL-HDYPGTVVAVTHD 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-211 |
2.06e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQeRPTRGTILLDGEPLPAEPGPD----RGVVFQRYS------VFPHL 88
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElarhRAYLSQQQTppfampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TvlgnvllgkelmaskykakLFGQARRsAIDEARQLITEV-GLSGAETKYP---AQLSGGMQQRLALAQALI-----MKP 159
Cdd:PRK03695 91 T-------------------LHQPDKT-RTEAVASALNEVaEALGLDDKLGrsvNQLSGGEWQRVRLAAVVLqvwpdINP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 160 --KVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMVTHDMREAFTLATRV 211
Cdd:PRK03695 151 agQLLLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRV 203
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-215 |
2.62e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 57.97 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 11 KEYGDQIVleNVSLTVASRA-FVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPgpdrgvvfqrysvfphlt 89
Cdd:cd03222 8 KRYGVFFL--LVELGVVKEGeVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP------------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 90 vlgnvllgkelmaskykaklfgqarrsaidearQLItevglsgaetkypaQLSGGMQQRLALAQALIMKPKVLLLDEPFG 169
Cdd:cd03222 68 ---------------------------------QYI--------------DLSGGELQRVAIAAALLRNATFYLFDEPSA 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517136998 170 ALDPGIRAEIHTLMKRLWNETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:cd03222 101 YLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-194 |
2.66e-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: 60.69 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGeplpaepgpdrgvvfqRYSVFPHL------TVL 91
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQTswimpgTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 GNVLLGKElmaskykaklFGQARRSAIDEARQLITEVGLSGAETKYP-----AQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:TIGR01271 505 DNIIFGLS----------YDEYRYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190
....*....|....*....|....*....|
gi 517136998 167 PFGALDPGIRAEI--HTLMKRLWNETQMTV 194
Cdd:TIGR01271 575 PFTHLDVVTEKEIfeSCLCKLMSNKTRILV 604
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-172 |
2.69e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 10 WKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGqERPTR--GTILLDGEPlpaepgpdrGVVFQRYSVFpH 87
Cdd:PLN03130 624 WDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-ELPPRsdASVVIRGTV---------AYVPQVSWIF-N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 88 LTVLGNVLLGKELMASKYKAKLfgqaRRSAIDEARQLI-----TEVGLSGaetkypAQLSGGMQQRLALAQALIMKPKVL 162
Cdd:PLN03130 693 ATVRDNILFGSPFDPERYERAI----DVTALQHDLDLLpggdlTEIGERG------VNISGGQKQRVSMARAVYSNSDVY 762
|
170
....*....|
gi 517136998 163 LLDEPFGALD 172
Cdd:PLN03130 763 IFDDPLSALD 772
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-215 |
3.98e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 32 VALVGPSGCGKSTFLRMLLGQERPTRGTILLDgEPLPAEPgpdrgvvfQRYSVFPHLTV---LGNVllGKELMASKYKAK 108
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKP--------QYIKPDYDGTVedlLRSI--TDDLGSSYYKSE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 109 LfgqARRSAIDEarqlITEvglsgaetKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWN 188
Cdd:PRK13409 437 I---IKPLQLER----LLD--------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAE 501
|
170 180
....*....|....*....|....*..
gi 517136998 189 ETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:PRK13409 502 EREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-172 |
4.41e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 12 EYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAepgpDRGV-------VFQRYSV 84
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTyqkqlcfVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 85 FPHLTVLGNVLLgkelmaskykaKLFGQARRSAIDEarqLITEVGLsGAETKYP-AQLSGGMQQRLALAQALIMKPKVLL 163
Cdd:PRK13540 86 NPYLTLRENCLY-----------DIHFSPGAVGITE---LCRLFSL-EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWL 150
|
....*....
gi 517136998 164 LDEPFGALD 172
Cdd:PRK13540 151 LDEPLVALD 159
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-220 |
7.14e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLL----------------------------GQERPT------------- 56
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqGDEEQNvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 57 -------------RGTILLDGEPLPAEPGPDRGVVFQRYSVFP---HLTVLGNVLLGKElMASKYKAKLfgQARRSAIDE 120
Cdd:PTZ00265 1263 eggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPmlfNMSIYENIKFGKE-DATREDVKR--ACKFAAIDE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 121 -----ARQLITEVGlsgaetKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQMTVV 195
Cdd:PTZ00265 1340 fieslPNKYDTNVG------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
|
250 260
....*....|....*....|....*
gi 517136998 196 MVTHDMrEAFTLATRVVAFERPrDR 220
Cdd:PTZ00265 1414 TIAHRI-ASIKRSDKIVVFNNP-DR 1436
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-215 |
8.07e-10 |
|
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: 59.03 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 32 VALVGPSGCGKSTFLRMLLGQERPTRGTILLDgepL-----PAEPGPDRGVVFQrysvfphlTVLGNVLlGKELMASKYK 106
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LkisykPQYISPDYDGTVE--------EFLRSAN-TDDFGSSYYK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 107 AKLfgqARRSAIDEARQlitevglsgaetKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRL 186
Cdd:COG1245 437 TEI---IKPLGLEKLLD------------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180
....*....|....*....|....*....
gi 517136998 187 WNETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:COG1245 502 AENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-201 |
2.91e-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: 57.10 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 32 VALVGPSGCGKSTFLRMLLGQERPTRGTIlldgeplpaEPGPDRGVVFQRYS---VFPHLTVLGNvllgKELMASkYK-- 106
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDY---------DEEPSWDEVLKRFRgteLQDYFKKLAN----GEIKVA-HKpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 107 -----AKLF-GQARR--SAIDE---ARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGI 175
Cdd:COG1245 168 yvdliPKVFkGTVREllEKVDErgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180
....*....|....*....|....*.
gi 517136998 176 RAEIHTLMKRLWNETQmTVVMVTHDM 201
Cdd:COG1245 248 RLNVARLIRELAEEGK-YVLVVEHDL 272
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-173 |
3.23e-09 |
|
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: 56.40 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKST----FLRMLlgqerPTRGTILLDGEPLPAEPGPDR----GVVFQRYSVF 85
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLL-----NTEGDIQIDGVSWNSVPLQKWrkafGVIPQKVFIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 phltvlgnvllgkelmASKYKAKL--FGQARRsaiDEARQLITEVGLSGAETKYPAQL-----------SGGMQQRLALA 152
Cdd:cd03289 90 ----------------SGTFRKNLdpYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLA 150
|
170 180
....*....|....*....|.
gi 517136998 153 QALIMKPKVLLLDEPFGALDP 173
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDP 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-200 |
3.24e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDG--------EPLPAEPGPDRGVVFQRYSVF 85
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPALEYVIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 86 PHLTvlgnvllgKELMASKYK------AKLFGQArrSAID------EARQLITEVGLSGAETKYPAQ-LSGGMQQRLALA 152
Cdd:PRK10636 92 RQLE--------AQLHDANERndghaiATIHGKL--DAIDawtirsRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517136998 153 QALIMKPKVLLLDEPFGALDpgIRAEIhtLMKRLWNETQMTVVMVTHD 200
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD--LDAVI--WLEKWLKSYQGTLILISHD 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-197 |
3.31e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 1 MSELIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQerptrgTILLDGEplpaepgpdrgvvfq 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGE------LPLLSGE--------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLLGKeLMASKYK----------AKLFGQARRSAI-----DEAR--QLITEVGLSGAETKYPAQLSG 143
Cdd:PRK10938 60 RQSQFSHITRLSFEQLQK-LVSDEWQrnntdmlspgEDDTGRTTAEIIqdevkDPARceQLAQQFGITALLDRRFKYLST 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517136998 144 GMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLwNETQMTVVMV 197
Cdd:PRK10938 139 GETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL-HQSGITLVLV 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-199 |
3.70e-09 |
|
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: 54.94 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGqeRPTRGTI----LLDGEPLPAEPGPDRGVVFQRYSVFPHLTVlgnv 94
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVItgeiLINGRPLDKNFQRSTGYVEQQDVHSPNLTV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 95 llgkelmaskYKAKLFGQARRsaidearqlitevGLSGAETKypaqlsggmqqRLALAQALIMKPKVLLLDEPFGALDPG 174
Cdd:cd03232 97 ----------REALRFSALLR-------------GLSVEQRK-----------RLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|....*
gi 517136998 175 IRAEIHTLMKRLWNETQmTVVMVTH 199
Cdd:cd03232 143 AAYNIVRFLKKLADSGQ-AILCTIH 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-199 |
4.36e-09 |
|
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: 57.23 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLgQERPTRGTILLDGEPLPAepgpdrgVVFQR----YSVFPHLTVLgn 93
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNS-------VTLQTwrkaFGVIPQKVFI-- 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 vllgkelMASKYKAKLFGQARRSAiDEARQLITEVGLSGAETKYPAQL-----------SGGMQQRLALAQALIMKPKVL 162
Cdd:TIGR01271 1304 -------FSGTFRKNLDPYEQWSD-EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190
....*....|....*....|....*....|....*..
gi 517136998 163 LLDEPFGALDPGIRAEIHTLMKRLWNETqmTVVMVTH 199
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNC--TVILSEH 1410
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-172 |
1.21e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 10 WKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGT-ILLDGEPLPAepgPDRGVVFqrysvfpHL 88
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRGSVAYV---PQVSWIF-------NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TVLGNVLLGKELMASKYKAKLFGQARRSAID--EARQLiTEVGLSGAetkypaQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PLN03232 694 TVRENILFGSDFESERYWRAIDVTALQHDLDllPGRDL-TEIGERGV------NISGGQKQRVSMARAVYSNSDIYIFDD 766
|
....*.
gi 517136998 167 PFGALD 172
Cdd:PLN03232 767 PLSALD 772
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-204 |
1.25e-08 |
|
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: 54.48 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGeplpaepgpdrgvvfqRYSVFPHL------TVL 91
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------------RISFSSQFswimpgTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 GNVLLGKELMASKYKAklfgqarrsaIDEARQLITEVglsgaeTKYPAQ-----------LSGGMQQRLALAQALIMKPK 160
Cdd:cd03291 116 ENIIFGVSYDEYRYKS----------VVKACQLEEDI------TKFPEKdntvlgeggitLSGGQRARISLARAVYKDAD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517136998 161 VLLLDEPFGALDPGIRAEI--HTLMKRLWNETQMTVVMVTHDMREA 204
Cdd:cd03291 180 LYLLDSPFGYLDVFTEKEIfeSCVCKLMANKTRILVTSKMEHLKKA 225
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-201 |
2.87e-08 |
|
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: 53.52 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 32 VALVGPSGCGKSTFLRMLLGQERPTRGTilldgepLPAEPGPD------RGVVFQRY-----------SVFPHL------ 88
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGK-------FDDPPDWDeildefRGSELQNYftkllegdvkvIVKPQYvdlipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 TVLGNVLlgkELMASKYKaklfgqarRSAIDEarqLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:cd03236 102 AVKGKVG---ELLKKKDE--------RGKLDE---LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 517136998 169 GALDPGIRAEIHTLMKRLwNETQMTVVMVTHDM 201
Cdd:cd03236 168 SYLDIKQRLNAARLIREL-AEDDNYVLVVEHDL 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-200 |
4.59e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 4 LIIDSVWKEYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDG------------EPLPAEP 71
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiklgyfaqhqlEFLRADE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 72 GPdrgvvfqrysvFPHLTVLgnvllgkelmaskykaklfgqARRSAIDEARQLITEVGLSGAE-TKYPAQLSGGMQQRLA 150
Cdd:PRK10636 393 SP-----------LQHLARL---------------------APQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLV 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517136998 151 LAQALIMKPKVLLLDEPFGALDPGIRaeiHTLMKRLWnETQMTVVMVTHD 200
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMR---QALTEALI-DFEGALVVVSHD 486
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-199 |
6.13e-08 |
|
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: 53.21 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 16 QIVLENVSLTVASRAFVALVGPSGCGKSTFLRmLLGQERPTRGTILLDGEP-----LPAEPGPDRGVvFQRYSVFPHltv 90
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKPAKgklfyVPQRPYMTLGT-LRDQIIYPD--- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 91 lgnvllGKELMaskyKAKLFGQARRSAIDEARQL----ITEVGLSgAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:TIGR00954 540 ------SSEDM----KRRGLSDKDLEQILDNVQLthilEREGGWS-AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 517136998 167 PFGALDPgiraEIHTLMKRLWNETQMTVVMVTH 199
Cdd:TIGR00954 609 CTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-196 |
6.95e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.49 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQ----ERPTrGTILLDGEP-LPAEPGPDRGVVF--QRYSVFPHLTVl 91
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPyKEFAEKYPGEIIYvsEEDVHFPTLTV- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 92 gnvllgKELMasKYKAKLFGQARrsaidearqlitevgLSGaetkypaqLSGGMQQRLALAQALIMKPKVLLLDEPFGAL 171
Cdd:cd03233 101 ------RETL--DFALRCKGNEF---------------VRG--------ISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180
....*....|....*....|....*
gi 517136998 172 DPGIRAEIHTLMKRLWNETQMTVVM 196
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFV 174
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-218 |
1.96e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 16 QIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILldgeplpAEpgpdRGVVF--QRYSVFpHLTVLGN 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AE----RSIAYvpQQAWIM-NATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 94 VLLGKELMAskykAKLFGQARRSAID-EARQLI----TEVGLSGAetkypaQLSGGMQQRLALAQALIMKPKVLLLDEPF 168
Cdd:PTZ00243 741 ILFFDEEDA----ARLADAVRVSQLEaDLAQLGggleTEIGEKGV------NLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517136998 169 GALDP--GIRAEIHTLMKRLWNETQmtvVMVTHDMrEAFTLATRVVAFERPR 218
Cdd:PTZ00243 811 SALDAhvGERVVEECFLGALAGKTR---VLATHQV-HVVPRADYVVALGDGR 858
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-173 |
5.15e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 12 EYGDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRM--------------LLGQERPTRGTILldgeplpaEPGPDRGV 77
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndltLFGRRRGSGETIW--------DIKKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 78 VfqrySVFPHL-----TVLGNVLL-------GKELMASKYKAKLfgqarrsaideARQLITEVGLSGAETKYPAQ-LSGG 144
Cdd:PRK10938 341 V----SSSLHLdyrvsTSVRNVILsgffdsiGIYQAVSDRQQKL-----------AQQWLDILGIDKRTADAPFHsLSWG 405
|
170 180 190
....*....|....*....|....*....|
gi 517136998 145 mQQRLAL-AQALIMKPKVLLLDEPFGALDP 173
Cdd:PRK10938 406 -QQRLALiVRALVKHPTLLILDEPLQGLDP 434
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-202 |
5.98e-07 |
|
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: 48.47 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRgtiLLDGEPLPaepgpdrgvvfqrysvFPHLTVlgnvllgk 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKAR---LISFLPKF----------------SRNKLI-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 99 elmaskykaklfgqarrsAIDEARQLItEVGLSGAETKYPAQ-LSGGMQQRLALAQALIMKPK--VLLLDEPFGALDPGI 175
Cdd:cd03238 64 ------------------FIDQLQFLI-DVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180
....*....|....*....|....*..
gi 517136998 176 RAEIHTLMKRLWNETQmTVVMVTHDMR 202
Cdd:cd03238 125 INQLLEVIKGLIDLGN-TVILIEHNLD 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-195 |
6.45e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDrgvVFQRYSVFPHLTVL--GNVL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRRVLSIIPQSPVLfsGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 96 LGKELMASKYKAKLFGQARRSAIDEARQLiTEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGI 175
Cdd:PLN03232 1328 FNIDPFSEHNDADLWEALERAHIKDVIDR-NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406
|
170 180
....*....|....*....|
gi 517136998 176 RAEIHTLMKRLWNETQMTVV 195
Cdd:PLN03232 1407 DSLIQRTIREEFKSCTMLVI 1426
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-166 |
6.63e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPDRGVVFQRYSVFPHLTVLGNV 94
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 95 llgkelmasKYKAKLFGQArrSAIDEArqlITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDE 166
Cdd:PRK13541 92 ---------KFWSEIYNSA--ETLYAA---IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-228 |
7.30e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDG---------------------EPLPAEPGP 73
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwrskigvvsqDPLLFSNSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 74 DRGVVFQRYSV-------------------------------FPHLTVLGNVLLGKELMASKYKAKLFGQArrSAIDEAR 122
Cdd:PTZ00265 477 KNNIKYSLYSLkdlealsnyynedgndsqenknkrnscrakcAGDLNDMSNTTDSNELIEMRKNYQTIKDS--EVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 123 QLITEVGLSGAETKY-------PAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRL-WNETQMTV 194
Cdd:PTZ00265 555 KVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITI 634
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 517136998 195 VmVTHDM--------------REAFTLATRVVAFERP-RDRPEEKERYG 228
Cdd:PTZ00265 635 I-IAHRLstiryantifvlsnRERGSTVDVDIIGEDPtKDNKENNNKNN 682
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-203 |
8.04e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 15 DQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQE--RPTRGTILLDGEPLP------------AEPGPDRgvvfQ 80
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDvstvsdaidaglAYVTEDR----K 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 81 RYSVFPHLTVLGNVLLgkelmaskykAKLFGQARRSAIDEARQliTEVglsgAE-------TKYP------AQLSGGMQQ 147
Cdd:NF040905 348 GYGLNLIDDIKRNITL----------ANLGKVSRRGVIDENEE--IKV----AEeyrkkmnIKTPsvfqkvGNLSGGNQQ 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 148 RLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETqMTVVMVTHDMRE 203
Cdd:NF040905 412 KVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEG-KGVIVISSELPE 466
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-212 |
1.20e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.20e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517136998 141 LSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNETQmTVVMVTHDMREAFTLATRVV 212
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRIL 462
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-201 |
1.25e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 32 VALVGPSGCGKSTFLRMLLGQERPTRGTilldgepLPAEPGPDRgvVFQRYSVfphlTVLGNVLlgKELMASKYKA---- 107
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGD-------YEEEPSWDE--VLKRFRG----TELQNYF--KKLYNGEIKVvhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 108 -------KLF-GQARR--SAIDE---ARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPG 174
Cdd:PRK13409 167 qyvdlipKVFkGKVREllKKVDErgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180
....*....|....*....|....*..
gi 517136998 175 IRAEIHTLMKRLWNETqmTVVMVTHDM 201
Cdd:PRK13409 247 QRLNVARLIRELAEGK--YVLVVEHDL 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
114-199 |
1.26e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 114 RRSAID----EARQLITEVGLS---GAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDpgiraeIHTLmkrL 186
Cdd:PLN03073 311 RLELIDaytaEARAASILAGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD------LHAV---L 381
|
90
....*....|....*...
gi 517136998 187 WNETQM-----TVVMVTH 199
Cdd:PLN03073 382 WLETYLlkwpkTFIVVSH 399
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-200 |
1.37e-06 |
|
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: 47.99 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 31 FVALVGPSGCGKSTFLRMLL----GQERPTrgTILLDGEPLPAEPGPDRGVVfqrYSVFPHLTvlgnvllGKELMASKYK 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltGELPPN--SKGGAHDPKLIREGEVRAQV---KLAFENAN-------GKKYTITRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 107 AKLfgqarRSAI----DEARQLITEVglsgaetkyPAQLSGGmQQ-------RLALAQALIMKPKVLLLDEPFGALDPG- 174
Cdd:cd03240 92 AIL-----ENVIfchqGESNWPLLDM---------RGRCSGG-EKvlasliiRLALAETFGSNCGILALDEPTTNLDEEn 156
|
170 180
....*....|....*....|....*.
gi 517136998 175 IRAEIHTLMKRLWNETQMTVVMVTHD 200
Cdd:cd03240 157 IEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-205 |
6.77e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 33 ALVGPSGCGKSTFLRMLLGqeRPTRGTIllDGEpLPAEPGPDRGVVFQRYSVF--------PHLTVLGNVL------LGK 98
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGGYI--EGD-IRISGFPKKQETFARISGYceqndihsPQVTVRESLIysaflrLPK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 99 ELmaSKYKAKLFgqarrsaIDEARQLITEVGLSGAETKYPA--QLSGGMQQRLALAQALIMKPKVLLLDEPFGALDPGIR 176
Cdd:PLN03140 985 EV--SKEEKMMF-------VDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
170 180 190
....*....|....*....|....*....|....*
gi 517136998 177 AeihTLMKRLWN--ETQMTVVMVTH----DMREAF 205
Cdd:PLN03140 1056 A---IVMRTVRNtvDTGRTVVCTIHqpsiDIFEAF 1087
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-215 |
1.91e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEplpaepgpdrgvvfqrYSVFPHLTVLGNVLLGK 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 99 ELMasKYKAKLFGQARRSaIDEARQLITEVGLSGAETKYPAQ-LSGGMQQRLALAQALIMKPKVLLLDEpfgALDPGIRA 177
Cdd:PRK13546 104 ENI--EFKMLCMGFKRKE-IKAMTPKIIEFSELGEFIYQPVKkYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517136998 178 EIHTLMKRL--WNETQMTVVMVTHDMREAFTLATRVVAFE 215
Cdd:PRK13546 178 FAQKCLDKIyeFKEQNKTIFFVSHNLGQVRQFCTKIAWIE 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-179 |
2.23e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 18 VLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEPLPAEPGPD-RGVVfqrySVFPHLTVL--GNV 94
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlRKVL----GIIPQAPVLfsGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 95 LLGKELMASKYKAKLFGQARRSAI-DEARQliTEVGLSGAETKYPAQLSGGMQQRLALAQALIMKPKVLLLDEPFGALDP 173
Cdd:PLN03130 1330 RFNLDPFNEHNDADLWESLERAHLkDVIRR--NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
....*.
gi 517136998 174 GIRAEI 179
Cdd:PLN03130 1408 RTDALI 1413
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-212 |
4.08e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 19 LENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQERPTRGTILLDGEplPAEPGPDRGVVFQrysvfphLTVLGNVLLgK 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--AALIAISSGLNGQ-------LTGIENIEL-K 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 99 ELMASKYKAKlfgqarrsaIDEARQLITEVGLSGAETKYPAQ-LSGGMQQRLALAQALIMKPKVLLLDEpfgALDPGIRA 177
Cdd:PRK13545 110 GLMMGLTKEK---------IKEIIPEIIEFADIGKFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQT 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 517136998 178 EIHTLMKRL--WNETQMTVVMVTHDMREAFTLATRVV 212
Cdd:PRK13545 178 FTKKCLDKMneFKEQGKTIFFISHSLSQVKSFCTKAL 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-202 |
4.87e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 14 GDQIVLENVSLTVASRAFVALVGPSGCGKSTFLRMLLGQerP----TRGTILLDGEP---LPAEPGPDRGV--VFQrysv 84
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGESildLEPEERAHLGIflAFQ---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 85 FPhLTVLGnVLLGKELMAS-KYKAKLFGQARRSAIdEARQLITE----VGLSgaetkyPAQL--------SGGMQQRLAL 151
Cdd:CHL00131 92 YP-IEIPG-VSNADFLRLAyNSKRKFQGLPELDPL-EFLEIINEklklVGMD------PSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517136998 152 AQALIMKPKVLLLDEPFGALD----PGIRAEIHTLMKrlwneTQMTVVMVTHDMR 202
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDidalKIIAEGINKLMT-----SENSIILITHYQR 212
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
138-200 |
1.13e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517136998 138 PAQLSGGMQQRLALAQALI---MKPKVLLLDEPFGALDPGIRAEIHTLMKRLWNE-TQmtVVMVTHD 200
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgAQ--LILTTHS 298
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
28-200 |
4.65e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 28 SRAFVALVGPSGCGKSTFL---RMLLGQERPTRGTILLDgeplPAEPGPDRG---VVF----QRYSV---------FPHL 88
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILeaiRYALYGKARSRSKLRSD----LINVGSEEAsveLEFehggKRYRIerrqgefaeFLEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 89 T------VLGNVL---LGKELMASKYKAKLFGQARRSAIDEARQLITEVGLSGAETKYPAQLSGGMQQRLALAQALimkp 159
Cdd:COG0419 98 KpserkeALKRLLgleIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLL---- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517136998 160 kVLLLDepFGALDPGIRAEIHTLMKRLwnetqmtvVMVTHD 200
Cdd:COG0419 174 -SLILD--FGSLDEERLERLLDALEEL--------AIITHV 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-200 |
5.74e-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: 39.65 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 17 IVLENVSLTVASRAFVALVGPSGCGKSTFLRmllgqerptrgTILLdgeplpaepgpdrgvvfqrysvfphltvlgnVLL 96
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILD-----------AIGL-------------------------------ALG 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 97 GKelMASKYKAKLFGQARRSAIDEArQLITEVGlsgaetkypaQLSGGMQQRLALAQALI---MKPKVL-LLDEPFGALD 172
Cdd:cd03227 47 GA--QSATRRRSGVKAGCIVAAVSA-ELIFTRL----------QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLD 113
|
170 180
....*....|....*....|....*...
gi 517136998 173 PGIRAEIHTLMKRLWNEtQMTVVMVTHD 200
Cdd:cd03227 114 PRDGQALAEAILEHLVK-GAQVIVITHL 140
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
29-52 |
2.45e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.62 E-value: 2.45e-03
10 20
....*....|....*....|....
gi 517136998 29 RAFVALVGPSGCGKSTFLRMLLGQ 52
Cdd:COG3267 43 GGFVVLTGEVGTGKTTLLRRLLER 66
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-201 |
3.30e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 3.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517136998 141 LSGGMQQRLALAQALIM---KPKVLLLDEPFGALDPgirAEIHTLMKRLWNETQM--TVVMVTHDM 201
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHT---HDIKALIYVLQSLTHQghTVVIIEHNM 872
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
102-204 |
3.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517136998 102 ASKYKAKLF-GQARRSAIDEARQLITEVGlSGaETKYPAQLSGG-MQQ-----RLALAQALIMKPKVLLLDEPFGALDPG 174
Cdd:COG4717 521 ASEYFSRLTdGRYRLIRIDEDLSLKVDTE-DG-RTRPVEELSRGtREQlylalRLALAELLAGEPLPLILDDAFVNFDDE 598
|
90 100 110
....*....|....*....|....*....|
gi 517136998 175 IRAEIHTLMKRLWNETQmtVVMVTHDMREA 204
Cdd:COG4717 599 RLRAALELLAELAKGRQ--VIYFTCHEELV 626
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
32-64 |
4.07e-03 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 38.07 E-value: 4.07e-03
10 20 30
....*....|....*....|....*....|....*.
gi 517136998 32 VALVGPSGCGKSTFLR---MLLGQERPTrgTILLDG 64
Cdd:PRK07429 11 LGVAGDSGCGKTTFLRglaDLLGEELVT--VICTDD 44
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
32-60 |
6.66e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.61 E-value: 6.66e-03
10 20
....*....|....*....|....*....
gi 517136998 32 VALVGPSGCGKSTFLRMLLGQERPTRGTI 60
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
33-60 |
6.68e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 36.28 E-value: 6.68e-03
10 20
....*....|....*....|....*...
gi 517136998 33 ALVGPSGCGKSTFLRMLLGQERPTRGTI 60
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEVSDV 28
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